Quantitative relationships between rate constants to calculate Km, kinetic efficiency (kcat/Km) and Vmax –I
Measurement of the rate constants for a simple enzymatic reaction obeying Michaelis-Menten kinetics gave the following results:
k1 = 2 x 108 M-1sec-1
k-1 = 1 x 103 sec-1
k2 = 5 x 103 sec-1
a. What is Ks, the dissociation constant for the enzyme-substrate complex?
b. What is Km, the Michaelis constant for this enzyme?
c. What is kcat (the turnover number) for this enzyme?
d. What is the catalytic efficiency (kcat/Km) for this enzyme?
e. Does this enzyme approach “kinetic perfection”? (That is, does kcat/Km approach the diffusion-controlled rate of enzyme association with substrate?)
f. If a kinetic measurement was made using 2 nanomoles of enzyme per mL and saturating amounts of substrate, what would Vmax equal?
g. Again, using 2 nanomoles of enzyme per mL of reaction mixture, what concentration of substrate would give v = 0.75 Vmax?
h. If a kinetic measurement was made using 4 nanomoles of enzyme per mL and saturating amounts of substrate, what would Vmax equal? What would Km equal under these conditions?
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