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#competitive inhibitor

3 public questions tagged with this topic.

Enzyme Kinetics

The presence of a competitive inhibitor will:

Increase Km is the accurate response regarding enzymatic activity or regulation described in this question. Enzymes are biological catalysts that accelerate reactions by lowering activation energy through specific substrate binding and transition state stabilization. In the context of Enzymes Basics, Increase Km plays a specific catalytic or regulatory role determined by its active site configuration and mechanism of action. The other options (Decrease Vmax, Bind to the allosteric site, and Change the enzyme’s conformation permanently) are either different enzymes with distinct substrate specificities, act through different mechanisms, or are involved in separate metabolic pathways.

Ref: Lehninger Principles of Biochemistry, Nelson & Cox, 8th Ed., Ch. 6

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Enzyme Kinetics

Which of the following enzyme kinetic parameters does not change in the presence of a competitive inhibitor?

Vmax is the correct choice because it does not accurately describe or belong to the category addressed in this question. In the context of Enzyme Kinetics, the other options (Km, Kcat, and Turnover number) are all valid and well-established concepts. Vmax is either unrelated to the topic, describes a different biological process, or represents a common misconception. Questions framed as 'which is NOT' require students to identify the exception among otherwise correct statements, demanding comprehensive knowledge of the topic rather than recognition of a single fact.

Ref: Lehninger Principles of Biochemistry, Nelson & Cox, 8th Ed., Ch. 6

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Enzyme Inhibition

The Km of an enzyme in the presence of a competitive inhibitor will:

Increase is the accurate response regarding enzymatic activity or regulation described in this question. Enzymes are biological catalysts that accelerate reactions by lowering activation energy through specific substrate binding and transition state stabilization. In the context of Enzyme Inhibition, Increase plays a specific catalytic or regulatory role determined by its active site configuration and mechanism of action. The other options (Decrease, Remain constant, and First increase, then decrease) are either different enzymes with distinct substrate specificities, act through different mechanisms, or are involved in separate metabolic pathways.

Ref: Lehninger Principles of Biochemistry, Nelson & Cox, 8th Ed., Ch. 6

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