Active site access vs. allosteric inhibition: In an allosterically regulated enzyme, how does a competitive inhibitor’s ability to bind the active site compare with a non-competitive inhibitor’s ability to bind that same active site?

Introduction / Context:
Enzyme inhibition is categorized by where and how an inhibitor binds. Competitive inhibitors compete directly with the substrate for the active site, while non-competitive inhibitors usually bind a topologically distinct allosteric site and modulate catalytic efficiency without occupying the active site itself.

Given Data / Assumptions:

• The enzyme is allosterically controlled (has regulatory sites distinct from the active site).
• Competitive inhibitors target the active site; non-competitive inhibitors do not require active-site binding.
• We compare the ability to bind the active site.

Concept / Approach:
By definition, a competitive inhibitor fits into the active site and blocks substrate access. A non-competitive inhibitor binds elsewhere and changes the enzyme’s conformation or catalytic rate constant; it does not depend on occupying the active site. Therefore, the competitive inhibitor’s ability to bind the active site is greater than that of a non-competitive inhibitor for the same enzyme.

Step-by-Step Solution:
Recall definitions: competitive → active site; non-competitive → distinct site. Compare access to the active site: competitive has direct access; non-competitive typically does not. Conclude that the competitive inhibitor’s ability to bind the active site is greater. Select “Greater.”

Verification / Alternative check:
Lineweaver–Burk (or modern non-linear fits) show competitive inhibition increases apparent Km; non-competitive reduces Vmax without changing Km, consistent with different binding locations.

Why Other Options Are Wrong:
“Lesser” or “equal” contradict the definitions; “half” has no kinetic meaning; absolute zero is too strong since the question asks comparatively and classical non-competitive binding is not at the active site.

Common Pitfalls:
Confusing non-competitive with uncompetitive inhibition; uncompetitive inhibitors bind only the enzyme–substrate complex, still not the free active site.

Final Answer:
Greater.