Multiple Choice
An enzyme transition state inhibitor
A) would probably bind much more tightly than a normal substrate.
B) probably would be a noncompetitive inhibitor of an enzyme.
C) would probably bind much less tightly than a normal substrate.
D) would have a Ki about equal to the Km for the substrate.
Correct Answer:

Verified
Correct Answer:
Verified
Q52: Specific activity of an enzyme refers to<br>A)
Q53: High concentrations of substrate overcome reversible inhibition
Q54: For an enzyme-substrate pair, a graph of
Q55: The Lineweaver-Burk plot gives<br>A) 1/Vmax as the
Q56: Creatine kinase (CK) activity is used as
Q58: Enzymes that contain aspartate or glutamate at
Q59: If an inorganic ion such as Mg<sup>2+</sup>
Q60: Allosteric control of enzyme action requires<br>A) a
Q61: In the presence of effector A an
Q62: Allosteric control most often occurs through changes