Enzymes catalyze chemical reactions. What constitutes the active site of an enzyme? What are the turnover number (kcat), the Michaelis constant (Km), and the maximal velocity (Vmax) of an enzyme? The kcat (catalytic rate constant) for carbonic anhydrase is 5 × 105 molecules per second. This is a “rate constant,” but not a “rate.” What is the difference? By what oncentration would you multiply this rate constant in order to determine an actual rate of prod- uct formation (V)? Under what circumstances would this rate become equal to the maximal velocity (Vmax) of the enzyme?

Enzymes catalyze chemical reactions. What constitutes the active site of an enzyme? What are the turnover number (kcat), the Michaelis constant (Km), and the maximal velocity (Vmax) of an enzyme? The kcat (catalytic rate constant) for carbonic anhydrase is 5 × 105 molecules per second. This is a “rate constant,” but not a “rate.” What is the difference? By what oncentration would you multiply this rate constant in order to determine an actual rate of prod- uct formation (V)? Under what circumstances would this rate become equal to the maximal velocity (Vmax) of the enzyme?

Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter19: The Tricarboxylic Acid Cycle

Section: Chapter Questions

Problem 7P

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