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nmdcat.online June 27, 2026

The interaction of an enzyme’s R-groups with a substrate that results in the transient formation and breakage of covalent bonds during catalysis describes the mechanism of

A. The lock-and-key model
B. Covalent catalysis
✓
C. Proximity effect only
D. Acid-base catalysis

📝 Explanation

In covalent catalysis, a powerful nucleophilic R-group in the active site (e.g., the -SH of cysteine or -OH of serine) forms a transient covalent bond with the substrate. This acyl-enzyme intermediate is then resolved by another step, releasing the product and regenerating the free enzyme.

📖 Additional Information

  • The lock-and-key model
  • Covalent catalysis
  • Proximity effect only
  • Acid-base catalysis

In covalent catalysis, a powerful nucleophilic R-group in the active site (e.g., the -SH of cysteine or -OH of serine) forms a transient covalent bond with the substrate. This acyl-enzyme intermediate is then resolved by another step, releasing the product and regenerating the free enzyme.

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