11. Quantitative Relationships between Rate Constants to Calculate K, Kinetic Efficiency (kcat/Km) and Vmax -II Triose phosphate isomerase catalyzes the conversion of glyceraldehyde-3-phosphate to dihydroxyacetone phosphate. Glyceraldehyde-3-P dihydroxyacetone-P The Km of this enzyme for its substrate glyceraldehyde-3-phosphate is 1.8 x 10-5 M When [glyceraldehydes-3-phosphate] =30 μM, the rate of the reaction, v, was 82.5 μmol mL-1 s-1. a. What is Vmax for this enzyme? b. Assuming 3 nm/mL of enzyme was used in this experiment (E total = 3nm/mL for this enzyme? c. What is the catalytic efficiency (kcat/km) for triose phosphate isomerase? d. Does this enzyme reach catalytic perfection?
11. Quantitative Relationships between Rate Constants to Calculate K, Kinetic Efficiency (kcat/Km) and Vmax -II Triose phosphate isomerase catalyzes the conversion of glyceraldehyde-3-phosphate to dihydroxyacetone phosphate. Glyceraldehyde-3-P dihydroxyacetone-P The Km of this enzyme for its substrate glyceraldehyde-3-phosphate is 1.8 x 10-5 M When [glyceraldehydes-3-phosphate] =30 μM, the rate of the reaction, v, was 82.5 μmol mL-1 s-1. a. What is Vmax for this enzyme? b. Assuming 3 nm/mL of enzyme was used in this experiment (E total = 3nm/mL for this enzyme? c. What is the catalytic efficiency (kcat/km) for triose phosphate isomerase? d. Does this enzyme reach catalytic perfection?
Biochemistry
6th Edition
ISBN:9781305577206
Author:Reginald H. Garrett, Charles M. Grisham
Publisher:Reginald H. Garrett, Charles M. Grisham
Chapter18: Glycolysis
Section: Chapter Questions
Problem 18P: Distinguishing the Mechanisms of Class I and Class I Aldolases Fructose bisphosphate aldolase in...
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