Title of article :
Structure-activity of cutinase, a small lipolytic enzyme
Author/Authors :
Sonia Longhi، نويسنده , , Dominique Bourgeois and Christian Cambillau، نويسنده ,
Pages :
12
From page :
185
To page :
196
Abstract :
Cutinase, a small lipolytic enzyme, is the smallest member of the α/β-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.
Keywords :
Cutinase , Hydrolase fold , crystal structure , lipases
Journal title :
Astroparticle Physics
Record number :
568310
Link To Document :
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