Phenyl-Methane-Sulfonyl-Fluoride (PMSF) Inactivates Serine Proteases by Binding Covalently to the Catalytic
Multiple Choice
Phenyl-methane-sulfonyl-fluoride (PMSF) inactivates serine proteases by binding covalently to the catalytic serine residue at the active site; this enzyme-inhibitor bond is not cleaved by the enzyme. This is an example of what kind of inhibition?
A) irreversible
B) competitive
C) noncompetitive
D) mixed
E) pH inhibition
Correct Answer:
Verified
Correct Answer:
Verified
Q94: Which molecule would NOT be effective to
Q95: Which enzymes are NOT among the six
Q96: Describe why the Michaelis constant (K<sub>m</sub>) and
Q97: Explain how a biochemist might discover that
Q98: Enzymes that cleave carbon-carbon bonds without the
Q100: Which statement about a plot of
Q101: In what way does an uncompetitive inhibitor
Q102: Which type of enzyme is responsible for
Q103: Describe how glucagon and insulin regulate the
Q104: An enzyme catalyzes the reaction A