An enzyme has a single active site at which it can bind and hydrolyze either X or Y but the enzyme cannot bind X and Y at the same time. Which of the following statements are TRUE? Multiple answers: Multiple answers are accepted for this question Select one or more answers and submit. For keyboard navigation. SHOW MORE V The Km for X will be affected if Y is present in the reaction mixture. a b Y is a competitive inhibitor of X. The Km for X will increase. The Vmax for X will be affected if Y is present in the reaction mixture. pH dependence of Vmax reflects the ionization state of catalytic site residues. e Consider the following: X and Y are methanol (poisonous) and ethanol respectively. If the Km for X= 0.01 M and the Km f for Y = 0.001 M then 0.01 M Y is 10 times the concentration of Y required for 0.5 Vmax. Addition of an enzyme to a chemical reaction increases the ratio of products to reactants (Keg). A mutation in the active site of an enzyme resulting in a large increase in stabilization of the ES complex but no change in the stabilization of the transition state complex would decrease the rate of product formation because increased stabilization of ES increases the activation energy although the transition state energy is unchanged. h i The kcat for a reaction with a Vmax Oof 0.005 M/sec and [Etotall = 0.000002 M is 0.0000000025/sec
An enzyme has a single active site at which it can bind and hydrolyze either X or Y but the enzyme cannot bind X and Y at the same time. Which of the following statements are TRUE? Multiple answers: Multiple answers are accepted for this question Select one or more answers and submit. For keyboard navigation. SHOW MORE V The Km for X will be affected if Y is present in the reaction mixture. a b Y is a competitive inhibitor of X. The Km for X will increase. The Vmax for X will be affected if Y is present in the reaction mixture. pH dependence of Vmax reflects the ionization state of catalytic site residues. e Consider the following: X and Y are methanol (poisonous) and ethanol respectively. If the Km for X= 0.01 M and the Km f for Y = 0.001 M then 0.01 M Y is 10 times the concentration of Y required for 0.5 Vmax. Addition of an enzyme to a chemical reaction increases the ratio of products to reactants (Keg). A mutation in the active site of an enzyme resulting in a large increase in stabilization of the ES complex but no change in the stabilization of the transition state complex would decrease the rate of product formation because increased stabilization of ES increases the activation energy although the transition state energy is unchanged. h i The kcat for a reaction with a Vmax Oof 0.005 M/sec and [Etotall = 0.000002 M is 0.0000000025/sec
Biochemistry
9th Edition
ISBN:9781319114671
Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Chapter1: Biochemistry: An Evolving Science
Section: Chapter Questions
Problem 1P
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Transcribed Image Text:An enzyme has a single active site at which it can bind and hydrolyze either X or Y but the enzyme cannot bind X and Y at the same
time. Which of the following statements are TRUE?
Multiple answers: Multiple answers are accepted for this question
Select one or more answers and submit. For keyboard navigation. SHOW MORE
The Km for X will be affected if Y is present in the reaction mixture.
a
Y is a competitive inhibitor of X.
The Km for X will increase.
d
The Vmax for X will be affected if Y is present in the reaction mixture.
pH dependence of Vmax reflects the ionization state of catalytic site residues.
e
Consider the following: X and Y are methanol (poisonous) and ethanol respectively. If the Km for X= 0.01 M and the Km
f
for Y = 0.001 M then 0.01 M Y is 10 times the concentration of Y required for 0.5 Vmax.
Addition of an enzyme to a chemical reaction increases the ratio of products to reactants (Ken).
A mutation in the active site of an enzyme resulting in a large increase in stabilization of the ES complex but no change in
the stabilization of the transition state complex would decrease the rate of product formation because increased
stabilization of ES increases the activation energy although the transition state energy is unchanged.
h
i
The kcar for a reaction with a Vmax
of 0.005 M/sec and [Etotal = 0.000002 M is 0.0000000025/sec
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