Skip to content
New summer mock series is live Attempt timed papers for SSC, banking, and engineering entrances with updated syllabi for this season. View exams

#irreversible inhibition

4 public questions tagged with this topic.

If an inhibitor binds irreversibly to an enzyme, the inhibition is called:

Suicide inhibition 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, Suicide inhibition plays a specific catalytic or regulatory role determined by its active site configuration and mechanism of action. The other options (Non-competitive, Competitive, and Uncompetitive) 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

Which of the following best describes the effect of a non-competitive inhibitor?

Km remains unchanged, Vmax decreases correctly describes the effect or change asked about in this question. In Enzyme Inhibition, understanding cause-and-effect relationships is essential for predicting biological outcomes. Km remains unchanged, Vmax decreases occurs because of specific molecular interactions, thermodynamic principles, or regulatory mechanisms that govern this biological process. The other options (Km increases, Vmax remains unchanged, Km decreases, Vmax decreases, and Km increases, Vmax increases) describe either opposite effects, effects that occur under different conditions, or changes associated with unrelated processes.

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

If an enzyme is irreversibly inhibited, the inhibitor:

Forms a strong covalent bond with the enzyme 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, Forms a strong covalent bond with the enzyme plays a specific catalytic or regulatory role determined by its active site configuration and mechanism of action. The other options (Forms a weak hydrogen bond with the enzyme, Can be removed by dialysis, and Can be reversed by increasing substrate concentration) 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