12. The K,m for the reaction of chymotrypsin with N-acetylvaline ethyl ester is 8.8x10-2 M, and the K.," for the reaction of chymotrypsin with N-acetyltyrosine ethyl ester is 6.6x10 M. (a) Which substrate has the higher apparent affinity for the enzyme? (b) Which substrate is likely to give a higher value for Vmax? 13. An enzyme catalyzes the reaction A B. The enzyme is present at a concentration of 2 nNM and the Vmax is 1.2 μΜ s-1. The Km for substrate A is 10 μΜ. Calculate the initial velocity of the reaction, Vo, when the substrate concentration is (a) 2 μΜ, (b) 10 μM, (c) 30 μΜ. 14. An enzyme catalyzes the reaction M N. The enzyme is present at a concentration of 1 nM, and the Vmax is 2 μΜ s-1. The Km for substrate M is 4 μΜ. Calculate kcat.
12. The K,m for the reaction of chymotrypsin with N-acetylvaline ethyl ester is 8.8x10-2 M, and the K.," for the reaction of chymotrypsin with N-acetyltyrosine ethyl ester is 6.6x10 M. (a) Which substrate has the higher apparent affinity for the enzyme? (b) Which substrate is likely to give a higher value for Vmax? 13. An enzyme catalyzes the reaction A B. The enzyme is present at a concentration of 2 nNM and the Vmax is 1.2 μΜ s-1. The Km for substrate A is 10 μΜ. Calculate the initial velocity of the reaction, Vo, when the substrate concentration is (a) 2 μΜ, (b) 10 μM, (c) 30 μΜ. 14. An enzyme catalyzes the reaction M N. The enzyme is present at a concentration of 1 nM, and the Vmax is 2 μΜ s-1. The Km for substrate M is 4 μΜ. Calculate kcat.
Introductory Chemistry: A Foundation
9th Edition
ISBN:9781337399425
Author:Steven S. Zumdahl, Donald J. DeCoste
Publisher:Steven S. Zumdahl, Donald J. DeCoste
Chapter21: Biochemistry
Section: Chapter Questions
Problem 28QAP: . Describe the lock-and-key model for enzymes. Why are the shapes of the enzyme and its substrate...
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