Multiple Choice
Exhibit 6A This is a reaction going on in your muscle cells right this very minute: The enzyme triose phosphate isomerase catalyzes this reaction in the forward direction as part of the glycolytic pathway. It follows simple Michaelis-Menten kinetics:
Typical cellular concentrations: triose phosphate isomerase = 0.1 nM
Dihydroxyacetone phosphate = 5 µM glyceraldehyde-3-phosphate = 2 µM
Refer to Exhibit 6A. "Hindrate" is an inhibitor of triose phosphate isomerase. When it is added to cells at a concentration of 0.1 nM, the enzyme's KM for the substrate is unchanged, but the apparent Vmax is altered to 50 nM\sec.
A) This is a competitive inhibitor.
B) This is an uncompetitive inhibitor.
C) This is a noncompetitive inhibitor.
D) This is an irreversible inhibitor.
Correct Answer:

Verified
Correct Answer:
Verified
Q12: The reaction catalyzed by aspartate transcarbamoylase is<br>A)
Q13: Which of the following is true?<br>A) The
Q14: According to the steady-state assumption<br>A) the product
Q15: Enzymatic activity has an optimum temperature because<br>A)
Q16: Exhibit 6A This is a reaction going
Q18: Exhibit 6A This is a reaction going
Q19: Exhibit 6A This is a reaction going
Q20: The amount of energy released during a
Q21: Irreversible inhibitors of enzymatic reactions<br>A) bind to
Q22: The Michaelis-Menten approach to describing the kinetics