Longhi_1999_Biochim.Biophys.Acta_1441_185

Reference

Title : Structure-activity of cutinase, a small lipolytic enzyme - Longhi_1999_Biochim.Biophys.Acta_1441_185
Author(s) : Longhi S , Cambillau C
Ref : Biochimica & Biophysica Acta , 1441 :185 , 1999
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.

PubMedSearch : Longhi_1999_Biochim.Biophys.Acta_1441_185
PubMedID: 10570246

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Citations formats

Longhi S, Cambillau C (1999)
Structure-activity of cutinase, a small lipolytic enzyme
Biochimica & Biophysica Acta 1441 :185

Longhi S, Cambillau C (1999)
Biochimica & Biophysica Acta 1441 :185