A carboxypeptidase was found to have a Michaelis constant KM of 2.00 μM and a kcat of 150 s-1 for its substrate A
a. What is the initial rate of reaction for a substrate concentration of 5.00 µM and an enzyme concentration of 0.01 μ µM? Give units.
b. The presence of 5.00 mM of a competitive inhibitor decreased the initial rate above by a factor of 2. What is the dissociation constant for the enzyme-inhibitor complex, K1, where K1 = [E][I]/[EI] ?
c. A competing substrate B is added to the solution in part (a). Its KM is 10.00 µM and its kcat is 100 s-1 Calculate the relative rates of substrate reaction for equal concentrations of substrates; that is, calculate vB/vA.
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