Structure-activity of cutinase, a small lipolytic enzyme.
Cutinase, a small lipolytic enzyme, is the smallest member of the alpha/beta-hydrolase fold family, to which the other lipases belong. Cutinase has a catalytic activity comparable to that of pancreatic lipase on short chain triglycerides, and retains a significant activity on long chain triglycerides. Cutinase has been extensively studied using site-directed mutagenesis, and we have thoroughly characterized it from a structural point of view. Besides the native enzyme, tens of mutants and several inhibitor complexes have been solved, providing a complete and precise picture of the structure, dynamics and catalytic machinery of cutinase.
Longhi
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Architecture et Fonction des Macromolécules Biologiques, UPR 9039, CNRS, IFR1, 31 Chemin Joseph Aiguier, 13402, Marseilles, France.
Cambillau
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D001665:Binding Sites; D002265:Carboxylic Ester Hydrolases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D002384:Catalysis; D008066:Lipolysis; D008958:Models, Molecular; D016297:Mutagenesis, Site-Directed; D063065:Organophosphonates / Q000378:metabolism; D017433:Protein Structure, Secondary; D013329:Structure-Activity Relationship; D014280:Triglycerides / Q000378:metabolism
D063065:Organophosphonates; D014280:Triglycerides; D002265:Carboxylic Ester Hydrolases; C019952:cutinase