Enzyme inhibitors are substances that reduce enzyme activity by interacting with an enzyme or a state of its catalytic cycle. Reversible binding can obstruct substrate association or alter the ability of a substrate-bound enzyme to complete turnover. The relationship between inhibitor binding and the reaction sequence produces characteristic inhibition kinetics [1][2]. Covalent inhibitors possess chemical groups capable of forming a bond with a residue in the target protein [3]. Their selectivity can be assessed across multiple enzymes by measuring competition with activity-based probes, which report accessible, reactive enzyme sites [4]. Recognition interactions position the inhibitor near a susceptible residue, while the inhibitor's reactive group participates in bond formation. Together, these features determine the target engagement and persistence of covalent inhibition [5].
- inhibitor binding
- enzyme kinetics
- partial inhibition
- enzyme inactivation
References
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- Micah J. Niphakis; Benjamin F. Cravatt; Enzyme Inhibitor Discovery by Activity-Based Protein Profiling. Annu. Rev. Biochem. 2014, 83, 341-377, 10.1146/annurev-biochem-060713-035708.
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