Acyl glycerol hydrolases: inhibitors, interface and catalysis.
The last five years have witnessed the solution of a large number of lipase structures, which has led, among other insights, to the structural interpretation of the interfacial activation phenomenon in terms of 'lid' opening. This interpretation has been extended this year to include phospholipase A2. Recent structural studies on lipases have provided data on the detailed mechanisms underlying the behaviour of lipases: how they bind to inhibitors or substrates, and what interactions occur between their hydrophobic face and hydrophobic molecules, for example. In addition, studies on cutinase point mutants have shed some light on the role of the oxyanion hole in lipolytic catalysis.
Cambillau
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Architecture et Fonction des Macromolécules Biologiques, UPR 9039, CNRS, IFR, 131 Chemin Joseph Aiguier, 13402 Marseille, CEDEX 20, France. cambilau@ibsm.cnrs-mrs.fr
Longhi
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Nicolas
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Martinez
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D000818:Animals; D001665:Binding Sites; D002265:Carboxylic Ester Hydrolases / Q000037:antagonists & inhibitors / Q000737:chemistry*; D002384:Catalysis; D004791:Enzyme Inhibitors; D006801:Humans; D011487:Protein Conformation
D004791:Enzyme Inhibitors; D002265:Carboxylic Ester Hydrolases