An allosteric enzyme that follows the concerted mechanism has a T/R ratio of 500 in the absence of substrate. Suppose that a mutation reversed the ratio. How would this mutation affect the relation between the rate of the reaction and substrate concentration? The mutant enzyme would behave like an enzyme that obeys Michaelis Menton kinetics. The mutant enzyme would have a smaller vmax There would be no difference in the mutant enzyme in terms of substrate binding and catalysis. More than one answer is correct. The mutant enzyme would display cooperativity more than the wild type.

Human Anatomy & Physiology (11th Edition)
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Author:Elaine N. Marieb, Katja N. Hoehn
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Chapter1: The Human Body: An Orientation
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An allosteric enzyme that follows the concerted mechanism has a T/R ratio of 500 in the absence of substrate. Suppose
that a mutation reversed the ratio. How would this mutation affect the relation between the rate of the reaction and
substrate concentration?
The mutant enzyme would behave like an enzyme that obeys Michaelis Menton kinetics.
The mutant enzyme would have a smaller vmax
There would be no difference in the mutant enzyme in terms of substrate binding and catalysis.
More than one answer is correct.
The mutant enzyme would display cooperativity more than the wild type.
MacBook Air
888
F5
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Transcribed Image Text:An allosteric enzyme that follows the concerted mechanism has a T/R ratio of 500 in the absence of substrate. Suppose that a mutation reversed the ratio. How would this mutation affect the relation between the rate of the reaction and substrate concentration? The mutant enzyme would behave like an enzyme that obeys Michaelis Menton kinetics. The mutant enzyme would have a smaller vmax There would be no difference in the mutant enzyme in terms of substrate binding and catalysis. More than one answer is correct. The mutant enzyme would display cooperativity more than the wild type. MacBook Air 888 F5 F4 F3 F2 %23 2$ %
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