BIO NMDCAT BIOLOGICAL MOLECULES

nmdcat.online June 27, 2026

In competitive inhibition, the apparent Km (Michaelis constant) of the enzyme for its substrate is

A. Unchanged

B. Decreased

C. Increased

✓

D. Equal to Vmax

📝 Explanation

A competitive inhibitor competes for the active site, effectively making it harder for the enzyme to bind its substrate. More substrate is required to reach half the maximum velocity. Therefore, the apparent Km (substrate concentration at 1/2 Vmax) is increased in the presence of a competitive inhibitor.

📖 Additional Information

Unchanged
Decreased
Increased
Equal to Vmax

A competitive inhibitor competes for the active site, effectively making it harder for the enzyme to bind its substrate. More substrate is required to reach half the maximum velocity. Therefore, the apparent Km (substrate concentration at 1/2 Vmax) is increased in the presence of a competitive inhibitor.

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