Mixed and non-competitive enzyme inhibition: underlying mechanisms and mechanistic irrelevance of the formal two-site model.

Mixed inhibition inhibition mechanism non-competitive inhibition

Journal

Journal of enzyme inhibition and medicinal chemistry
ISSN: 1475-6374
Titre abrégé: J Enzyme Inhib Med Chem
Pays: England
ID NLM: 101150203

Informations de publication

Date de publication:
Dec 2023
Historique:
medline: 15 8 2023
pubmed: 14 8 2023
entrez: 14 8 2023
Statut: ppublish

Résumé

The formal mechanism of linear mixed and non-competitive enzyme inhibition implies the binding of inhibitors to both the active site of the free enzyme in competition with the substrate, and to an allosteric site on the enzyme-substrate complex. However, it is evident from a review of the scientific literature that the two-site mechanism is frequently mistaken as the actual underlying mechanism of mixed inhibition. In this study, we conducted a comprehensive assessment of the mechanistic relevance of this type of inhibition using a statistical approach. By combining a statistical analysis of the inhibition cases documented in the BRENDA database with a theoretical investigation of inhibition models, we conclude that mixed inhibitors exclusively bind to the active site of enzymes. Hence ruling out any implication of allosteric sites and depriving the two-site model of any mechanistic relevance.

Identifiants

pubmed: 37577806
doi: 10.1080/14756366.2023.2245168
pmc: PMC10683834
doi:

Substances chimiques

Enzyme Inhibitors 0

Types de publication

Review Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

2245168

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Auteurs

Alessandro Pesaresi (A)

Istituto di Cristallografia - Consiglio Nazionale delle Ricerche, Trieste, Italy.

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Classifications MeSH