THE CRYSTAL-STRUCTURE OF TRIACYLGLYCEROL LIPASE FROM PSEUDOMONAS-GLUMAE REVEALS A PARTIALLY REDUNDANT CATALYTIC ASPARTATE

被引：243

作者：

NOBLE, MEM ^{[1
]}

CLEASBY, A ^{[1
]}

JOHNSON, LN ^{[1
]}

EGMOND, MR ^{[1
]}

FRENKEN, LGJ ^{[1
]}

机构：

[1] UNILEVER RES LABS,3133 AT VLAARDINGEN,NETHERLANDS

来源：

FEBS LETTERS | 1993年 / 331卷 / 1-2期

关键词：

TRIACYLGLYCEROL ACYLHYDROLASE; EC; 3.1.1.3; CRYSTAL STRUCTURE; DENSITY MODIFICATION; CATALYTIC TRIAD; HYDROLASE FOLD;

D O I：

10.1016/0014-5793(93)80310-Q

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：

The family of lipases (triacylglycerol-acyl-hydrolases, EC 3.1.1.3) constitutes an interesting class of enzymes because of their ability to interact with lipid-water interfaces, their wide range of substrate specificities, and their potential industrial applications [1,2]. Here we report the first crystal structure of a bacterial lipase, from Pseudomonas glumae. The structure is formed from three domains, the largest of which contains a subset of the alpha/beta hydrolase fold and a calcium site. Asp263, the acidic residue in the catalytic triad, has previously been mutated into an alanine with only a modest reduction in activity [3].

引用

页码：123 / 128

页数：6

共 29 条

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