MC <p>03ff</p> <p>Which one of the following statements is<strong> <span style="color: #ba372a;"><strong>FALSE</strong></span> </strong> about Michaelis-Menten kinetics?</p> A.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the change in <strong><span style="color: #ff0000;">concentration</span></strong> of <strong><span style="color: #2fbd0f;">enzyme-substrate complex [ES]</span></strong> does<strong> <strong>NOT</strong> </strong>change. Incorrect B.<strong> </strong>When the substrate <strong><span style="color: #ff0000;">concentration</span></strong>, [S], is much smaller than K<sub>M</sub>, the <strong><span style="color: #a1005e;">reaction rate</span></strong> is linear. Incorrect C.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> does<strong> <strong>NOT</strong> </strong>apply to allosteric enzymes. Incorrect D.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> was developed by German biochemist Leonor Michaelis and Canadian physician Maud Menten in 1913. Incorrect E.<strong> </strong><strong><span style="color: #0d57a5;"><strong><span style="color: #0d57a5;">M-M kinetics</span></strong></span></strong> assumes that the <strong><span style="color: #2fbd0f;"><strong><span style="color: #2fbd0f;">enzyme-substrate complex [ES]</span></strong></span></strong> is short lived and does<strong> <strong>NOT</strong> </strong>contribute to the <strong><span style="color: #a1005e;"><strong><span style="color: #a1005e;">reaction rate</span></strong></span></strong>. Correct MC <p>0662</p> <p>Which one of the following statements is<strong> <span style="color: #ba372a;"><strong>FALSE</strong></span> </strong> about Michaelis-Menten kinetics?</p> A.<strong> </strong>When the substrate <strong><span style="color: #ff0000;"><strong><span style="color: #ff0000;">concentration</span></strong></span></strong>, [S], is much larger than K<sub>M</sub>, the <strong><span style="color: #a1005e;"><strong><span style="color: #a1005e;">reaction rate</span></strong></span></strong> is linear. Correct B.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the product is<strong> <strong>NOT</strong> </strong>available and there is no measureable reverse <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect C.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> does<strong> <strong>NOT</strong> </strong>apply to allosteric enzymes. Incorrect D.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the enzyme bound to the product [EP] is short lived and does<strong> <strong>NOT</strong> </strong>contribute to the <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect E.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> was developed by German biochemist Leonor Michaelis and Canadian physician Maud Menten in 1913. Incorrect MC <p>118a</p> <p>Which one of the following statements is<strong> <span style="color: #169179;"><strong>TRUE</strong></span> </strong> of Michaelis-Menten kinetics?</p> A.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the enzyme bound to the substrate [ES] is short lived and does<strong> <strong>NOT</strong> </strong>contribute to the <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect B.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> was developed by American linguist Laura Michaelis and Belgian cyclist Milan Menten in 1913. Incorrect C.<strong> </strong>The <strong><span style="color: #a1005e;"><strong><span style="color: #a1005e;">reaction rate</span></strong></span></strong> is <strong><span style="color: #009e4c;"><i><strong><span style="color: #009e4c;"><i>proportional</i></span></strong></i></span></strong> to the substrate <strong><span style="color: #ff0000;"><strong><span style="color: #ff0000;">concentration</span></strong></span></strong>. Correct D.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the <strong><span style="color: #ff0000;">concentration</span></strong> of <strong><span style="color: #ff5e00;">enzyme-product complex [EP]</span></strong> is <strong><span style="color: #6d108e;"><i>constant</i></span></strong>. Incorrect E.<strong> </strong>When the substrate <strong><span style="color: #ff0000;">concentration</span></strong>, [S], is much larger than K<sub>M</sub>, the <strong><span style="color: #a1005e;">reaction rate</span></strong> is linear. Incorrect MC <p>1199</p> <p>Which one of the following statements is<strong> <span style="color: #169179;"><strong>TRUE</strong></span> </strong> of Michaelis-Menten kinetics?</p> A.<strong> </strong>When the substrate <strong><span style="color: #ff0000;">concentration</span></strong>, [S], is much smaller than K<sub>M</sub>, the <strong><span style="color: #a1005e;">reaction rate</span></strong> is <strong><span style="color: #6d108e;"><i>constant</i></span></strong>. Incorrect B.<strong> </strong><strong><span style="color: #0d57a5;"><strong><span style="color: #0d57a5;">M-M kinetics</span></strong></span></strong> was developed by German biochemist Leonor Michaelis and Canadian physician Maud Menten in 1913. Correct C.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the change in <strong><span style="color: #ff0000;">concentration</span></strong> of <strong><span style="color: #ff5e00;">enzyme-product complex [EP]</span></strong> does<strong> <strong>NOT</strong> </strong>change. Incorrect D.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the substrate is<strong> <strong>NOT</strong> </strong>available and there is no measureable reverse <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect E.<strong> </strong>The <strong><span style="color: #a1005e;">reaction rate</span></strong> is <strong><span style="color: #009e4c;"><i>proportional</i></span></strong> to the product <strong><span style="color: #ff0000;">concentration</span></strong>. Incorrect MC <p>1218</p> <p>Which one of the following statements is<strong> <span style="color: #ba372a;"><strong>FALSE</strong></span> </strong> concerning Michaelis-Menten kinetics?</p> A.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the product is<strong> <strong>NOT</strong> </strong>available and there is no measureable reverse <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect B.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the change in <strong><span style="color: #ff0000;">concentration</span></strong> of <strong><span style="color: #2fbd0f;">enzyme-substrate complex [ES]</span></strong> does<strong> <strong>NOT</strong> </strong>change. Incorrect C.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the enzyme bound to the product [EP] is short lived and does<strong> <strong>NOT</strong> </strong>contribute to the <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect D.<strong> </strong>The <strong><span style="color: #a1005e;">reaction rate</span></strong> is <strong><span style="color: #009e4c;"><i>proportional</i></span></strong> to the substrate <strong><span style="color: #ff0000;">concentration</span></strong>. Incorrect E.<strong> </strong>When the substrate <strong><span style="color: #ff0000;"><strong><span style="color: #ff0000;">concentration</span></strong></span></strong>, [S], is much larger than K<sub>M</sub>, the <strong><span style="color: #a1005e;"><strong><span style="color: #a1005e;">reaction rate</span></strong></span></strong> is linear. Correct MC <p>14f8</p> <p>Which one of the following statements is<strong> <span style="color: #169179;"><strong>TRUE</strong></span> </strong> of Michaelis-Menten kinetics?</p> A.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the rate of breaking the <strong><span style="color: #ff5e00;">enzyme-product complex [EP]</span></strong> is equal to the rate of its formation. Incorrect B.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> was developed by Greek economist Leo Michelis and Dutch bobsledder Hubert Menten in 1913. Incorrect C.<strong> </strong>When the substrate <strong><span style="color: #ff0000;">concentration</span></strong>, [S], is much larger than K<sub>M</sub>, the <strong><span style="color: #a1005e;">reaction rate</span></strong> is linear. Incorrect D.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the enzyme bound to the substrate [ES] is short lived and does<strong> <strong>NOT</strong> </strong>contribute to the <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect E.<strong> </strong><strong><span style="color: #0d57a5;"><strong><span style="color: #0d57a5;">M-M kinetics</span></strong></span></strong> does<strong> <strong>NOT</strong> </strong>apply to allosteric enzymes. Correct MC <p>1554</p> <p>Which one of the following statements is<strong> <span style="color: #ba372a;"><strong>FALSE</strong></span> </strong> concerning Michaelis-Menten kinetics?</p> A.<strong> </strong><strong><span style="color: #0d57a5;"><strong><span style="color: #0d57a5;">M-M kinetics</span></strong></span></strong> assumes that there is no substrate available and there is no measureable reverse <strong><span style="color: #a1005e;"><strong><span style="color: #a1005e;">reaction rate</span></strong></span></strong>. Correct B.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> was developed by German biochemist Leonor Michaelis and Canadian physician Maud Menten in 1913. Incorrect C.<strong> </strong>When the substrate <strong><span style="color: #ff0000;">concentration</span></strong>, [S], is much larger than K<sub>M</sub>, the <strong><span style="color: #a1005e;">reaction rate</span></strong> is <strong><span style="color: #6d108e;"><i>constant</i></span></strong>. Incorrect D.<strong> </strong>The <strong><span style="color: #a1005e;">reaction rate</span></strong> is <strong><span style="color: #009e4c;"><i>proportional</i></span></strong> to the substrate <strong><span style="color: #ff0000;">concentration</span></strong>. Incorrect E.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> does<strong> <strong>NOT</strong> </strong>apply to allosteric enzymes. Incorrect MC <p>17d8</p> <p>Which one of the following statements is<strong> <span style="color: #169179;"><strong>TRUE</strong></span> </strong> regarding Michaelis-Menten kinetics?</p> A.<strong> </strong><strong><span style="color: #0d57a5;"><strong><span style="color: #0d57a5;">M-M kinetics</span></strong></span></strong> assumes that there is no product available and there is no measureable reverse <strong><span style="color: #a1005e;"><strong><span style="color: #a1005e;">reaction rate</span></strong></span></strong>. Correct B.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the change in <strong><span style="color: #ff0000;">concentration</span></strong> of <strong><span style="color: #ff5e00;">enzyme-product complex [EP]</span></strong> does<strong> <strong>NOT</strong> </strong>change. Incorrect C.<strong> </strong>The <strong><span style="color: #a1005e;">reaction rate</span></strong> is <strong><span style="color: #009e4c;"><i>proportional</i></span></strong> to the product <strong><span style="color: #ff0000;">concentration</span></strong>. Incorrect D.<strong> </strong>When the substrate <strong><span style="color: #ff0000;">concentration</span></strong>, [S], is much smaller than K<sub>M</sub>, the <strong><span style="color: #a1005e;">reaction rate</span></strong> is <strong><span style="color: #6d108e;"><i>constant</i></span></strong>. Incorrect E.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the <strong><span style="color: #2fbd0f;">enzyme-substrate complex [ES]</span></strong> is short lived and does<strong> <strong>NOT</strong> </strong>contribute to the <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect MC <p>18df</p> <p>Which one of the following statements is<strong> <span style="color: #169179;"><strong>TRUE</strong></span> </strong> regarding Michaelis-Menten kinetics?</p> A.<strong> </strong>The <strong><span style="color: #a1005e;">reaction rate</span></strong> is <strong><span style="color: #009e4c;"><i>proportional</i></span></strong> to the product <strong><span style="color: #ff0000;">concentration</span></strong>. Incorrect B.<strong> </strong>When the substrate <strong><span style="color: #ff0000;">concentration</span></strong>, [S], is much smaller than K<sub>M</sub>, the <strong><span style="color: #a1005e;">reaction rate</span></strong> is <strong><span style="color: #6d108e;"><i>constant</i></span></strong>. Incorrect C.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> was developed by Greek economist Leo Michelis and Dutch bobsledder Hubert Menten in 1913. Incorrect D.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the substrate is<strong> <strong>NOT</strong> </strong>available and there is no measureable reverse <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect E.<strong> </strong><strong><span style="color: #0d57a5;"><strong><span style="color: #0d57a5;">M-M kinetics</span></strong></span></strong> assumes a quasi-steady state, that the <strong><span style="color: #2fbd0f;"><strong><span style="color: #2fbd0f;">enzyme-substrate complex [ES]</span></strong></span></strong> is <strong><span style="color: #6d108e;"><i><strong><span style="color: #6d108e;"><i>constant</i></span></strong></i></span></strong>. Correct MC <p>1a33</p> <p>Which one of the following statements is<strong> <span style="color: #169179;"><strong>TRUE</strong></span> </strong> regarding Michaelis-Menten kinetics?</p> A.<strong> </strong><strong><span style="color: #0d57a5;"><strong><span style="color: #0d57a5;">M-M kinetics</span></strong></span></strong> was developed by German biochemist Leonor Michaelis and Canadian physician Maud Menten in 1913. Correct B.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the <strong><span style="color: #ff0000;">concentration</span></strong> of <strong><span style="color: #ff5e00;">enzyme-product complex [EP]</span></strong> is <strong><span style="color: #6d108e;"><i>constant</i></span></strong>. Incorrect C.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the substrate is<strong> <strong>NOT</strong> </strong>available and there is no measureable reverse <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect D.<strong> </strong>The <strong><span style="color: #a1005e;">reaction rate</span></strong> is <strong><span style="color: #009e4c;"><i>proportional</i></span></strong> to the product <strong><span style="color: #ff0000;">concentration</span></strong>. Incorrect E.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the enzyme bound to the substrate [ES] is short lived and does<strong> <strong>NOT</strong> </strong>contribute to the <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect MC <p>1e09</p> <p>Which one of the following statements is<strong> <span style="color: #169179;"><strong>TRUE</strong></span> </strong> regarding Michaelis-Menten kinetics?</p> A.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the <strong><span style="color: #ff0000;">concentration</span></strong> of <strong><span style="color: #ff5e00;">enzyme-product complex [EP]</span></strong> is <strong><span style="color: #6d108e;"><i>constant</i></span></strong>. Incorrect B.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> was developed by Greek economist Leo Michelis and Dutch bobsledder Hubert Menten in 1913. Incorrect C.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the enzyme bound to the substrate [ES] is short lived and does<strong> <strong>NOT</strong> </strong>contribute to the <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect D.<strong> </strong>The <strong><span style="color: #a1005e;">reaction rate</span></strong> is <strong><span style="color: #009e4c;"><i>proportional</i></span></strong> to the product <strong><span style="color: #ff0000;">concentration</span></strong>. Incorrect E.<strong> </strong>When the substrate <strong><span style="color: #ff0000;"><strong><span style="color: #ff0000;">concentration</span></strong></span></strong>, [S], is much smaller than K<sub>M</sub>, the <strong><span style="color: #a1005e;"><strong><span style="color: #a1005e;">reaction rate</span></strong></span></strong> is linear. Correct MC <p>1fe2</p> <p>Which one of the following statements is<strong> <span style="color: #169179;"><strong>TRUE</strong></span> </strong> regarding Michaelis-Menten kinetics?</p> A.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> was developed by American linguist Laura Michaelis and Belgian cyclist Milan Menten in 1913. Incorrect B.<strong> </strong>The <strong><span style="color: #a1005e;">reaction rate</span></strong> is <strong><span style="color: #009e4c;"><i>proportional</i></span></strong> to the product <strong><span style="color: #ff0000;">concentration</span></strong>. Incorrect C.<strong> </strong>When the substrate <strong><span style="color: #ff0000;">concentration</span></strong>, [S], is much larger than K<sub>M</sub>, the <strong><span style="color: #a1005e;">reaction rate</span></strong> is linear. Incorrect D.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that there is no substrate available and there is no measureable reverse <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect E.<strong> </strong><strong><span style="color: #0d57a5;"><strong><span style="color: #0d57a5;">M-M kinetics</span></strong></span></strong> assumes that the enzyme bound to the product [EP] is short lived and does<strong> <strong>NOT</strong> </strong>contribute to the <strong><span style="color: #a1005e;"><strong><span style="color: #a1005e;">reaction rate</span></strong></span></strong>. Correct MC <p>251f</p> <p>Which one of the following statements is<strong> <span style="color: #ba372a;"><strong>FALSE</strong></span> </strong> concerning Michaelis-Menten kinetics?</p> A.<strong> </strong>The <strong><span style="color: #a1005e;">reaction rate</span></strong> is <strong><span style="color: #009e4c;"><i>proportional</i></span></strong> to the substrate <strong><span style="color: #ff0000;">concentration</span></strong>. Incorrect B.<strong> </strong>When the substrate <strong><span style="color: #ff0000;"><strong><span style="color: #ff0000;">concentration</span></strong></span></strong>, [S], is much larger than K<sub>M</sub>, the <strong><span style="color: #a1005e;"><strong><span style="color: #a1005e;">reaction rate</span></strong></span></strong> is linear. Correct C.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> was developed by German biochemist Leonor Michaelis and Canadian physician Maud Menten in 1913. Incorrect D.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that there is no product available and there is no measureable reverse <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect E.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the <strong><span style="color: #ff5e00;">enzyme-product complex [EP]</span></strong> is short lived and does<strong> <strong>NOT</strong> </strong>contribute to the <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect MC <p>25df</p> <p>Which one of the following statements is<strong> <span style="color: #169179;"><strong>TRUE</strong></span> </strong> of Michaelis-Menten kinetics?</p> A.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the <strong><span style="color: #ff5e00;">enzyme-product complex [EP]</span></strong> is <strong><span style="color: #6d108e;"><i>constant</i></span></strong>. Incorrect B.<strong> </strong>The <strong><span style="color: #a1005e;">reaction rate</span></strong> is <strong><span style="color: #009e4c;"><i>proportional</i></span></strong> to the product <strong><span style="color: #ff0000;">concentration</span></strong>. Incorrect C.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the substrate is<strong> <strong>NOT</strong> </strong>available and there is no measureable reverse <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect D.<strong> </strong><strong><span style="color: #0d57a5;"><strong><span style="color: #0d57a5;">M-M kinetics</span></strong></span></strong> does<strong> <strong>NOT</strong> </strong>apply to allosteric enzymes. Correct E.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> was developed by Greek economist Leo Michelis and Dutch bobsledder Hubert Menten in 1913. Incorrect MC <p>27d6</p> <p>Which one of the following statements is<strong> <span style="color: #169179;"><strong>TRUE</strong></span> </strong> of Michaelis-Menten kinetics?</p> A.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the change in <strong><span style="color: #ff0000;">concentration</span></strong> of <strong><span style="color: #ff5e00;">enzyme-product complex [EP]</span></strong> does<strong> <strong>NOT</strong> </strong>change. Incorrect B.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> was developed by Greek economist Leo Michelis and Dutch bobsledder Hubert Menten in 1913. Incorrect C.<strong> </strong>The <strong><span style="color: #a1005e;"><strong><span style="color: #a1005e;">reaction rate</span></strong></span></strong> is <strong><span style="color: #009e4c;"><i><strong><span style="color: #009e4c;"><i>proportional</i></span></strong></i></span></strong> to the substrate <strong><span style="color: #ff0000;"><strong><span style="color: #ff0000;">concentration</span></strong></span></strong>. Correct D.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the substrate is<strong> <strong>NOT</strong> </strong>available and there is no measureable reverse <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect E.<strong> </strong>When the substrate <strong><span style="color: #ff0000;">concentration</span></strong>, [S], is much larger than K<sub>M</sub>, the <strong><span style="color: #a1005e;">reaction rate</span></strong> is linear. Incorrect MC <p>288a</p> <p>Which one of the following statements is<strong> <span style="color: #ba372a;"><strong>FALSE</strong></span> </strong> about Michaelis-Menten kinetics?</p> A.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the <strong><span style="color: #ff0000;">concentration</span></strong> of <strong><span style="color: #2fbd0f;">enzyme-substrate complex [ES]</span></strong> is <strong><span style="color: #6d108e;"><i>constant</i></span></strong>. Incorrect B.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that there is no product available and there is no measureable reverse <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect C.<strong> </strong>The <strong><span style="color: #a1005e;">reaction rate</span></strong> is <strong><span style="color: #009e4c;"><i>proportional</i></span></strong> to the substrate <strong><span style="color: #ff0000;">concentration</span></strong>. Incorrect D.<strong> </strong>When the substrate <strong><span style="color: #ff0000;">concentration</span></strong>, [S], is much smaller than K<sub>M</sub>, the <strong><span style="color: #a1005e;">reaction rate</span></strong> is linear. Incorrect E.<strong> </strong><strong><span style="color: #0d57a5;"><strong><span style="color: #0d57a5;">M-M kinetics</span></strong></span></strong> was developed by American linguist Laura Michaelis and Belgian cyclist Milan Menten in 1913. Correct MC <p>299b</p> <p>Which one of the following statements is<strong> <span style="color: #ba372a;"><strong>FALSE</strong></span> </strong> concerning Michaelis-Menten kinetics?</p> A.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> does<strong> <strong>NOT</strong> </strong>apply to allosteric enzymes. Incorrect B.<strong> </strong>The <strong><span style="color: #a1005e;">reaction rate</span></strong> is <strong><span style="color: #009e4c;"><i>proportional</i></span></strong> to the substrate <strong><span style="color: #ff0000;">concentration</span></strong>. Incorrect C.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the <strong><span style="color: #ff0000;">concentration</span></strong> of <strong><span style="color: #2fbd0f;">enzyme-substrate complex [ES]</span></strong> is <strong><span style="color: #6d108e;"><i>constant</i></span></strong>. Incorrect D.<strong> </strong><strong><span style="color: #0d57a5;"><strong><span style="color: #0d57a5;">M-M kinetics</span></strong></span></strong> assumes that the enzyme bound to the substrate [ES] is short lived and does<strong> <strong>NOT</strong> </strong>contribute to the <strong><span style="color: #a1005e;"><strong><span style="color: #a1005e;">reaction rate</span></strong></span></strong>. Correct E.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the product is<strong> <strong>NOT</strong> </strong>available and there is no measureable reverse <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect MC <p>2a1a</p> <p>Which one of the following statements is<strong> <span style="color: #169179;"><strong>TRUE</strong></span> </strong> of Michaelis-Menten kinetics?</p> A.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the substrate is<strong> <strong>NOT</strong> </strong>available and there is no measureable reverse <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect B.<strong> </strong><strong><span style="color: #0d57a5;"><strong><span style="color: #0d57a5;">M-M kinetics</span></strong></span></strong> assumes that the change in <strong><span style="color: #ff0000;"><strong><span style="color: #ff0000;">concentration</span></strong></span></strong> of <strong><span style="color: #2fbd0f;"><strong><span style="color: #2fbd0f;">enzyme-substrate complex [ES]</span></strong></span></strong> does<strong> <strong>NOT</strong> </strong>change. Correct C.<strong> </strong>When the substrate <strong><span style="color: #ff0000;">concentration</span></strong>, [S], is much larger than K<sub>M</sub>, the <strong><span style="color: #a1005e;">reaction rate</span></strong> is linear. Incorrect D.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the enzyme bound to the substrate [ES] is short lived and does<strong> <strong>NOT</strong> </strong>contribute to the <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect E.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> was developed by American linguist Laura Michaelis and Belgian cyclist Milan Menten in 1913. Incorrect MC <p>2c18</p> <p>Which one of the following statements is<strong> <span style="color: #ba372a;"><strong>FALSE</strong></span> </strong> about Michaelis-Menten kinetics?</p> A.<strong> </strong>When the substrate <strong><span style="color: #ff0000;">concentration</span></strong>, [S], is much smaller than K<sub>M</sub>, the <strong><span style="color: #a1005e;">reaction rate</span></strong> is linear. Incorrect B.<strong> </strong>The <strong><span style="color: #a1005e;">reaction rate</span></strong> is <strong><span style="color: #009e4c;"><i>proportional</i></span></strong> to the substrate <strong><span style="color: #ff0000;">concentration</span></strong>. Incorrect C.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the product is<strong> <strong>NOT</strong> </strong>available and there is no measureable reverse <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect D.<strong> </strong><strong><span style="color: #0d57a5;"><strong><span style="color: #0d57a5;">M-M kinetics</span></strong></span></strong> was developed by Greek economist Leo Michelis and Dutch bobsledder Hubert Menten in 1913. Correct E.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> does<strong> <strong>NOT</strong> </strong>apply to allosteric enzymes. Incorrect MC <p>2d68</p> <p>Which one of the following statements is<strong> <span style="color: #ba372a;"><strong>FALSE</strong></span> </strong> concerning Michaelis-Menten kinetics?</p> A.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes a quasi-steady state, that the <strong><span style="color: #2fbd0f;">enzyme-substrate complex [ES]</span></strong> is <strong><span style="color: #6d108e;"><i>constant</i></span></strong>. Incorrect B.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the enzyme bound to the product [EP] is short lived and does<strong> <strong>NOT</strong> </strong>contribute to the <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect C.<strong> </strong>The <strong><span style="color: #a1005e;"><strong><span style="color: #a1005e;">reaction rate</span></strong></span></strong> is <strong><span style="color: #009e4c;"><i><strong><span style="color: #009e4c;"><i>proportional</i></span></strong></i></span></strong> to the product <strong><span style="color: #ff0000;"><strong><span style="color: #ff0000;">concentration</span></strong></span></strong>. Correct D.<strong> </strong>When the substrate <strong><span style="color: #ff0000;">concentration</span></strong>, [S], is much larger than K<sub>M</sub>, the <strong><span style="color: #a1005e;">reaction rate</span></strong> is <strong><span style="color: #6d108e;"><i>constant</i></span></strong>. Incorrect E.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that there is no product available and there is no measureable reverse <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect MC <p>2e8a</p> <p>Which one of the following statements is<strong> <span style="color: #169179;"><strong>TRUE</strong></span> </strong> regarding Michaelis-Menten kinetics?</p> A.<strong> </strong>When the substrate <strong><span style="color: #ff0000;"><strong><span style="color: #ff0000;">concentration</span></strong></span></strong>, [S], is much larger than K<sub>M</sub>, the <strong><span style="color: #a1005e;"><strong><span style="color: #a1005e;">reaction rate</span></strong></span></strong> is <strong><span style="color: #6d108e;"><i><strong><span style="color: #6d108e;"><i>constant</i></span></strong></i></span></strong>. Correct B.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that there is no substrate available and there is no measureable reverse <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect C.<strong> </strong>The <strong><span style="color: #a1005e;">reaction rate</span></strong> is <strong><span style="color: #009e4c;"><i>proportional</i></span></strong> to the product <strong><span style="color: #ff0000;">concentration</span></strong>. Incorrect D.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> was developed by Greek economist Leo Michelis and Dutch bobsledder Hubert Menten in 1913. Incorrect E.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the enzyme bound to the substrate [ES] is short lived and does<strong> <strong>NOT</strong> </strong>contribute to the <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect MC <p>2f08</p> <p>Which one of the following statements is<strong> <span style="color: #ba372a;"><strong>FALSE</strong></span> </strong> about Michaelis-Menten kinetics?</p> A.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> was developed by German biochemist Leonor Michaelis and Canadian physician Maud Menten in 1913. Incorrect B.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> does<strong> <strong>NOT</strong> </strong>apply to allosteric enzymes. Incorrect C.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the <strong><span style="color: #ff5e00;">enzyme-product complex [EP]</span></strong> is short lived and does<strong> <strong>NOT</strong> </strong>contribute to the <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect D.<strong> </strong><strong><span style="color: #0d57a5;"><strong><span style="color: #0d57a5;">M-M kinetics</span></strong></span></strong> assumes that the substrate is<strong> <strong>NOT</strong> </strong>available and there is no measureable reverse <strong><span style="color: #a1005e;"><strong><span style="color: #a1005e;">reaction rate</span></strong></span></strong>. Correct E.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes a quasi-steady state, that the <strong><span style="color: #2fbd0f;">enzyme-substrate complex [ES]</span></strong> is <strong><span style="color: #6d108e;"><i>constant</i></span></strong>. Incorrect MC <p>33d7</p> <p>Which one of the following statements is<strong> <span style="color: #169179;"><strong>TRUE</strong></span> </strong> of Michaelis-Menten kinetics?</p> A.<strong> </strong><strong><span style="color: #0d57a5;"><strong><span style="color: #0d57a5;">M-M kinetics</span></strong></span></strong> was developed by German biochemist Leonor Michaelis and Canadian physician Maud Menten in 1913. Correct B.<strong> </strong>When the substrate <strong><span style="color: #ff0000;">concentration</span></strong>, [S], is much larger than K<sub>M</sub>, the <strong><span style="color: #a1005e;">reaction rate</span></strong> is linear. Incorrect C.<strong> </strong>The <strong><span style="color: #a1005e;">reaction rate</span></strong> is <strong><span style="color: #009e4c;"><i>proportional</i></span></strong> to the product <strong><span style="color: #ff0000;">concentration</span></strong>. Incorrect D.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the change in <strong><span style="color: #ff0000;">concentration</span></strong> of <strong><span style="color: #ff5e00;">enzyme-product complex [EP]</span></strong> does<strong> <strong>NOT</strong> </strong>change. Incorrect E.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the enzyme bound to the substrate [ES] is short lived and does<strong> <strong>NOT</strong> </strong>contribute to the <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect MC <p>3b01</p> <p>Which one of the following statements is<strong> <span style="color: #ba372a;"><strong>FALSE</strong></span> </strong> about Michaelis-Menten kinetics?</p> A.<strong> </strong>When the substrate <strong><span style="color: #ff0000;">concentration</span></strong>, [S], is much smaller than K<sub>M</sub>, the <strong><span style="color: #a1005e;">reaction rate</span></strong> is linear. Incorrect B.<strong> </strong><strong><span style="color: #0d57a5;"><strong><span style="color: #0d57a5;">M-M kinetics</span></strong></span></strong> assumes that there is no substrate available and there is no measureable reverse <strong><span style="color: #a1005e;"><strong><span style="color: #a1005e;">reaction rate</span></strong></span></strong>. Correct C.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes a quasi-steady state, that the <strong><span style="color: #2fbd0f;">enzyme-substrate complex [ES]</span></strong> is <strong><span style="color: #6d108e;"><i>constant</i></span></strong>. Incorrect D.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> does<strong> <strong>NOT</strong> </strong>apply to allosteric enzymes. Incorrect E.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> was developed by German biochemist Leonor Michaelis and Canadian physician Maud Menten in 1913. Incorrect MC <p>3caa</p> <p>Which one of the following statements is<strong> <span style="color: #169179;"><strong>TRUE</strong></span> </strong> regarding Michaelis-Menten kinetics?</p> A.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the <strong><span style="color: #ff5e00;">enzyme-product complex [EP]</span></strong> is <strong><span style="color: #6d108e;"><i>constant</i></span></strong>. Incorrect B.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the <strong><span style="color: #2fbd0f;">enzyme-substrate complex [ES]</span></strong> is short lived and does<strong> <strong>NOT</strong> </strong>contribute to the <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect C.<strong> </strong><strong><span style="color: #0d57a5;"><strong><span style="color: #0d57a5;">M-M kinetics</span></strong></span></strong> assumes the enzyme has a single active site. Correct D.<strong> </strong>The <strong><span style="color: #a1005e;">reaction rate</span></strong> is <strong><span style="color: #009e4c;"><i>proportional</i></span></strong> to the product <strong><span style="color: #ff0000;">concentration</span></strong>. Incorrect E.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> was developed by Greek economist Leo Michelis and Dutch bobsledder Hubert Menten in 1913. Incorrect MC <p>3cb6</p> <p>Which one of the following statements is<strong> <span style="color: #ba372a;"><strong>FALSE</strong></span> </strong> about Michaelis-Menten kinetics?</p> A.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the <strong><span style="color: #ff5e00;">enzyme-product complex [EP]</span></strong> is short lived and does<strong> <strong>NOT</strong> </strong>contribute to the <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect B.<strong> </strong>The <strong><span style="color: #a1005e;">reaction rate</span></strong> is <strong><span style="color: #009e4c;"><i>proportional</i></span></strong> to the substrate <strong><span style="color: #ff0000;">concentration</span></strong>. Incorrect C.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the change in <strong><span style="color: #ff0000;">concentration</span></strong> of <strong><span style="color: #2fbd0f;">enzyme-substrate complex [ES]</span></strong> does<strong> <strong>NOT</strong> </strong>change. Incorrect D.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that there is no product available and there is no measureable reverse <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect E.<strong> </strong>When the substrate <strong><span style="color: #ff0000;"><strong><span style="color: #ff0000;">concentration</span></strong></span></strong>, [S], is much larger than K<sub>M</sub>, the <strong><span style="color: #a1005e;"><strong><span style="color: #a1005e;">reaction rate</span></strong></span></strong> is linear. Correct MC <p>3ccb</p> <p>Which one of the following statements is<strong> <span style="color: #ba372a;"><strong>FALSE</strong></span> </strong> about Michaelis-Menten kinetics?</p> A.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes the enzyme has a single active site. Incorrect B.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the <strong><span style="color: #ff5e00;">enzyme-product complex [EP]</span></strong> is short lived and does<strong> <strong>NOT</strong> </strong>contribute to the <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect C.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the product is<strong> <strong>NOT</strong> </strong>available and there is no measureable reverse <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect D.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the rate of breaking the <strong><span style="color: #2fbd0f;">enzyme-substrate complex [ES]</span></strong> is equal to the rate of its formation. Incorrect E.<strong> </strong><strong><span style="color: #0d57a5;"><strong><span style="color: #0d57a5;">M-M kinetics</span></strong></span></strong> was developed by American linguist Laura Michaelis and Belgian cyclist Milan Menten in 1913. Correct MC <p>3fb3</p> <p>Which one of the following statements is<strong> <span style="color: #ba372a;"><strong>FALSE</strong></span> </strong> concerning Michaelis-Menten kinetics?</p> A.<strong> </strong>When the substrate <strong><span style="color: #ff0000;">concentration</span></strong>, [S], is much smaller than K<sub>M</sub>, the <strong><span style="color: #a1005e;">reaction rate</span></strong> is linear. Incorrect B.<strong> </strong><strong><span style="color: #0d57a5;"><strong><span style="color: #0d57a5;">M-M kinetics</span></strong></span></strong> assumes that the substrate is<strong> <strong>NOT</strong> </strong>available and there is no measureable reverse <strong><span style="color: #a1005e;"><strong><span style="color: #a1005e;">reaction rate</span></strong></span></strong>. Correct C.<strong> </strong>The <strong><span style="color: #a1005e;">reaction rate</span></strong> is <strong><span style="color: #009e4c;"><i>proportional</i></span></strong> to the substrate <strong><span style="color: #ff0000;">concentration</span></strong>. Incorrect D.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the <strong><span style="color: #ff0000;">concentration</span></strong> of <strong><span style="color: #2fbd0f;">enzyme-substrate complex [ES]</span></strong> is <strong><span style="color: #6d108e;"><i>constant</i></span></strong>. Incorrect E.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the <strong><span style="color: #ff5e00;">enzyme-product complex [EP]</span></strong> is short lived and does<strong> <strong>NOT</strong> </strong>contribute to the <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect MC <p>4004</p> <p>Which one of the following statements is<strong> <span style="color: #ba372a;"><strong>FALSE</strong></span> </strong> about Michaelis-Menten kinetics?</p> A.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> was developed by German biochemist Leonor Michaelis and Canadian physician Maud Menten in 1913. Incorrect B.<strong> </strong>When the substrate <strong><span style="color: #ff0000;">concentration</span></strong>, [S], is much larger than K<sub>M</sub>, the <strong><span style="color: #a1005e;">reaction rate</span></strong> is <strong><span style="color: #6d108e;"><i>constant</i></span></strong>. Incorrect C.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> does<strong> <strong>NOT</strong> </strong>apply to allosteric enzymes. Incorrect D.<strong> </strong><strong><span style="color: #0d57a5;"><strong><span style="color: #0d57a5;">M-M kinetics</span></strong></span></strong> assumes that the <strong><span style="color: #ff0000;"><strong><span style="color: #ff0000;">concentration</span></strong></span></strong> of <strong><span style="color: #ff5e00;"><strong><span style="color: #ff5e00;">enzyme-product complex [EP]</span></strong></span></strong> is <strong><span style="color: #6d108e;"><i><strong><span style="color: #6d108e;"><i>constant</i></span></strong></i></span></strong>. Correct E.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that there is no product available and there is no measureable reverse <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect MC <p>40d6</p> <p>Which one of the following statements is<strong> <span style="color: #169179;"><strong>TRUE</strong></span> </strong> of Michaelis-Menten kinetics?</p> A.<strong> </strong>The <strong><span style="color: #a1005e;">reaction rate</span></strong> is <strong><span style="color: #009e4c;"><i>proportional</i></span></strong> to the product <strong><span style="color: #ff0000;">concentration</span></strong>. Incorrect B.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> was developed by American linguist Laura Michaelis and Belgian cyclist Milan Menten in 1913. Incorrect C.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the rate of breaking the <strong><span style="color: #ff5e00;">enzyme-product complex [EP]</span></strong> is equal to the rate of its formation. Incorrect D.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the substrate is<strong> <strong>NOT</strong> </strong>available and there is no measureable reverse <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect E.<strong> </strong><strong><span style="color: #0d57a5;"><strong><span style="color: #0d57a5;">M-M kinetics</span></strong></span></strong> assumes the enzyme has a single active site. Correct MC <p>4ddd</p> <p>Which one of the following statements is<strong> <span style="color: #ba372a;"><strong>FALSE</strong></span> </strong> concerning Michaelis-Menten kinetics?</p> A.<strong> </strong><strong><span style="color: #0d57a5;"><strong><span style="color: #0d57a5;">M-M kinetics</span></strong></span></strong> assumes that the <strong><span style="color: #ff0000;"><strong><span style="color: #ff0000;">concentration</span></strong></span></strong> of <strong><span style="color: #ff5e00;"><strong><span style="color: #ff5e00;">enzyme-product complex [EP]</span></strong></span></strong> is <strong><span style="color: #6d108e;"><i><strong><span style="color: #6d108e;"><i>constant</i></span></strong></i></span></strong>. Correct B.<strong> </strong>The <strong><span style="color: #a1005e;">reaction rate</span></strong> is <strong><span style="color: #009e4c;"><i>proportional</i></span></strong> to the substrate <strong><span style="color: #ff0000;">concentration</span></strong>. Incorrect C.<strong> </strong>When the substrate <strong><span style="color: #ff0000;">concentration</span></strong>, [S], is much smaller than K<sub>M</sub>, the <strong><span style="color: #a1005e;">reaction rate</span></strong> is linear. Incorrect D.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the product is<strong> <strong>NOT</strong> </strong>available and there is no measureable reverse <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect E.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> was developed by German biochemist Leonor Michaelis and Canadian physician Maud Menten in 1913. Incorrect MC <p>4eb7</p> <p>Which one of the following statements is<strong> <span style="color: #169179;"><strong>TRUE</strong></span> </strong> regarding Michaelis-Menten kinetics?</p> A.<strong> </strong>When the substrate <strong><span style="color: #ff0000;">concentration</span></strong>, [S], is much larger than K<sub>M</sub>, the <strong><span style="color: #a1005e;">reaction rate</span></strong> is linear. Incorrect B.<strong> </strong>The <strong><span style="color: #a1005e;">reaction rate</span></strong> is <strong><span style="color: #009e4c;"><i>proportional</i></span></strong> to the product <strong><span style="color: #ff0000;">concentration</span></strong>. Incorrect C.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the change in <strong><span style="color: #ff0000;">concentration</span></strong> of <strong><span style="color: #ff5e00;">enzyme-product complex [EP]</span></strong> does<strong> <strong>NOT</strong> </strong>change. Incorrect D.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that there is no substrate available and there is no measureable reverse <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect E.<strong> </strong><strong><span style="color: #0d57a5;"><strong><span style="color: #0d57a5;">M-M kinetics</span></strong></span></strong> assumes that the enzyme bound to the product [EP] is short lived and does<strong> <strong>NOT</strong> </strong>contribute to the <strong><span style="color: #a1005e;"><strong><span style="color: #a1005e;">reaction rate</span></strong></span></strong>. Correct MC <p>520d</p> <p>Which one of the following statements is<strong> <span style="color: #ba372a;"><strong>FALSE</strong></span> </strong> about Michaelis-Menten kinetics?</p> A.<strong> </strong>When the substrate <strong><span style="color: #ff0000;">concentration</span></strong>, [S], is much larger than K<sub>M</sub>, the <strong><span style="color: #a1005e;">reaction rate</span></strong> is <strong><span style="color: #6d108e;"><i>constant</i></span></strong>. Incorrect B.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> was developed by German biochemist Leonor Michaelis and Canadian physician Maud Menten in 1913. Incorrect C.<strong> </strong>The <strong><span style="color: #a1005e;">reaction rate</span></strong> is <strong><span style="color: #009e4c;"><i>proportional</i></span></strong> to the substrate <strong><span style="color: #ff0000;">concentration</span></strong>. Incorrect D.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes the enzyme has a single active site. Incorrect E.<strong> </strong><strong><span style="color: #0d57a5;"><strong><span style="color: #0d57a5;">M-M kinetics</span></strong></span></strong> assumes that the <strong><span style="color: #ff0000;"><strong><span style="color: #ff0000;">concentration</span></strong></span></strong> of <strong><span style="color: #ff5e00;"><strong><span style="color: #ff5e00;">enzyme-product complex [EP]</span></strong></span></strong> is <strong><span style="color: #6d108e;"><i><strong><span style="color: #6d108e;"><i>constant</i></span></strong></i></span></strong>. Correct MC <p>5453</p> <p>Which one of the following statements is<strong> <span style="color: #169179;"><strong>TRUE</strong></span> </strong> of Michaelis-Menten kinetics?</p> A.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the <strong><span style="color: #ff5e00;">enzyme-product complex [EP]</span></strong> is <strong><span style="color: #6d108e;"><i>constant</i></span></strong>. Incorrect B.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> was developed by American linguist Laura Michaelis and Belgian cyclist Milan Menten in 1913. Incorrect C.<strong> </strong><strong><span style="color: #0d57a5;"><strong><span style="color: #0d57a5;">M-M kinetics</span></strong></span></strong> assumes the enzyme has a single active site. Correct D.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the enzyme bound to the substrate [ES] is short lived and does<strong> <strong>NOT</strong> </strong>contribute to the <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect E.<strong> </strong>When the substrate <strong><span style="color: #ff0000;">concentration</span></strong>, [S], is much larger than K<sub>M</sub>, the <strong><span style="color: #a1005e;">reaction rate</span></strong> is linear. Incorrect MC <p>5869</p> <p>Which one of the following statements is<strong> <span style="color: #ba372a;"><strong>FALSE</strong></span> </strong> concerning Michaelis-Menten kinetics?</p> A.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the change in <strong><span style="color: #ff0000;">concentration</span></strong> of <strong><span style="color: #2fbd0f;">enzyme-substrate complex [ES]</span></strong> does<strong> <strong>NOT</strong> </strong>change. Incorrect B.<strong> </strong>When the substrate <strong><span style="color: #ff0000;">concentration</span></strong>, [S], is much smaller than K<sub>M</sub>, the <strong><span style="color: #a1005e;">reaction rate</span></strong> is linear. Incorrect C.<strong> </strong>The <strong><span style="color: #a1005e;">reaction rate</span></strong> is <strong><span style="color: #009e4c;"><i>proportional</i></span></strong> to the substrate <strong><span style="color: #ff0000;">concentration</span></strong>. Incorrect D.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> does<strong> <strong>NOT</strong> </strong>apply to allosteric enzymes. Incorrect E.<strong> </strong><strong><span style="color: #0d57a5;"><strong><span style="color: #0d57a5;">M-M kinetics</span></strong></span></strong> assumes that the substrate is<strong> <strong>NOT</strong> </strong>available and there is no measureable reverse <strong><span style="color: #a1005e;"><strong><span style="color: #a1005e;">reaction rate</span></strong></span></strong>. Correct MC <p>59e8</p> <p>Which one of the following statements is<strong> <span style="color: #169179;"><strong>TRUE</strong></span> </strong> regarding Michaelis-Menten kinetics?</p> A.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the <strong><span style="color: #2fbd0f;">enzyme-substrate complex [ES]</span></strong> is short lived and does<strong> <strong>NOT</strong> </strong>contribute to the <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect B.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the substrate is<strong> <strong>NOT</strong> </strong>available and there is no measureable reverse <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect C.<strong> </strong>The <strong><span style="color: #a1005e;">reaction rate</span></strong> is <strong><span style="color: #009e4c;"><i>proportional</i></span></strong> to the product <strong><span style="color: #ff0000;">concentration</span></strong>. Incorrect D.<strong> </strong><strong><span style="color: #0d57a5;"><strong><span style="color: #0d57a5;">M-M kinetics</span></strong></span></strong> assumes that the <strong><span style="color: #ff0000;"><strong><span style="color: #ff0000;">concentration</span></strong></span></strong> of <strong><span style="color: #2fbd0f;"><strong><span style="color: #2fbd0f;">enzyme-substrate complex [ES]</span></strong></span></strong> is <strong><span style="color: #6d108e;"><i><strong><span style="color: #6d108e;"><i>constant</i></span></strong></i></span></strong>. Correct E.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> was developed by American linguist Laura Michaelis and Belgian cyclist Milan Menten in 1913. Incorrect MC <p>5bc6</p> <p>Which one of the following statements is<strong> <span style="color: #ba372a;"><strong>FALSE</strong></span> </strong> concerning Michaelis-Menten kinetics?</p> A.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> was developed by German biochemist Leonor Michaelis and Canadian physician Maud Menten in 1913. Incorrect B.<strong> </strong>The <strong><span style="color: #a1005e;">reaction rate</span></strong> is <strong><span style="color: #009e4c;"><i>proportional</i></span></strong> to the substrate <strong><span style="color: #ff0000;">concentration</span></strong>. Incorrect C.<strong> </strong><strong><span style="color: #0d57a5;"><strong><span style="color: #0d57a5;">M-M kinetics</span></strong></span></strong> assumes that the rate of breaking the <strong><span style="color: #ff5e00;"><strong><span style="color: #ff5e00;">enzyme-product complex [EP]</span></strong></span></strong> is equal to the rate of its formation. Correct D.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that there is no product available and there is no measureable reverse <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect E.<strong> </strong>When the substrate <strong><span style="color: #ff0000;">concentration</span></strong>, [S], is much larger than K<sub>M</sub>, the <strong><span style="color: #a1005e;">reaction rate</span></strong> is <strong><span style="color: #6d108e;"><i>constant</i></span></strong>. Incorrect MC <p>610b</p> <p>Which one of the following statements is<strong> <span style="color: #169179;"><strong>TRUE</strong></span> </strong> regarding Michaelis-Menten kinetics?</p> A.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the rate of breaking the <strong><span style="color: #ff5e00;">enzyme-product complex [EP]</span></strong> is equal to the rate of its formation. Incorrect B.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the <strong><span style="color: #2fbd0f;">enzyme-substrate complex [ES]</span></strong> is short lived and does<strong> <strong>NOT</strong> </strong>contribute to the <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect C.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the substrate is<strong> <strong>NOT</strong> </strong>available and there is no measureable reverse <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect D.<strong> </strong>When the substrate <strong><span style="color: #ff0000;"><strong><span style="color: #ff0000;">concentration</span></strong></span></strong>, [S], is much smaller than K<sub>M</sub>, the <strong><span style="color: #a1005e;"><strong><span style="color: #a1005e;">reaction rate</span></strong></span></strong> is linear. Correct E.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> was developed by Greek economist Leo Michelis and Dutch bobsledder Hubert Menten in 1913. Incorrect MC <p>6567</p> <p>Which one of the following statements is<strong> <span style="color: #169179;"><strong>TRUE</strong></span> </strong> of Michaelis-Menten kinetics?</p> A.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> was developed by Greek economist Leo Michelis and Dutch bobsledder Hubert Menten in 1913. Incorrect B.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the enzyme bound to the substrate [ES] is short lived and does<strong> <strong>NOT</strong> </strong>contribute to the <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect C.<strong> </strong>The <strong><span style="color: #a1005e;">reaction rate</span></strong> is <strong><span style="color: #009e4c;"><i>proportional</i></span></strong> to the product <strong><span style="color: #ff0000;">concentration</span></strong>. Incorrect D.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the change in <strong><span style="color: #ff0000;">concentration</span></strong> of <strong><span style="color: #ff5e00;">enzyme-product complex [EP]</span></strong> does<strong> <strong>NOT</strong> </strong>change. Incorrect E.<strong> </strong><strong><span style="color: #0d57a5;"><strong><span style="color: #0d57a5;">M-M kinetics</span></strong></span></strong> does<strong> <strong>NOT</strong> </strong>apply to allosteric enzymes. Correct MC <p>6582</p> <p>Which one of the following statements is<strong> <span style="color: #169179;"><strong>TRUE</strong></span> </strong> regarding Michaelis-Menten kinetics?</p> A.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> was developed by Greek economist Leo Michelis and Dutch bobsledder Hubert Menten in 1913. Incorrect B.<strong> </strong>When the substrate <strong><span style="color: #ff0000;"><strong><span style="color: #ff0000;">concentration</span></strong></span></strong>, [S], is much larger than K<sub>M</sub>, the <strong><span style="color: #a1005e;"><strong><span style="color: #a1005e;">reaction rate</span></strong></span></strong> is <strong><span style="color: #6d108e;"><i><strong><span style="color: #6d108e;"><i>constant</i></span></strong></i></span></strong>. Correct C.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the <strong><span style="color: #ff0000;">concentration</span></strong> of <strong><span style="color: #ff5e00;">enzyme-product complex [EP]</span></strong> is <strong><span style="color: #6d108e;"><i>constant</i></span></strong>. Incorrect D.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the enzyme bound to the substrate [ES] is short lived and does<strong> <strong>NOT</strong> </strong>contribute to the <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect E.<strong> </strong>The <strong><span style="color: #a1005e;">reaction rate</span></strong> is <strong><span style="color: #009e4c;"><i>proportional</i></span></strong> to the product <strong><span style="color: #ff0000;">concentration</span></strong>. Incorrect MC <p>65d9</p> <p>Which one of the following statements is<strong> <span style="color: #ba372a;"><strong>FALSE</strong></span> </strong> concerning Michaelis-Menten kinetics?</p> A.<strong> </strong>When the substrate <strong><span style="color: #ff0000;">concentration</span></strong>, [S], is much smaller than K<sub>M</sub>, the <strong><span style="color: #a1005e;">reaction rate</span></strong> is linear. Incorrect B.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> was developed by German biochemist Leonor Michaelis and Canadian physician Maud Menten in 1913. Incorrect C.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the rate of breaking the <strong><span style="color: #2fbd0f;">enzyme-substrate complex [ES]</span></strong> is equal to the rate of its formation. Incorrect D.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes the enzyme has a single active site. Incorrect E.<strong> </strong><strong><span style="color: #0d57a5;"><strong><span style="color: #0d57a5;">M-M kinetics</span></strong></span></strong> assumes that the enzyme bound to the substrate [ES] is short lived and does<strong> <strong>NOT</strong> </strong>contribute to the <strong><span style="color: #a1005e;"><strong><span style="color: #a1005e;">reaction rate</span></strong></span></strong>. Correct MC <p>6974</p> <p>Which one of the following statements is<strong> <span style="color: #ba372a;"><strong>FALSE</strong></span> </strong> about Michaelis-Menten kinetics?</p> A.<strong> </strong>The <strong><span style="color: #a1005e;">reaction rate</span></strong> is <strong><span style="color: #009e4c;"><i>proportional</i></span></strong> to the substrate <strong><span style="color: #ff0000;">concentration</span></strong>. Incorrect B.<strong> </strong>When the substrate <strong><span style="color: #ff0000;"><strong><span style="color: #ff0000;">concentration</span></strong></span></strong>, [S], is much smaller than K<sub>M</sub>, the <strong><span style="color: #a1005e;"><strong><span style="color: #a1005e;">reaction rate</span></strong></span></strong> is <strong><span style="color: #6d108e;"><i><strong><span style="color: #6d108e;"><i>constant</i></span></strong></i></span></strong>. Correct C.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes the enzyme has a single active site. Incorrect D.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the <strong><span style="color: #ff0000;">concentration</span></strong> of <strong><span style="color: #2fbd0f;">enzyme-substrate complex [ES]</span></strong> is <strong><span style="color: #6d108e;"><i>constant</i></span></strong>. Incorrect E.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the product is<strong> <strong>NOT</strong> </strong>available and there is no measureable reverse <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect MC <p>6ae8</p> <p>Which one of the following statements is<strong> <span style="color: #ba372a;"><strong>FALSE</strong></span> </strong> about Michaelis-Menten kinetics?</p> A.<strong> </strong>The <strong><span style="color: #a1005e;">reaction rate</span></strong> is <strong><span style="color: #009e4c;"><i>proportional</i></span></strong> to the substrate <strong><span style="color: #ff0000;">concentration</span></strong>. Incorrect B.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the rate of breaking the <strong><span style="color: #2fbd0f;">enzyme-substrate complex [ES]</span></strong> is equal to the rate of its formation. Incorrect C.<strong> </strong><strong><span style="color: #0d57a5;"><strong><span style="color: #0d57a5;">M-M kinetics</span></strong></span></strong> assumes that the substrate is<strong> <strong>NOT</strong> </strong>available and there is no measureable reverse <strong><span style="color: #a1005e;"><strong><span style="color: #a1005e;">reaction rate</span></strong></span></strong>. Correct D.<strong> </strong>When the substrate <strong><span style="color: #ff0000;">concentration</span></strong>, [S], is much larger than K<sub>M</sub>, the <strong><span style="color: #a1005e;">reaction rate</span></strong> is <strong><span style="color: #6d108e;"><i>constant</i></span></strong>. Incorrect E.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> was developed by German biochemist Leonor Michaelis and Canadian physician Maud Menten in 1913. Incorrect MC <p>7178</p> <p>Which one of the following statements is<strong> <span style="color: #169179;"><strong>TRUE</strong></span> </strong> of Michaelis-Menten kinetics?</p> A.<strong> </strong>When the substrate <strong><span style="color: #ff0000;">concentration</span></strong>, [S], is much larger than K<sub>M</sub>, the <strong><span style="color: #a1005e;">reaction rate</span></strong> is linear. Incorrect B.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that there is no substrate available and there is no measureable reverse <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect C.<strong> </strong><strong><span style="color: #0d57a5;"><strong><span style="color: #0d57a5;">M-M kinetics</span></strong></span></strong> assumes that the enzyme bound to the product [EP] is short lived and does<strong> <strong>NOT</strong> </strong>contribute to the <strong><span style="color: #a1005e;"><strong><span style="color: #a1005e;">reaction rate</span></strong></span></strong>. Correct D.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the rate of breaking the <strong><span style="color: #ff5e00;">enzyme-product complex [EP]</span></strong> is equal to the rate of its formation. Incorrect E.<strong> </strong>The <strong><span style="color: #a1005e;">reaction rate</span></strong> is <strong><span style="color: #009e4c;"><i>proportional</i></span></strong> to the product <strong><span style="color: #ff0000;">concentration</span></strong>. Incorrect MC <p>7182</p> <p>Which one of the following statements is<strong> <span style="color: #169179;"><strong>TRUE</strong></span> </strong> of Michaelis-Menten kinetics?</p> A.<strong> </strong>When the substrate <strong><span style="color: #ff0000;">concentration</span></strong>, [S], is much larger than K<sub>M</sub>, the <strong><span style="color: #a1005e;">reaction rate</span></strong> is linear. Incorrect B.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the enzyme bound to the substrate [ES] is short lived and does<strong> <strong>NOT</strong> </strong>contribute to the <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect C.<strong> </strong><strong><span style="color: #0d57a5;"><strong><span style="color: #0d57a5;">M-M kinetics</span></strong></span></strong> assumes a quasi-steady state, that the <strong><span style="color: #2fbd0f;"><strong><span style="color: #2fbd0f;">enzyme-substrate complex [ES]</span></strong></span></strong> is <strong><span style="color: #6d108e;"><i><strong><span style="color: #6d108e;"><i>constant</i></span></strong></i></span></strong>. Correct D.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that there is no substrate available and there is no measureable reverse <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect E.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> was developed by American linguist Laura Michaelis and Belgian cyclist Milan Menten in 1913. Incorrect MC <p>7264</p> <p>Which one of the following statements is<strong> <span style="color: #169179;"><strong>TRUE</strong></span> </strong> regarding Michaelis-Menten kinetics?</p> A.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> was developed by Greek economist Leo Michelis and Dutch bobsledder Hubert Menten in 1913. Incorrect B.<strong> </strong><strong><span style="color: #0d57a5;"><strong><span style="color: #0d57a5;">M-M kinetics</span></strong></span></strong> assumes that the rate of breaking the <strong><span style="color: #2fbd0f;"><strong><span style="color: #2fbd0f;">enzyme-substrate complex [ES]</span></strong></span></strong> is equal to the rate of its formation. Correct C.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that there is no substrate available and there is no measureable reverse <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect D.<strong> </strong>When the substrate <strong><span style="color: #ff0000;">concentration</span></strong>, [S], is much smaller than K<sub>M</sub>, the <strong><span style="color: #a1005e;">reaction rate</span></strong> is <strong><span style="color: #6d108e;"><i>constant</i></span></strong>. Incorrect E.<strong> </strong>The <strong><span style="color: #a1005e;">reaction rate</span></strong> is <strong><span style="color: #009e4c;"><i>proportional</i></span></strong> to the product <strong><span style="color: #ff0000;">concentration</span></strong>. Incorrect MC <p>7753</p> <p>Which one of the following statements is<strong> <span style="color: #169179;"><strong>TRUE</strong></span> </strong> regarding Michaelis-Menten kinetics?</p> A.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that there is no substrate available and there is no measureable reverse <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect B.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> was developed by American linguist Laura Michaelis and Belgian cyclist Milan Menten in 1913. Incorrect C.<strong> </strong>The <strong><span style="color: #a1005e;">reaction rate</span></strong> is <strong><span style="color: #009e4c;"><i>proportional</i></span></strong> to the product <strong><span style="color: #ff0000;">concentration</span></strong>. Incorrect D.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the <strong><span style="color: #2fbd0f;">enzyme-substrate complex [ES]</span></strong> is short lived and does<strong> <strong>NOT</strong> </strong>contribute to the <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect E.<strong> </strong>When the substrate <strong><span style="color: #ff0000;"><strong><span style="color: #ff0000;">concentration</span></strong></span></strong>, [S], is much smaller than K<sub>M</sub>, the <strong><span style="color: #a1005e;"><strong><span style="color: #a1005e;">reaction rate</span></strong></span></strong> is linear. Correct MC <p>7943</p> <p>Which one of the following statements is<strong> <span style="color: #169179;"><strong>TRUE</strong></span> </strong> of Michaelis-Menten kinetics?</p> A.<strong> </strong>The <strong><span style="color: #a1005e;">reaction rate</span></strong> is <strong><span style="color: #009e4c;"><i>proportional</i></span></strong> to the product <strong><span style="color: #ff0000;">concentration</span></strong>. Incorrect B.<strong> </strong><strong><span style="color: #0d57a5;"><strong><span style="color: #0d57a5;">M-M kinetics</span></strong></span></strong> assumes a quasi-steady state, that the <strong><span style="color: #2fbd0f;"><strong><span style="color: #2fbd0f;">enzyme-substrate complex [ES]</span></strong></span></strong> is <strong><span style="color: #6d108e;"><i><strong><span style="color: #6d108e;"><i>constant</i></span></strong></i></span></strong>. Correct C.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the substrate is<strong> <strong>NOT</strong> </strong>available and there is no measureable reverse <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect D.<strong> </strong>When the substrate <strong><span style="color: #ff0000;">concentration</span></strong>, [S], is much smaller than K<sub>M</sub>, the <strong><span style="color: #a1005e;">reaction rate</span></strong> is <strong><span style="color: #6d108e;"><i>constant</i></span></strong>. Incorrect E.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the enzyme bound to the substrate [ES] is short lived and does<strong> <strong>NOT</strong> </strong>contribute to the <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect MC <p>8479</p> <p>Which one of the following statements is<strong> <span style="color: #169179;"><strong>TRUE</strong></span> </strong> regarding Michaelis-Menten kinetics?</p> A.<strong> </strong>When the substrate <strong><span style="color: #ff0000;">concentration</span></strong>, [S], is much larger than K<sub>M</sub>, the <strong><span style="color: #a1005e;">reaction rate</span></strong> is linear. Incorrect B.<strong> </strong><strong><span style="color: #0d57a5;"><strong><span style="color: #0d57a5;">M-M kinetics</span></strong></span></strong> does<strong> <strong>NOT</strong> </strong>apply to allosteric enzymes. Correct C.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the substrate is<strong> <strong>NOT</strong> </strong>available and there is no measureable reverse <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect D.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the <strong><span style="color: #ff0000;">concentration</span></strong> of <strong><span style="color: #ff5e00;">enzyme-product complex [EP]</span></strong> is <strong><span style="color: #6d108e;"><i>constant</i></span></strong>. Incorrect E.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> was developed by American linguist Laura Michaelis and Belgian cyclist Milan Menten in 1913. Incorrect MC <p>850d</p> <p>Which one of the following statements is<strong> <span style="color: #169179;"><strong>TRUE</strong></span> </strong> of Michaelis-Menten kinetics?</p> A.<strong> </strong>The <strong><span style="color: #a1005e;"><strong><span style="color: #a1005e;">reaction rate</span></strong></span></strong> is <strong><span style="color: #009e4c;"><i><strong><span style="color: #009e4c;"><i>proportional</i></span></strong></i></span></strong> to the substrate <strong><span style="color: #ff0000;"><strong><span style="color: #ff0000;">concentration</span></strong></span></strong>. Correct B.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> was developed by Greek economist Leo Michelis and Dutch bobsledder Hubert Menten in 1913. Incorrect C.<strong> </strong>When the substrate <strong><span style="color: #ff0000;">concentration</span></strong>, [S], is much larger than K<sub>M</sub>, the <strong><span style="color: #a1005e;">reaction rate</span></strong> is linear. Incorrect D.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the enzyme bound to the substrate [ES] is short lived and does<strong> <strong>NOT</strong> </strong>contribute to the <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect E.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the change in <strong><span style="color: #ff0000;">concentration</span></strong> of <strong><span style="color: #ff5e00;">enzyme-product complex [EP]</span></strong> does<strong> <strong>NOT</strong> </strong>change. Incorrect MC <p>857b</p> <p>Which one of the following statements is<strong> <span style="color: #ba372a;"><strong>FALSE</strong></span> </strong> concerning Michaelis-Menten kinetics?</p> A.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the rate of breaking the <strong><span style="color: #2fbd0f;">enzyme-substrate complex [ES]</span></strong> is equal to the rate of its formation. Incorrect B.<strong> </strong>The <strong><span style="color: #a1005e;"><strong><span style="color: #a1005e;">reaction rate</span></strong></span></strong> is <strong><span style="color: #009e4c;"><i><strong><span style="color: #009e4c;"><i>proportional</i></span></strong></i></span></strong> to the product <strong><span style="color: #ff0000;"><strong><span style="color: #ff0000;">concentration</span></strong></span></strong>. Correct C.<strong> </strong>When the substrate <strong><span style="color: #ff0000;">concentration</span></strong>, [S], is much smaller than K<sub>M</sub>, the <strong><span style="color: #a1005e;">reaction rate</span></strong> is linear. Incorrect D.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the product is<strong> <strong>NOT</strong> </strong>available and there is no measureable reverse <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect E.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the enzyme bound to the product [EP] is short lived and does<strong> <strong>NOT</strong> </strong>contribute to the <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect MC <p>86cc</p> <p>Which one of the following statements is<strong> <span style="color: #ba372a;"><strong>FALSE</strong></span> </strong> about Michaelis-Menten kinetics?</p> A.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the <strong><span style="color: #ff5e00;">enzyme-product complex [EP]</span></strong> is short lived and does<strong> <strong>NOT</strong> </strong>contribute to the <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect B.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes the enzyme has a single active site. Incorrect C.<strong> </strong>The <strong><span style="color: #a1005e;">reaction rate</span></strong> is <strong><span style="color: #009e4c;"><i>proportional</i></span></strong> to the substrate <strong><span style="color: #ff0000;">concentration</span></strong>. Incorrect D.<strong> </strong><strong><span style="color: #0d57a5;"><strong><span style="color: #0d57a5;">M-M kinetics</span></strong></span></strong> assumes that there is no substrate available and there is no measureable reverse <strong><span style="color: #a1005e;"><strong><span style="color: #a1005e;">reaction rate</span></strong></span></strong>. Correct E.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> was developed by German biochemist Leonor Michaelis and Canadian physician Maud Menten in 1913. Incorrect MC <p>8bcd</p> <p>Which one of the following statements is<strong> <span style="color: #169179;"><strong>TRUE</strong></span> </strong> regarding Michaelis-Menten kinetics?</p> A.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> was developed by American linguist Laura Michaelis and Belgian cyclist Milan Menten in 1913. Incorrect B.<strong> </strong>When the substrate <strong><span style="color: #ff0000;">concentration</span></strong>, [S], is much larger than K<sub>M</sub>, the <strong><span style="color: #a1005e;">reaction rate</span></strong> is linear. Incorrect C.<strong> </strong><strong><span style="color: #0d57a5;"><strong><span style="color: #0d57a5;">M-M kinetics</span></strong></span></strong> assumes that the <strong><span style="color: #ff0000;"><strong><span style="color: #ff0000;">concentration</span></strong></span></strong> of <strong><span style="color: #2fbd0f;"><strong><span style="color: #2fbd0f;">enzyme-substrate complex [ES]</span></strong></span></strong> is <strong><span style="color: #6d108e;"><i><strong><span style="color: #6d108e;"><i>constant</i></span></strong></i></span></strong>. Correct D.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that there is no substrate available and there is no measureable reverse <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect E.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the <strong><span style="color: #2fbd0f;">enzyme-substrate complex [ES]</span></strong> is short lived and does<strong> <strong>NOT</strong> </strong>contribute to the <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect MC <p>91aa</p> <p>Which one of the following statements is<strong> <span style="color: #169179;"><strong>TRUE</strong></span> </strong> of Michaelis-Menten kinetics?</p> A.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that there is no substrate available and there is no measureable reverse <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect B.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the <strong><span style="color: #ff0000;">concentration</span></strong> of <strong><span style="color: #ff5e00;">enzyme-product complex [EP]</span></strong> is <strong><span style="color: #6d108e;"><i>constant</i></span></strong>. Incorrect C.<strong> </strong><strong><span style="color: #0d57a5;"><strong><span style="color: #0d57a5;">M-M kinetics</span></strong></span></strong> was developed by German biochemist Leonor Michaelis and Canadian physician Maud Menten in 1913. Correct D.<strong> </strong>When the substrate <strong><span style="color: #ff0000;">concentration</span></strong>, [S], is much larger than K<sub>M</sub>, the <strong><span style="color: #a1005e;">reaction rate</span></strong> is linear. Incorrect E.<strong> </strong>The <strong><span style="color: #a1005e;">reaction rate</span></strong> is <strong><span style="color: #009e4c;"><i>proportional</i></span></strong> to the product <strong><span style="color: #ff0000;">concentration</span></strong>. Incorrect MC <p>93ac</p> <p>Which one of the following statements is<strong> <span style="color: #ba372a;"><strong>FALSE</strong></span> </strong> concerning Michaelis-Menten kinetics?</p> A.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> was developed by German biochemist Leonor Michaelis and Canadian physician Maud Menten in 1913. Incorrect B.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the enzyme bound to the product [EP] is short lived and does<strong> <strong>NOT</strong> </strong>contribute to the <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect C.<strong> </strong><strong><span style="color: #0d57a5;"><strong><span style="color: #0d57a5;">M-M kinetics</span></strong></span></strong> assumes that the substrate is<strong> <strong>NOT</strong> </strong>available and there is no measureable reverse <strong><span style="color: #a1005e;"><strong><span style="color: #a1005e;">reaction rate</span></strong></span></strong>. Correct D.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes a quasi-steady state, that the <strong><span style="color: #2fbd0f;">enzyme-substrate complex [ES]</span></strong> is <strong><span style="color: #6d108e;"><i>constant</i></span></strong>. Incorrect E.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes the enzyme has a single active site. Incorrect MC <p>94aa</p> <p>Which one of the following statements is<strong> <span style="color: #169179;"><strong>TRUE</strong></span> </strong> of Michaelis-Menten kinetics?</p> A.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the rate of breaking the <strong><span style="color: #ff5e00;">enzyme-product complex [EP]</span></strong> is equal to the rate of its formation. Incorrect B.<strong> </strong>The <strong><span style="color: #a1005e;">reaction rate</span></strong> is <strong><span style="color: #009e4c;"><i>proportional</i></span></strong> to the product <strong><span style="color: #ff0000;">concentration</span></strong>. Incorrect C.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that there is no substrate available and there is no measureable reverse <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect D.<strong> </strong>When the substrate <strong><span style="color: #ff0000;"><strong><span style="color: #ff0000;">concentration</span></strong></span></strong>, [S], is much smaller than K<sub>M</sub>, the <strong><span style="color: #a1005e;"><strong><span style="color: #a1005e;">reaction rate</span></strong></span></strong> is linear. Correct E.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> was developed by Greek economist Leo Michelis and Dutch bobsledder Hubert Menten in 1913. Incorrect MC <p>955f</p> <p>Which one of the following statements is<strong> <span style="color: #169179;"><strong>TRUE</strong></span> </strong> of Michaelis-Menten kinetics?</p> A.<strong> </strong>The <strong><span style="color: #a1005e;">reaction rate</span></strong> is <strong><span style="color: #009e4c;"><i>proportional</i></span></strong> to the product <strong><span style="color: #ff0000;">concentration</span></strong>. Incorrect B.<strong> </strong><strong><span style="color: #0d57a5;"><strong><span style="color: #0d57a5;">M-M kinetics</span></strong></span></strong> assumes that the product is<strong> <strong>NOT</strong> </strong>available and there is no measureable reverse <strong><span style="color: #a1005e;"><strong><span style="color: #a1005e;">reaction rate</span></strong></span></strong>. Correct C.<strong> </strong>When the substrate <strong><span style="color: #ff0000;">concentration</span></strong>, [S], is much smaller than K<sub>M</sub>, the <strong><span style="color: #a1005e;">reaction rate</span></strong> is <strong><span style="color: #6d108e;"><i>constant</i></span></strong>. Incorrect D.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the <strong><span style="color: #2fbd0f;">enzyme-substrate complex [ES]</span></strong> is short lived and does<strong> <strong>NOT</strong> </strong>contribute to the <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect E.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> was developed by American linguist Laura Michaelis and Belgian cyclist Milan Menten in 1913. Incorrect MC <p>9566</p> <p>Which one of the following statements is<strong> <span style="color: #ba372a;"><strong>FALSE</strong></span> </strong> about Michaelis-Menten kinetics?</p> A.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the <strong><span style="color: #ff5e00;">enzyme-product complex [EP]</span></strong> is short lived and does<strong> <strong>NOT</strong> </strong>contribute to the <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect B.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> was developed by German biochemist Leonor Michaelis and Canadian physician Maud Menten in 1913. Incorrect C.<strong> </strong>The <strong><span style="color: #a1005e;">reaction rate</span></strong> is <strong><span style="color: #009e4c;"><i>proportional</i></span></strong> to the substrate <strong><span style="color: #ff0000;">concentration</span></strong>. Incorrect D.<strong> </strong><strong><span style="color: #0d57a5;"><strong><span style="color: #0d57a5;">M-M kinetics</span></strong></span></strong> assumes that there is no substrate available and there is no measureable reverse <strong><span style="color: #a1005e;"><strong><span style="color: #a1005e;">reaction rate</span></strong></span></strong>. Correct E.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the <strong><span style="color: #ff0000;">concentration</span></strong> of <strong><span style="color: #2fbd0f;">enzyme-substrate complex [ES]</span></strong> is <strong><span style="color: #6d108e;"><i>constant</i></span></strong>. Incorrect MC <p>977a</p> <p>Which one of the following statements is<strong> <span style="color: #169179;"><strong>TRUE</strong></span> </strong> regarding Michaelis-Menten kinetics?</p> A.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that there is no substrate available and there is no measureable reverse <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect B.<strong> </strong>When the substrate <strong><span style="color: #ff0000;">concentration</span></strong>, [S], is much larger than K<sub>M</sub>, the <strong><span style="color: #a1005e;">reaction rate</span></strong> is linear. Incorrect C.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the <strong><span style="color: #ff0000;">concentration</span></strong> of <strong><span style="color: #ff5e00;">enzyme-product complex [EP]</span></strong> is <strong><span style="color: #6d108e;"><i>constant</i></span></strong>. Incorrect D.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the <strong><span style="color: #2fbd0f;">enzyme-substrate complex [ES]</span></strong> is short lived and does<strong> <strong>NOT</strong> </strong>contribute to the <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect E.<strong> </strong>The <strong><span style="color: #a1005e;"><strong><span style="color: #a1005e;">reaction rate</span></strong></span></strong> is <strong><span style="color: #009e4c;"><i><strong><span style="color: #009e4c;"><i>proportional</i></span></strong></i></span></strong> to the substrate <strong><span style="color: #ff0000;"><strong><span style="color: #ff0000;">concentration</span></strong></span></strong>. Correct MC <p>9848</p> <p>Which one of the following statements is<strong> <span style="color: #169179;"><strong>TRUE</strong></span> </strong> of Michaelis-Menten kinetics?</p> A.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the rate of breaking the <strong><span style="color: #ff5e00;">enzyme-product complex [EP]</span></strong> is equal to the rate of its formation. Incorrect B.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the substrate is<strong> <strong>NOT</strong> </strong>available and there is no measureable reverse <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect C.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the enzyme bound to the substrate [ES] is short lived and does<strong> <strong>NOT</strong> </strong>contribute to the <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect D.<strong> </strong>When the substrate <strong><span style="color: #ff0000;"><strong><span style="color: #ff0000;">concentration</span></strong></span></strong>, [S], is much smaller than K<sub>M</sub>, the <strong><span style="color: #a1005e;"><strong><span style="color: #a1005e;">reaction rate</span></strong></span></strong> is linear. Correct E.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> was developed by Greek economist Leo Michelis and Dutch bobsledder Hubert Menten in 1913. Incorrect MC <p>9ad1</p> <p>Which one of the following statements is<strong> <span style="color: #ba372a;"><strong>FALSE</strong></span> </strong> concerning Michaelis-Menten kinetics?</p> A.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes the enzyme has a single active site. Incorrect B.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the <strong><span style="color: #ff5e00;">enzyme-product complex [EP]</span></strong> is short lived and does<strong> <strong>NOT</strong> </strong>contribute to the <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect C.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes a quasi-steady state, that the <strong><span style="color: #2fbd0f;">enzyme-substrate complex [ES]</span></strong> is <strong><span style="color: #6d108e;"><i>constant</i></span></strong>. Incorrect D.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> was developed by German biochemist Leonor Michaelis and Canadian physician Maud Menten in 1913. Incorrect E.<strong> </strong><strong><span style="color: #0d57a5;"><strong><span style="color: #0d57a5;">M-M kinetics</span></strong></span></strong> assumes that there is no substrate available and there is no measureable reverse <strong><span style="color: #a1005e;"><strong><span style="color: #a1005e;">reaction rate</span></strong></span></strong>. Correct MC <p>9c6a</p> <p>Which one of the following statements is<strong> <span style="color: #ba372a;"><strong>FALSE</strong></span> </strong> about Michaelis-Menten kinetics?</p> A.<strong> </strong><strong><span style="color: #0d57a5;"><strong><span style="color: #0d57a5;">M-M kinetics</span></strong></span></strong> assumes that the enzyme bound to the substrate [ES] is short lived and does<strong> <strong>NOT</strong> </strong>contribute to the <strong><span style="color: #a1005e;"><strong><span style="color: #a1005e;">reaction rate</span></strong></span></strong>. Correct B.<strong> </strong>When the substrate <strong><span style="color: #ff0000;">concentration</span></strong>, [S], is much larger than K<sub>M</sub>, the <strong><span style="color: #a1005e;">reaction rate</span></strong> is <strong><span style="color: #6d108e;"><i>constant</i></span></strong>. Incorrect C.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> was developed by German biochemist Leonor Michaelis and Canadian physician Maud Menten in 1913. Incorrect D.<strong> </strong>The <strong><span style="color: #a1005e;">reaction rate</span></strong> is <strong><span style="color: #009e4c;"><i>proportional</i></span></strong> to the substrate <strong><span style="color: #ff0000;">concentration</span></strong>. Incorrect E.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that there is no product available and there is no measureable reverse <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect MC <p>9dd7</p> <p>Which one of the following statements is<strong> <span style="color: #ba372a;"><strong>FALSE</strong></span> </strong> about Michaelis-Menten kinetics?</p> A.<strong> </strong><strong><span style="color: #0d57a5;"><strong><span style="color: #0d57a5;">M-M kinetics</span></strong></span></strong> assumes that the <strong><span style="color: #2fbd0f;"><strong><span style="color: #2fbd0f;">enzyme-substrate complex [ES]</span></strong></span></strong> is short lived and does<strong> <strong>NOT</strong> </strong>contribute to the <strong><span style="color: #a1005e;"><strong><span style="color: #a1005e;">reaction rate</span></strong></span></strong>. Correct B.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes the enzyme has a single active site. Incorrect C.<strong> </strong>When the substrate <strong><span style="color: #ff0000;">concentration</span></strong>, [S], is much smaller than K<sub>M</sub>, the <strong><span style="color: #a1005e;">reaction rate</span></strong> is linear. Incorrect D.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> was developed by German biochemist Leonor Michaelis and Canadian physician Maud Menten in 1913. Incorrect E.<strong> </strong>The <strong><span style="color: #a1005e;">reaction rate</span></strong> is <strong><span style="color: #009e4c;"><i>proportional</i></span></strong> to the substrate <strong><span style="color: #ff0000;">concentration</span></strong>. Incorrect MC <p>9ea4</p> <p>Which one of the following statements is<strong> <span style="color: #ba372a;"><strong>FALSE</strong></span> </strong> about Michaelis-Menten kinetics?</p> A.<strong> </strong>The <strong><span style="color: #a1005e;">reaction rate</span></strong> is <strong><span style="color: #009e4c;"><i>proportional</i></span></strong> to the substrate <strong><span style="color: #ff0000;">concentration</span></strong>. Incorrect B.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that there is no product available and there is no measureable reverse <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect C.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> does<strong> <strong>NOT</strong> </strong>apply to allosteric enzymes. Incorrect D.<strong> </strong><strong><span style="color: #0d57a5;"><strong><span style="color: #0d57a5;">M-M kinetics</span></strong></span></strong> assumes that the <strong><span style="color: #ff0000;"><strong><span style="color: #ff0000;">concentration</span></strong></span></strong> of <strong><span style="color: #ff5e00;"><strong><span style="color: #ff5e00;">enzyme-product complex [EP]</span></strong></span></strong> is <strong><span style="color: #6d108e;"><i><strong><span style="color: #6d108e;"><i>constant</i></span></strong></i></span></strong>. Correct E.<strong> </strong>When the substrate <strong><span style="color: #ff0000;">concentration</span></strong>, [S], is much larger than K<sub>M</sub>, the <strong><span style="color: #a1005e;">reaction rate</span></strong> is <strong><span style="color: #6d108e;"><i>constant</i></span></strong>. Incorrect MC <p>9fb3</p> <p>Which one of the following statements is<strong> <span style="color: #ba372a;"><strong>FALSE</strong></span> </strong> concerning Michaelis-Menten kinetics?</p> A.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> does<strong> <strong>NOT</strong> </strong>apply to allosteric enzymes. Incorrect B.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the enzyme bound to the product [EP] is short lived and does<strong> <strong>NOT</strong> </strong>contribute to the <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect C.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> was developed by German biochemist Leonor Michaelis and Canadian physician Maud Menten in 1913. Incorrect D.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes a quasi-steady state, that the <strong><span style="color: #2fbd0f;">enzyme-substrate complex [ES]</span></strong> is <strong><span style="color: #6d108e;"><i>constant</i></span></strong>. Incorrect E.<strong> </strong>The <strong><span style="color: #a1005e;"><strong><span style="color: #a1005e;">reaction rate</span></strong></span></strong> is <strong><span style="color: #009e4c;"><i><strong><span style="color: #009e4c;"><i>proportional</i></span></strong></i></span></strong> to the product <strong><span style="color: #ff0000;"><strong><span style="color: #ff0000;">concentration</span></strong></span></strong>. Correct MC <p>a1ad</p> <p>Which one of the following statements is<strong> <span style="color: #169179;"><strong>TRUE</strong></span> </strong> regarding Michaelis-Menten kinetics?</p> A.<strong> </strong>When the substrate <strong><span style="color: #ff0000;">concentration</span></strong>, [S], is much smaller than K<sub>M</sub>, the <strong><span style="color: #a1005e;">reaction rate</span></strong> is <strong><span style="color: #6d108e;"><i>constant</i></span></strong>. Incorrect B.<strong> </strong><strong><span style="color: #0d57a5;"><strong><span style="color: #0d57a5;">M-M kinetics</span></strong></span></strong> assumes that the change in <strong><span style="color: #ff0000;"><strong><span style="color: #ff0000;">concentration</span></strong></span></strong> of <strong><span style="color: #2fbd0f;"><strong><span style="color: #2fbd0f;">enzyme-substrate complex [ES]</span></strong></span></strong> does<strong> <strong>NOT</strong> </strong>change. Correct C.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that there is no substrate available and there is no measureable reverse <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect D.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> was developed by American linguist Laura Michaelis and Belgian cyclist Milan Menten in 1913. Incorrect E.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the enzyme bound to the substrate [ES] is short lived and does<strong> <strong>NOT</strong> </strong>contribute to the <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect MC <p>a27c</p> <p>Which one of the following statements is<strong> <span style="color: #ba372a;"><strong>FALSE</strong></span> </strong> concerning Michaelis-Menten kinetics?</p> A.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the enzyme bound to the product [EP] is short lived and does<strong> <strong>NOT</strong> </strong>contribute to the <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect B.<strong> </strong>The <strong><span style="color: #a1005e;">reaction rate</span></strong> is <strong><span style="color: #009e4c;"><i>proportional</i></span></strong> to the substrate <strong><span style="color: #ff0000;">concentration</span></strong>. Incorrect C.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the <strong><span style="color: #ff0000;">concentration</span></strong> of <strong><span style="color: #2fbd0f;">enzyme-substrate complex [ES]</span></strong> is <strong><span style="color: #6d108e;"><i>constant</i></span></strong>. Incorrect D.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes the enzyme has a single active site. Incorrect E.<strong> </strong><strong><span style="color: #0d57a5;"><strong><span style="color: #0d57a5;">M-M kinetics</span></strong></span></strong> assumes that there is no substrate available and there is no measureable reverse <strong><span style="color: #a1005e;"><strong><span style="color: #a1005e;">reaction rate</span></strong></span></strong>. Correct MC <p>a30e</p> <p>Which one of the following statements is<strong> <span style="color: #169179;"><strong>TRUE</strong></span> </strong> regarding Michaelis-Menten kinetics?</p> A.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the rate of breaking the <strong><span style="color: #ff5e00;">enzyme-product complex [EP]</span></strong> is equal to the rate of its formation. Incorrect B.<strong> </strong><strong><span style="color: #0d57a5;"><strong><span style="color: #0d57a5;">M-M kinetics</span></strong></span></strong> assumes that there is no product available and there is no measureable reverse <strong><span style="color: #a1005e;"><strong><span style="color: #a1005e;">reaction rate</span></strong></span></strong>. Correct C.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> was developed by Greek economist Leo Michelis and Dutch bobsledder Hubert Menten in 1913. Incorrect D.<strong> </strong>When the substrate <strong><span style="color: #ff0000;">concentration</span></strong>, [S], is much smaller than K<sub>M</sub>, the <strong><span style="color: #a1005e;">reaction rate</span></strong> is <strong><span style="color: #6d108e;"><i>constant</i></span></strong>. Incorrect E.<strong> </strong>The <strong><span style="color: #a1005e;">reaction rate</span></strong> is <strong><span style="color: #009e4c;"><i>proportional</i></span></strong> to the product <strong><span style="color: #ff0000;">concentration</span></strong>. Incorrect MC <p>a5f0</p> <p>Which one of the following statements is<strong> <span style="color: #169179;"><strong>TRUE</strong></span> </strong> of Michaelis-Menten kinetics?</p> A.<strong> </strong><strong><span style="color: #0d57a5;"><strong><span style="color: #0d57a5;">M-M kinetics</span></strong></span></strong> assumes that the enzyme bound to the product [EP] is short lived and does<strong> <strong>NOT</strong> </strong>contribute to the <strong><span style="color: #a1005e;"><strong><span style="color: #a1005e;">reaction rate</span></strong></span></strong>. Correct B.<strong> </strong>When the substrate <strong><span style="color: #ff0000;">concentration</span></strong>, [S], is much smaller than K<sub>M</sub>, the <strong><span style="color: #a1005e;">reaction rate</span></strong> is <strong><span style="color: #6d108e;"><i>constant</i></span></strong>. Incorrect C.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that there is no substrate available and there is no measureable reverse <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect D.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> was developed by Greek economist Leo Michelis and Dutch bobsledder Hubert Menten in 1913. Incorrect E.<strong> </strong>The <strong><span style="color: #a1005e;">reaction rate</span></strong> is <strong><span style="color: #009e4c;"><i>proportional</i></span></strong> to the product <strong><span style="color: #ff0000;">concentration</span></strong>. Incorrect MC <p>ac95</p> <p>Which one of the following statements is<strong> <span style="color: #169179;"><strong>TRUE</strong></span> </strong> of Michaelis-Menten kinetics?</p> A.<strong> </strong>The <strong><span style="color: #a1005e;">reaction rate</span></strong> is <strong><span style="color: #009e4c;"><i>proportional</i></span></strong> to the product <strong><span style="color: #ff0000;">concentration</span></strong>. Incorrect B.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that there is no substrate available and there is no measureable reverse <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect C.<strong> </strong><strong><span style="color: #0d57a5;"><strong><span style="color: #0d57a5;">M-M kinetics</span></strong></span></strong> assumes that the <strong><span style="color: #ff0000;"><strong><span style="color: #ff0000;">concentration</span></strong></span></strong> of <strong><span style="color: #2fbd0f;"><strong><span style="color: #2fbd0f;">enzyme-substrate complex [ES]</span></strong></span></strong> is <strong><span style="color: #6d108e;"><i><strong><span style="color: #6d108e;"><i>constant</i></span></strong></i></span></strong>. Correct D.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> was developed by Greek economist Leo Michelis and Dutch bobsledder Hubert Menten in 1913. Incorrect E.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the enzyme bound to the substrate [ES] is short lived and does<strong> <strong>NOT</strong> </strong>contribute to the <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect MC <p>b176</p> <p>Which one of the following statements is<strong> <span style="color: #ba372a;"><strong>FALSE</strong></span> </strong> concerning Michaelis-Menten kinetics?</p> A.<strong> </strong>The <strong><span style="color: #a1005e;">reaction rate</span></strong> is <strong><span style="color: #009e4c;"><i>proportional</i></span></strong> to the substrate <strong><span style="color: #ff0000;">concentration</span></strong>. Incorrect B.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the rate of breaking the <strong><span style="color: #2fbd0f;">enzyme-substrate complex [ES]</span></strong> is equal to the rate of its formation. Incorrect C.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> was developed by German biochemist Leonor Michaelis and Canadian physician Maud Menten in 1913. Incorrect D.<strong> </strong><strong><span style="color: #0d57a5;"><strong><span style="color: #0d57a5;">M-M kinetics</span></strong></span></strong> assumes that there is no substrate available and there is no measureable reverse <strong><span style="color: #a1005e;"><strong><span style="color: #a1005e;">reaction rate</span></strong></span></strong>. Correct E.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes the enzyme has a single active site. Incorrect MC <p>b1a4</p> <p>Which one of the following statements is<strong> <span style="color: #ba372a;"><strong>FALSE</strong></span> </strong> about Michaelis-Menten kinetics?</p> A.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> was developed by German biochemist Leonor Michaelis and Canadian physician Maud Menten in 1913. Incorrect B.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the enzyme bound to the product [EP] is short lived and does<strong> <strong>NOT</strong> </strong>contribute to the <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect C.<strong> </strong>When the substrate <strong><span style="color: #ff0000;"><strong><span style="color: #ff0000;">concentration</span></strong></span></strong>, [S], is much smaller than K<sub>M</sub>, the <strong><span style="color: #a1005e;"><strong><span style="color: #a1005e;">reaction rate</span></strong></span></strong> is <strong><span style="color: #6d108e;"><i><strong><span style="color: #6d108e;"><i>constant</i></span></strong></i></span></strong>. Correct D.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> does<strong> <strong>NOT</strong> </strong>apply to allosteric enzymes. Incorrect E.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the product is<strong> <strong>NOT</strong> </strong>available and there is no measureable reverse <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect MC <p>b509</p> <p>Which one of the following statements is<strong> <span style="color: #ba372a;"><strong>FALSE</strong></span> </strong> about Michaelis-Menten kinetics?</p> A.<strong> </strong>The <strong><span style="color: #a1005e;"><strong><span style="color: #a1005e;">reaction rate</span></strong></span></strong> is <strong><span style="color: #009e4c;"><i><strong><span style="color: #009e4c;"><i>proportional</i></span></strong></i></span></strong> to the product <strong><span style="color: #ff0000;"><strong><span style="color: #ff0000;">concentration</span></strong></span></strong>. Correct B.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the <strong><span style="color: #ff5e00;">enzyme-product complex [EP]</span></strong> is short lived and does<strong> <strong>NOT</strong> </strong>contribute to the <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect C.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> was developed by German biochemist Leonor Michaelis and Canadian physician Maud Menten in 1913. Incorrect D.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the rate of breaking the <strong><span style="color: #2fbd0f;">enzyme-substrate complex [ES]</span></strong> is equal to the rate of its formation. Incorrect E.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> does<strong> <strong>NOT</strong> </strong>apply to allosteric enzymes. Incorrect MC <p>bb11</p> <p>Which one of the following statements is<strong> <span style="color: #169179;"><strong>TRUE</strong></span> </strong> regarding Michaelis-Menten kinetics?</p> A.<strong> </strong><strong><span style="color: #0d57a5;"><strong><span style="color: #0d57a5;">M-M kinetics</span></strong></span></strong> assumes that the change in <strong><span style="color: #ff0000;"><strong><span style="color: #ff0000;">concentration</span></strong></span></strong> of <strong><span style="color: #2fbd0f;"><strong><span style="color: #2fbd0f;">enzyme-substrate complex [ES]</span></strong></span></strong> does<strong> <strong>NOT</strong> </strong>change. Correct B.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> was developed by American linguist Laura Michaelis and Belgian cyclist Milan Menten in 1913. Incorrect C.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that there is no substrate available and there is no measureable reverse <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect D.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the enzyme bound to the substrate [ES] is short lived and does<strong> <strong>NOT</strong> </strong>contribute to the <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect E.<strong> </strong>The <strong><span style="color: #a1005e;">reaction rate</span></strong> is <strong><span style="color: #009e4c;"><i>proportional</i></span></strong> to the product <strong><span style="color: #ff0000;">concentration</span></strong>. Incorrect MC <p>bbf2</p> <p>Which one of the following statements is<strong> <span style="color: #ba372a;"><strong>FALSE</strong></span> </strong> about Michaelis-Menten kinetics?</p> A.<strong> </strong>The <strong><span style="color: #a1005e;">reaction rate</span></strong> is <strong><span style="color: #009e4c;"><i>proportional</i></span></strong> to the substrate <strong><span style="color: #ff0000;">concentration</span></strong>. Incorrect B.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> was developed by German biochemist Leonor Michaelis and Canadian physician Maud Menten in 1913. Incorrect C.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes the enzyme has a single active site. Incorrect D.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the <strong><span style="color: #ff5e00;">enzyme-product complex [EP]</span></strong> is short lived and does<strong> <strong>NOT</strong> </strong>contribute to the <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect E.<strong> </strong><strong><span style="color: #0d57a5;"><strong><span style="color: #0d57a5;">M-M kinetics</span></strong></span></strong> assumes that the <strong><span style="color: #ff5e00;"><strong><span style="color: #ff5e00;">enzyme-product complex [EP]</span></strong></span></strong> is <strong><span style="color: #6d108e;"><i><strong><span style="color: #6d108e;"><i>constant</i></span></strong></i></span></strong>. Correct MC <p>bfbb</p> <p>Which one of the following statements is<strong> <span style="color: #169179;"><strong>TRUE</strong></span> </strong> of Michaelis-Menten kinetics?</p> A.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the enzyme bound to the substrate [ES] is short lived and does<strong> <strong>NOT</strong> </strong>contribute to the <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect B.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> was developed by American linguist Laura Michaelis and Belgian cyclist Milan Menten in 1913. Incorrect C.<strong> </strong><strong><span style="color: #0d57a5;"><strong><span style="color: #0d57a5;">M-M kinetics</span></strong></span></strong> assumes that the product is<strong> <strong>NOT</strong> </strong>available and there is no measureable reverse <strong><span style="color: #a1005e;"><strong><span style="color: #a1005e;">reaction rate</span></strong></span></strong>. Correct D.<strong> </strong>When the substrate <strong><span style="color: #ff0000;">concentration</span></strong>, [S], is much smaller than K<sub>M</sub>, the <strong><span style="color: #a1005e;">reaction rate</span></strong> is <strong><span style="color: #6d108e;"><i>constant</i></span></strong>. Incorrect E.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the rate of breaking the <strong><span style="color: #ff5e00;">enzyme-product complex [EP]</span></strong> is equal to the rate of its formation. Incorrect MC <p>c302</p> <p>Which one of the following statements is<strong> <span style="color: #ba372a;"><strong>FALSE</strong></span> </strong> about Michaelis-Menten kinetics?</p> A.<strong> </strong><strong><span style="color: #0d57a5;"><strong><span style="color: #0d57a5;">M-M kinetics</span></strong></span></strong> assumes that the rate of breaking the <strong><span style="color: #ff5e00;"><strong><span style="color: #ff5e00;">enzyme-product complex [EP]</span></strong></span></strong> is equal to the rate of its formation. Correct B.<strong> </strong>When the substrate <strong><span style="color: #ff0000;">concentration</span></strong>, [S], is much smaller than K<sub>M</sub>, the <strong><span style="color: #a1005e;">reaction rate</span></strong> is linear. Incorrect C.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that there is no product available and there is no measureable reverse <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect D.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the <strong><span style="color: #ff5e00;">enzyme-product complex [EP]</span></strong> is short lived and does<strong> <strong>NOT</strong> </strong>contribute to the <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect E.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> was developed by German biochemist Leonor Michaelis and Canadian physician Maud Menten in 1913. Incorrect MC <p>c33f</p> <p>Which one of the following statements is<strong> <span style="color: #ba372a;"><strong>FALSE</strong></span> </strong> about Michaelis-Menten kinetics?</p> A.<strong> </strong>The <strong><span style="color: #a1005e;">reaction rate</span></strong> is <strong><span style="color: #009e4c;"><i>proportional</i></span></strong> to the substrate <strong><span style="color: #ff0000;">concentration</span></strong>. Incorrect B.<strong> </strong><strong><span style="color: #0d57a5;"><strong><span style="color: #0d57a5;">M-M kinetics</span></strong></span></strong> assumes that the <strong><span style="color: #ff0000;"><strong><span style="color: #ff0000;">concentration</span></strong></span></strong> of <strong><span style="color: #ff5e00;"><strong><span style="color: #ff5e00;">enzyme-product complex [EP]</span></strong></span></strong> is <strong><span style="color: #6d108e;"><i><strong><span style="color: #6d108e;"><i>constant</i></span></strong></i></span></strong>. Correct C.<strong> </strong>When the substrate <strong><span style="color: #ff0000;">concentration</span></strong>, [S], is much larger than K<sub>M</sub>, the <strong><span style="color: #a1005e;">reaction rate</span></strong> is <strong><span style="color: #6d108e;"><i>constant</i></span></strong>. Incorrect D.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the product is<strong> <strong>NOT</strong> </strong>available and there is no measureable reverse <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect E.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> was developed by German biochemist Leonor Michaelis and Canadian physician Maud Menten in 1913. Incorrect MC <p>c7a8</p> <p>Which one of the following statements is<strong> <span style="color: #ba372a;"><strong>FALSE</strong></span> </strong> concerning Michaelis-Menten kinetics?</p> A.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that there is no product available and there is no measureable reverse <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect B.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the <strong><span style="color: #ff5e00;">enzyme-product complex [EP]</span></strong> is short lived and does<strong> <strong>NOT</strong> </strong>contribute to the <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect C.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the <strong><span style="color: #ff0000;">concentration</span></strong> of <strong><span style="color: #2fbd0f;">enzyme-substrate complex [ES]</span></strong> is <strong><span style="color: #6d108e;"><i>constant</i></span></strong>. Incorrect D.<strong> </strong><strong><span style="color: #0d57a5;"><strong><span style="color: #0d57a5;">M-M kinetics</span></strong></span></strong> was developed by American linguist Laura Michaelis and Belgian cyclist Milan Menten in 1913. Correct E.<strong> </strong>When the substrate <strong><span style="color: #ff0000;">concentration</span></strong>, [S], is much smaller than K<sub>M</sub>, the <strong><span style="color: #a1005e;">reaction rate</span></strong> is linear. Incorrect MC <p>caa9</p> <p>Which one of the following statements is<strong> <span style="color: #169179;"><strong>TRUE</strong></span> </strong> regarding Michaelis-Menten kinetics?</p> A.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> was developed by American linguist Laura Michaelis and Belgian cyclist Milan Menten in 1913. Incorrect B.<strong> </strong><strong><span style="color: #0d57a5;"><strong><span style="color: #0d57a5;">M-M kinetics</span></strong></span></strong> does<strong> <strong>NOT</strong> </strong>apply to allosteric enzymes. Correct C.<strong> </strong>The <strong><span style="color: #a1005e;">reaction rate</span></strong> is <strong><span style="color: #009e4c;"><i>proportional</i></span></strong> to the product <strong><span style="color: #ff0000;">concentration</span></strong>. Incorrect D.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the substrate is<strong> <strong>NOT</strong> </strong>available and there is no measureable reverse <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect E.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the <strong><span style="color: #2fbd0f;">enzyme-substrate complex [ES]</span></strong> is short lived and does<strong> <strong>NOT</strong> </strong>contribute to the <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect MC <p>cc26</p> <p>Which one of the following statements is<strong> <span style="color: #ba372a;"><strong>FALSE</strong></span> </strong> concerning Michaelis-Menten kinetics?</p> A.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that there is no product available and there is no measureable reverse <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect B.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> was developed by German biochemist Leonor Michaelis and Canadian physician Maud Menten in 1913. Incorrect C.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes the enzyme has a single active site. Incorrect D.<strong> </strong><strong><span style="color: #0d57a5;"><strong><span style="color: #0d57a5;">M-M kinetics</span></strong></span></strong> assumes that the rate of breaking the <strong><span style="color: #ff5e00;"><strong><span style="color: #ff5e00;">enzyme-product complex [EP]</span></strong></span></strong> is equal to the rate of its formation. Correct E.<strong> </strong>The <strong><span style="color: #a1005e;">reaction rate</span></strong> is <strong><span style="color: #009e4c;"><i>proportional</i></span></strong> to the substrate <strong><span style="color: #ff0000;">concentration</span></strong>. Incorrect MC <p>cecf</p> <p>Which one of the following statements is<strong> <span style="color: #169179;"><strong>TRUE</strong></span> </strong> regarding Michaelis-Menten kinetics?</p> A.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that there is no substrate available and there is no measureable reverse <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect B.<strong> </strong>The <strong><span style="color: #a1005e;">reaction rate</span></strong> is <strong><span style="color: #009e4c;"><i>proportional</i></span></strong> to the product <strong><span style="color: #ff0000;">concentration</span></strong>. Incorrect C.<strong> </strong><strong><span style="color: #0d57a5;"><strong><span style="color: #0d57a5;">M-M kinetics</span></strong></span></strong> assumes that the <strong><span style="color: #ff5e00;"><strong><span style="color: #ff5e00;">enzyme-product complex [EP]</span></strong></span></strong> is short lived and does<strong> <strong>NOT</strong> </strong>contribute to the <strong><span style="color: #a1005e;"><strong><span style="color: #a1005e;">reaction rate</span></strong></span></strong>. Correct D.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> was developed by American linguist Laura Michaelis and Belgian cyclist Milan Menten in 1913. Incorrect E.<strong> </strong>When the substrate <strong><span style="color: #ff0000;">concentration</span></strong>, [S], is much larger than K<sub>M</sub>, the <strong><span style="color: #a1005e;">reaction rate</span></strong> is linear. Incorrect MC <p>d146</p> <p>Which one of the following statements is<strong> <span style="color: #ba372a;"><strong>FALSE</strong></span> </strong> about Michaelis-Menten kinetics?</p> A.<strong> </strong>When the substrate <strong><span style="color: #ff0000;"><strong><span style="color: #ff0000;">concentration</span></strong></span></strong>, [S], is much larger than K<sub>M</sub>, the <strong><span style="color: #a1005e;"><strong><span style="color: #a1005e;">reaction rate</span></strong></span></strong> is linear. Correct B.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that there is no product available and there is no measureable reverse <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect C.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> does<strong> <strong>NOT</strong> </strong>apply to allosteric enzymes. Incorrect D.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the enzyme bound to the product [EP] is short lived and does<strong> <strong>NOT</strong> </strong>contribute to the <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect E.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes a quasi-steady state, that the <strong><span style="color: #2fbd0f;">enzyme-substrate complex [ES]</span></strong> is <strong><span style="color: #6d108e;"><i>constant</i></span></strong>. Incorrect MC <p>d1e4</p> <p>Which one of the following statements is<strong> <span style="color: #ba372a;"><strong>FALSE</strong></span> </strong> concerning Michaelis-Menten kinetics?</p> A.<strong> </strong>When the substrate <strong><span style="color: #ff0000;">concentration</span></strong>, [S], is much smaller than K<sub>M</sub>, the <strong><span style="color: #a1005e;">reaction rate</span></strong> is linear. Incorrect B.<strong> </strong><strong><span style="color: #0d57a5;"><strong><span style="color: #0d57a5;">M-M kinetics</span></strong></span></strong> assumes that the <strong><span style="color: #ff0000;"><strong><span style="color: #ff0000;">concentration</span></strong></span></strong> of <strong><span style="color: #ff5e00;"><strong><span style="color: #ff5e00;">enzyme-product complex [EP]</span></strong></span></strong> is <strong><span style="color: #6d108e;"><i><strong><span style="color: #6d108e;"><i>constant</i></span></strong></i></span></strong>. Correct C.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> was developed by German biochemist Leonor Michaelis and Canadian physician Maud Menten in 1913. Incorrect D.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes the enzyme has a single active site. Incorrect E.<strong> </strong>The <strong><span style="color: #a1005e;">reaction rate</span></strong> is <strong><span style="color: #009e4c;"><i>proportional</i></span></strong> to the substrate <strong><span style="color: #ff0000;">concentration</span></strong>. Incorrect MC <p>d764</p> <p>Which one of the following statements is<strong> <span style="color: #ba372a;"><strong>FALSE</strong></span> </strong> about Michaelis-Menten kinetics?</p> A.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> does<strong> <strong>NOT</strong> </strong>apply to allosteric enzymes. Incorrect B.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> was developed by German biochemist Leonor Michaelis and Canadian physician Maud Menten in 1913. Incorrect C.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that there is no product available and there is no measureable reverse <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect D.<strong> </strong>The <strong><span style="color: #a1005e;"><strong><span style="color: #a1005e;">reaction rate</span></strong></span></strong> is <strong><span style="color: #009e4c;"><i><strong><span style="color: #009e4c;"><i>proportional</i></span></strong></i></span></strong> to the product <strong><span style="color: #ff0000;"><strong><span style="color: #ff0000;">concentration</span></strong></span></strong>. Correct E.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the change in <strong><span style="color: #ff0000;">concentration</span></strong> of <strong><span style="color: #2fbd0f;">enzyme-substrate complex [ES]</span></strong> does<strong> <strong>NOT</strong> </strong>change. Incorrect MC <p>d8e2</p> <p>Which one of the following statements is<strong> <span style="color: #ba372a;"><strong>FALSE</strong></span> </strong> about Michaelis-Menten kinetics?</p> A.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> was developed by German biochemist Leonor Michaelis and Canadian physician Maud Menten in 1913. Incorrect B.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the rate of breaking the <strong><span style="color: #2fbd0f;">enzyme-substrate complex [ES]</span></strong> is equal to the rate of its formation. Incorrect C.<strong> </strong>When the substrate <strong><span style="color: #ff0000;">concentration</span></strong>, [S], is much smaller than K<sub>M</sub>, the <strong><span style="color: #a1005e;">reaction rate</span></strong> is linear. Incorrect D.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that there is no product available and there is no measureable reverse <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect E.<strong> </strong><strong><span style="color: #0d57a5;"><strong><span style="color: #0d57a5;">M-M kinetics</span></strong></span></strong> assumes that the <strong><span style="color: #2fbd0f;"><strong><span style="color: #2fbd0f;">enzyme-substrate complex [ES]</span></strong></span></strong> is short lived and does<strong> <strong>NOT</strong> </strong>contribute to the <strong><span style="color: #a1005e;"><strong><span style="color: #a1005e;">reaction rate</span></strong></span></strong>. Correct MC <p>d911</p> <p>Which one of the following statements is<strong> <span style="color: #ba372a;"><strong>FALSE</strong></span> </strong> about Michaelis-Menten kinetics?</p> A.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes the enzyme has a single active site. Incorrect B.<strong> </strong><strong><span style="color: #0d57a5;"><strong><span style="color: #0d57a5;">M-M kinetics</span></strong></span></strong> was developed by Greek economist Leo Michelis and Dutch bobsledder Hubert Menten in 1913. Correct C.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the rate of breaking the <strong><span style="color: #2fbd0f;">enzyme-substrate complex [ES]</span></strong> is equal to the rate of its formation. Incorrect D.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the product is<strong> <strong>NOT</strong> </strong>available and there is no measureable reverse <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect E.<strong> </strong>When the substrate <strong><span style="color: #ff0000;">concentration</span></strong>, [S], is much smaller than K<sub>M</sub>, the <strong><span style="color: #a1005e;">reaction rate</span></strong> is linear. Incorrect MC <p>d92c</p> <p>Which one of the following statements is<strong> <span style="color: #169179;"><strong>TRUE</strong></span> </strong> of Michaelis-Menten kinetics?</p> A.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the <strong><span style="color: #ff0000;">concentration</span></strong> of <strong><span style="color: #ff5e00;">enzyme-product complex [EP]</span></strong> is <strong><span style="color: #6d108e;"><i>constant</i></span></strong>. Incorrect B.<strong> </strong><strong><span style="color: #0d57a5;"><strong><span style="color: #0d57a5;">M-M kinetics</span></strong></span></strong> assumes that there is no product available and there is no measureable reverse <strong><span style="color: #a1005e;"><strong><span style="color: #a1005e;">reaction rate</span></strong></span></strong>. Correct C.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the enzyme bound to the substrate [ES] is short lived and does<strong> <strong>NOT</strong> </strong>contribute to the <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect D.<strong> </strong>When the substrate <strong><span style="color: #ff0000;">concentration</span></strong>, [S], is much larger than K<sub>M</sub>, the <strong><span style="color: #a1005e;">reaction rate</span></strong> is linear. Incorrect E.<strong> </strong>The <strong><span style="color: #a1005e;">reaction rate</span></strong> is <strong><span style="color: #009e4c;"><i>proportional</i></span></strong> to the product <strong><span style="color: #ff0000;">concentration</span></strong>. Incorrect MC <p>dc3d</p> <p>Which one of the following statements is<strong> <span style="color: #169179;"><strong>TRUE</strong></span> </strong> of Michaelis-Menten kinetics?</p> A.<strong> </strong>When the substrate <strong><span style="color: #ff0000;">concentration</span></strong>, [S], is much larger than K<sub>M</sub>, the <strong><span style="color: #a1005e;">reaction rate</span></strong> is linear. Incorrect B.<strong> </strong><strong><span style="color: #0d57a5;"><strong><span style="color: #0d57a5;">M-M kinetics</span></strong></span></strong> assumes that the product is<strong> <strong>NOT</strong> </strong>available and there is no measureable reverse <strong><span style="color: #a1005e;"><strong><span style="color: #a1005e;">reaction rate</span></strong></span></strong>. Correct C.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the <strong><span style="color: #ff0000;">concentration</span></strong> of <strong><span style="color: #ff5e00;">enzyme-product complex [EP]</span></strong> is <strong><span style="color: #6d108e;"><i>constant</i></span></strong>. Incorrect D.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the enzyme bound to the substrate [ES] is short lived and does<strong> <strong>NOT</strong> </strong>contribute to the <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect E.<strong> </strong>The <strong><span style="color: #a1005e;">reaction rate</span></strong> is <strong><span style="color: #009e4c;"><i>proportional</i></span></strong> to the product <strong><span style="color: #ff0000;">concentration</span></strong>. Incorrect MC <p>e1ad</p> <p>Which one of the following statements is<strong> <span style="color: #169179;"><strong>TRUE</strong></span> </strong> regarding Michaelis-Menten kinetics?</p> A.<strong> </strong>When the substrate <strong><span style="color: #ff0000;">concentration</span></strong>, [S], is much larger than K<sub>M</sub>, the <strong><span style="color: #a1005e;">reaction rate</span></strong> is linear. Incorrect B.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> was developed by Greek economist Leo Michelis and Dutch bobsledder Hubert Menten in 1913. Incorrect C.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the change in <strong><span style="color: #ff0000;">concentration</span></strong> of <strong><span style="color: #ff5e00;">enzyme-product complex [EP]</span></strong> does<strong> <strong>NOT</strong> </strong>change. Incorrect D.<strong> </strong><strong><span style="color: #0d57a5;"><strong><span style="color: #0d57a5;">M-M kinetics</span></strong></span></strong> assumes that the product is<strong> <strong>NOT</strong> </strong>available and there is no measureable reverse <strong><span style="color: #a1005e;"><strong><span style="color: #a1005e;">reaction rate</span></strong></span></strong>. Correct E.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the enzyme bound to the substrate [ES] is short lived and does<strong> <strong>NOT</strong> </strong>contribute to the <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect MC <p>e1cf</p> <p>Which one of the following statements is<strong> <span style="color: #ba372a;"><strong>FALSE</strong></span> </strong> concerning Michaelis-Menten kinetics?</p> A.<strong> </strong>When the substrate <strong><span style="color: #ff0000;"><strong><span style="color: #ff0000;">concentration</span></strong></span></strong>, [S], is much larger than K<sub>M</sub>, the <strong><span style="color: #a1005e;"><strong><span style="color: #a1005e;">reaction rate</span></strong></span></strong> is linear. Correct B.<strong> </strong>The <strong><span style="color: #a1005e;">reaction rate</span></strong> is <strong><span style="color: #009e4c;"><i>proportional</i></span></strong> to the substrate <strong><span style="color: #ff0000;">concentration</span></strong>. Incorrect C.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that there is no product available and there is no measureable reverse <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect D.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> was developed by German biochemist Leonor Michaelis and Canadian physician Maud Menten in 1913. Incorrect E.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> does<strong> <strong>NOT</strong> </strong>apply to allosteric enzymes. Incorrect MC <p>e5c1</p> <p>Which one of the following statements is<strong> <span style="color: #169179;"><strong>TRUE</strong></span> </strong> regarding Michaelis-Menten kinetics?</p> A.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the <strong><span style="color: #2fbd0f;">enzyme-substrate complex [ES]</span></strong> is short lived and does<strong> <strong>NOT</strong> </strong>contribute to the <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect B.<strong> </strong>When the substrate <strong><span style="color: #ff0000;">concentration</span></strong>, [S], is much larger than K<sub>M</sub>, the <strong><span style="color: #a1005e;">reaction rate</span></strong> is linear. Incorrect C.<strong> </strong><strong><span style="color: #0d57a5;"><strong><span style="color: #0d57a5;">M-M kinetics</span></strong></span></strong> assumes that the product is<strong> <strong>NOT</strong> </strong>available and there is no measureable reverse <strong><span style="color: #a1005e;"><strong><span style="color: #a1005e;">reaction rate</span></strong></span></strong>. Correct D.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the <strong><span style="color: #ff0000;">concentration</span></strong> of <strong><span style="color: #ff5e00;">enzyme-product complex [EP]</span></strong> is <strong><span style="color: #6d108e;"><i>constant</i></span></strong>. Incorrect E.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> was developed by American linguist Laura Michaelis and Belgian cyclist Milan Menten in 1913. Incorrect MC <p>f0d9</p> <p>Which one of the following statements is<strong> <span style="color: #ba372a;"><strong>FALSE</strong></span> </strong> about Michaelis-Menten kinetics?</p> A.<strong> </strong><strong><span style="color: #0d57a5;"><strong><span style="color: #0d57a5;">M-M kinetics</span></strong></span></strong> assumes that the rate of breaking the <strong><span style="color: #ff5e00;"><strong><span style="color: #ff5e00;">enzyme-product complex [EP]</span></strong></span></strong> is equal to the rate of its formation. Correct B.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> was developed by German biochemist Leonor Michaelis and Canadian physician Maud Menten in 1913. Incorrect C.<strong> </strong>The <strong><span style="color: #a1005e;">reaction rate</span></strong> is <strong><span style="color: #009e4c;"><i>proportional</i></span></strong> to the substrate <strong><span style="color: #ff0000;">concentration</span></strong>. Incorrect D.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that there is no product available and there is no measureable reverse <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect E.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the enzyme bound to the product [EP] is short lived and does<strong> <strong>NOT</strong> </strong>contribute to the <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect MC <p>f3da</p> <p>Which one of the following statements is<strong> <span style="color: #ba372a;"><strong>FALSE</strong></span> </strong> about Michaelis-Menten kinetics?</p> A.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the rate of breaking the <strong><span style="color: #2fbd0f;">enzyme-substrate complex [ES]</span></strong> is equal to the rate of its formation. Incorrect B.<strong> </strong><strong><span style="color: #0d57a5;"><strong><span style="color: #0d57a5;">M-M kinetics</span></strong></span></strong> assumes that the <strong><span style="color: #2fbd0f;"><strong><span style="color: #2fbd0f;">enzyme-substrate complex [ES]</span></strong></span></strong> is short lived and does<strong> <strong>NOT</strong> </strong>contribute to the <strong><span style="color: #a1005e;"><strong><span style="color: #a1005e;">reaction rate</span></strong></span></strong>. Correct C.<strong> </strong>When the substrate <strong><span style="color: #ff0000;">concentration</span></strong>, [S], is much smaller than K<sub>M</sub>, the <strong><span style="color: #a1005e;">reaction rate</span></strong> is linear. Incorrect D.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes the enzyme has a single active site. Incorrect E.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the product is<strong> <strong>NOT</strong> </strong>available and there is no measureable reverse <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect MC <p>f57e</p> <p>Which one of the following statements is<strong> <span style="color: #ba372a;"><strong>FALSE</strong></span> </strong> concerning Michaelis-Menten kinetics?</p> A.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that there is no product available and there is no measureable reverse <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect B.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the <strong><span style="color: #ff5e00;">enzyme-product complex [EP]</span></strong> is short lived and does<strong> <strong>NOT</strong> </strong>contribute to the <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect C.<strong> </strong><strong><span style="color: #0d57a5;"><strong><span style="color: #0d57a5;">M-M kinetics</span></strong></span></strong> assumes that the <strong><span style="color: #ff0000;"><strong><span style="color: #ff0000;">concentration</span></strong></span></strong> of <strong><span style="color: #ff5e00;"><strong><span style="color: #ff5e00;">enzyme-product complex [EP]</span></strong></span></strong> is <strong><span style="color: #6d108e;"><i><strong><span style="color: #6d108e;"><i>constant</i></span></strong></i></span></strong>. Correct D.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> was developed by German biochemist Leonor Michaelis and Canadian physician Maud Menten in 1913. Incorrect E.<strong> </strong>When the substrate <strong><span style="color: #ff0000;">concentration</span></strong>, [S], is much smaller than K<sub>M</sub>, the <strong><span style="color: #a1005e;">reaction rate</span></strong> is linear. Incorrect MC <p>f710</p> <p>Which one of the following statements is<strong> <span style="color: #ba372a;"><strong>FALSE</strong></span> </strong> about Michaelis-Menten kinetics?</p> A.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> does<strong> <strong>NOT</strong> </strong>apply to allosteric enzymes. Incorrect B.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that there is no product available and there is no measureable reverse <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect C.<strong> </strong><strong><span style="color: #0d57a5;"><strong><span style="color: #0d57a5;">M-M kinetics</span></strong></span></strong> assumes that the change in <strong><span style="color: #ff0000;"><strong><span style="color: #ff0000;">concentration</span></strong></span></strong> of <strong><span style="color: #ff5e00;"><strong><span style="color: #ff5e00;">enzyme-product complex [EP]</span></strong></span></strong> does<strong> <strong>NOT</strong> </strong>change. Correct D.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> was developed by German biochemist Leonor Michaelis and Canadian physician Maud Menten in 1913. Incorrect E.<strong> </strong>When the substrate <strong><span style="color: #ff0000;">concentration</span></strong>, [S], is much larger than K<sub>M</sub>, the <strong><span style="color: #a1005e;">reaction rate</span></strong> is <strong><span style="color: #6d108e;"><i>constant</i></span></strong>. Incorrect MC <p>f818</p> <p>Which one of the following statements is<strong> <span style="color: #ba372a;"><strong>FALSE</strong></span> </strong> concerning Michaelis-Menten kinetics?</p> A.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the enzyme bound to the product [EP] is short lived and does<strong> <strong>NOT</strong> </strong>contribute to the <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect B.<strong> </strong>The <strong><span style="color: #a1005e;">reaction rate</span></strong> is <strong><span style="color: #009e4c;"><i>proportional</i></span></strong> to the substrate <strong><span style="color: #ff0000;">concentration</span></strong>. Incorrect C.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> was developed by German biochemist Leonor Michaelis and Canadian physician Maud Menten in 1913. Incorrect D.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes a quasi-steady state, that the <strong><span style="color: #2fbd0f;">enzyme-substrate complex [ES]</span></strong> is <strong><span style="color: #6d108e;"><i>constant</i></span></strong>. Incorrect E.<strong> </strong>When the substrate <strong><span style="color: #ff0000;"><strong><span style="color: #ff0000;">concentration</span></strong></span></strong>, [S], is much smaller than K<sub>M</sub>, the <strong><span style="color: #a1005e;"><strong><span style="color: #a1005e;">reaction rate</span></strong></span></strong> is <strong><span style="color: #6d108e;"><i><strong><span style="color: #6d108e;"><i>constant</i></span></strong></i></span></strong>. Correct MC <p>fb08</p> <p>Which one of the following statements is<strong> <span style="color: #169179;"><strong>TRUE</strong></span> </strong> of Michaelis-Menten kinetics?</p> A.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that there is no substrate available and there is no measureable reverse <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect B.<strong> </strong><strong><span style="color: #0d57a5;"><strong><span style="color: #0d57a5;">M-M kinetics</span></strong></span></strong> assumes that the enzyme bound to the product [EP] is short lived and does<strong> <strong>NOT</strong> </strong>contribute to the <strong><span style="color: #a1005e;"><strong><span style="color: #a1005e;">reaction rate</span></strong></span></strong>. Correct C.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> was developed by Greek economist Leo Michelis and Dutch bobsledder Hubert Menten in 1913. Incorrect D.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the <strong><span style="color: #ff5e00;">enzyme-product complex [EP]</span></strong> is <strong><span style="color: #6d108e;"><i>constant</i></span></strong>. Incorrect E.<strong> </strong>When the substrate <strong><span style="color: #ff0000;">concentration</span></strong>, [S], is much smaller than K<sub>M</sub>, the <strong><span style="color: #a1005e;">reaction rate</span></strong> is <strong><span style="color: #6d108e;"><i>constant</i></span></strong>. Incorrect MC <p>feb0</p> <p>Which one of the following statements is<strong> <span style="color: #ba372a;"><strong>FALSE</strong></span> </strong> concerning Michaelis-Menten kinetics?</p> A.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the enzyme bound to the product [EP] is short lived and does<strong> <strong>NOT</strong> </strong>contribute to the <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect B.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> was developed by German biochemist Leonor Michaelis and Canadian physician Maud Menten in 1913. Incorrect C.<strong> </strong><strong><span style="color: #0d57a5;"><strong><span style="color: #0d57a5;">M-M kinetics</span></strong></span></strong> assumes that the change in <strong><span style="color: #ff0000;"><strong><span style="color: #ff0000;">concentration</span></strong></span></strong> of <strong><span style="color: #ff5e00;"><strong><span style="color: #ff5e00;">enzyme-product complex [EP]</span></strong></span></strong> does<strong> <strong>NOT</strong> </strong>change. Correct D.<strong> </strong><strong><span style="color: #0d57a5;">M-M kinetics</span></strong> assumes that the product is<strong> <strong>NOT</strong> </strong>available and there is no measureable reverse <strong><span style="color: #a1005e;">reaction rate</span></strong>. Incorrect E.<strong> </strong>When the substrate <strong><span style="color: #ff0000;">concentration</span></strong>, [S], is much smaller than K<sub>M</sub>, the <strong><span style="color: #a1005e;">reaction rate</span></strong> is linear. Incorrect