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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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Question 23
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
Y is a competitive inhibitor of X.
The Km for X will increase.
d.
The V for X will be affected if Y is present in the reaction mixture.
max
pH dependence of Vmax reflects the ionization state of catalytic site
e
residues.
Consider the following: X and Y are methanol (poisonous) and ethanol
respectively. If the Km for X = 0.01 M and the Km 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
g
products to reactants (Keg).

a
The Km for X will be affected if Y is present in the reaction mixture.
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
e
residues.
Consider the following: X and Y are methanol (poisonous) and ethanol
respectively. If the Km for X = 0.01 M and the Km 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
g
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.
The kcat for a reaction with a Vmax of 0.005 M/sec and [Erotal =
i
0.000002 M is 0.0000000025/sec

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