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Updated: Aug 22, 2026

Defining Substrate Specificities for Lipase and Phospholipase Candidates
Published on: November 23, 2016
Covalent inhibition of digestive lipases by chiral phosphonates
J F Cavalier1, G Buono, R Verger
1Laboratoire de Lipolyse Enzymatique, UPR 9025, IFR 1 du CNRS, 31 Chemin Joseph Aiguier, F-13402 Marseille Cedex 20, France.
Abstract:
Designing and synthesizing specific inhibitors is of fundamental value for understanding the molecular mechanisms involved in the interfacial adsorption step as well as the catalytic activity of lipases. In this Account, we will review and discuss results obtained mostly at our laboratory concerning the covalent inhibition of human gastric and human pancreatic lipases by chiral phosphonates. Rather than presenting an exhaustive list of compounds tested so far with lipases of animal and microbial origin, we selected recent experimental data illustrating well the specific problems encountered during the covalent inhibition of these digestive lipases.
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