Biochemistry
Biochemistry
6th Edition
ISBN: 9781305577206
Author: Reginald H. Garrett, Charles M. Grisham
Publisher: Cengage Learning
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Chapter 13, Problem 13P

Answers to all problems are at the end of this book. Detailed solutions are available in the Student Solutions Manual, Study Guide, and Problems Book.

Quantitative Relationships Between Rate Constants to Calculate Km, Kinetic Efficiency (kcat/Km) and Vmax - V Acetylcholinesterase catalyzes the hydrolysis of the neurotransmitter acetylcholine:

Acetylcholine + H 2 O acetate+choline The Km of acetylcholinesterase for its substrate acetylcholine is 9 × 10-5 M. In a reaction mixture containing 5 nanomoles/mL of acetylcholinesterase and 130 μM acetylcholine, a velocity v 0 = 40 μ mol/mL sec was observed for the acetylcholinesterase reaction.

a. Calculate Vmax for this amount of enzyme.

b. Calculate kcat for acetylcholinesterase.

c. Calculate the catalytic efficiency (kcat/Km) for acetylcholinesterase.

d. Does acetylcholinesterase approach "catalytic perfection"?

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