Structure-activity of cutinase, a small lipolytic enzyme

被引：108

作者：

Longhi, S ^{[1
]}

Cambillau, C ^{[1
]}

机构：

[1] IFRI, CNRS, UPR 9039, F-13402 Marseille 20, France

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR AND CELL BIOLOGY OF LIPIDS | 1999年 / 1441卷 / 2-3期

关键词：

cutinase; lipases; crystal structure; hydrolase fold;

D O I：

10.1016/S1388-1981(99)00159-6

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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. (C) 1999 Elsevier Science B.V. All rights reserved.

引用

页码：185 / 196

页数：12

共 52 条

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