1. The covalent intermediate formed by a serine protease reacting with its subst

Question

1. The covalent intermediate formed by a serine protease reacting with its substrate is called the
a. Michaelis complex
b. acyl-enzyme
c. transition state
d. apoenzyme

2. The slowest step in the reaction mechanism of an enzyme-catalyzed reaction is called the
a. acylation step
b. product release step
c. rate-limiting step
d. diffusion limiting rate

3. The maximal rate observed with increasing substrate concentration at a fixed enzyme concentration indicates the
a. diffusion limit
b. rate limiting step
c. inhibition of the enzyme by the product
d. saturation of the active site by substrate

4. As an enzyme sample is further purified the slope of the plot of rate vs enzyme conc will
a. decrease
b. stay the same
c. increase
d. become non-linear

Explanation / Answer

Answer 1)d. apoenzyme 2)c. rate-limiting step 3)c. inhibition of the enzyme by the product 4)d. become non-linear

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