Structure-activity of cutinase, a small lipolytic enzyme |
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Authors: | Longhi S Cambillau C |
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Affiliation: | Architecture et Fonction des Macromolécules Biologiques, UPR 9039, CNRS, IFR1, 31 Chemin Joseph Aiguier, 13402, Marseilles, France. |
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Abstract: | 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. |
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