Quantitative relationships between rate constants to calculate Km, kinetic efficiency (kcat/Km) and Vmax –II
Triose phosphate isomerase catalyzes the conversion of glyceraldehyde-3-phosphate to dihydroxyacetone phosphate.
Glyceraldehyde-3-P dihydroxyaceone-P
The Km of this enzyme for its substrate glyceraldehyde-3-phosphate is 1.8 x 10-5 M.
When [glyceraldehyde-3-phosphate] = 30 µM the rate of the reaction, v, was 82.5 µmole mL-1 sec-1.
a. What is Vmax for this enzyme?
b. Assuming 3 nanomoles per mL of enzyme was used in this experiment ([Etotal] = 3 nanomol/mL), what is kcat for this enzyme?
c. What is the catalytic efficiency (kcat/Km) for triose phosphate isomerase?
d. Does the value of kcat/Km reveal whether triose phosphate isomerase approaches “catalytic perfection”?
e. What determines the ultimate speed limit of an enzyme-catalyzed reaction? That is, what is it that imposes the physical limit on kinetic perfection?
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