Structural classification and properties of ketoacyl reductases, hydroxyacyl dehydratases and enoyl reductases

被引：6

作者：

Cantu, David C. ^{[1
]}

Dai, Tingsong ^{[1
]}

Beversdorf, Zachary S. ^{[1
]}

Reilly, Peter J. ^{[1
]}

机构：

[1] Iowa State Univ, Dept Chem & Biol Engn, Ames, IA 50011 USA

来源：

PROTEIN ENGINEERING DESIGN & SELECTION | 2012年 / 25卷 / 12期

基金：

美国国家科学基金会;

关键词：

enoyl reductase; fatty acid synthesis cycle; hydroxyacyl dehydratase; ketoacyl reductase; polyketide synthesis cycle; FATTY-ACID SYNTHASE; 2-ENOYL THIOESTER REDUCTASE; CRYSTAL-STRUCTURE; MOLECULAR-CLONING; COA HYDRATASE; ACP REDUCTASE; PROTEIN; GENE; COENZYME; ENZYMES;

D O I：

10.1093/protein/gzs050

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：

Ketoacyl reductases (KRs), hydroxyacyl dehydratases (HDs) and enoyl reductases (ERs) are part of the fatty acid and polyketide synthesis cycles. Their reverse reactions, catalyzed by acyl dehydrogenases (equivalent to ERs), enoyl hydratases (equivalent to HDs) and hydroxyacyl dehydrogenases (equivalent to KRs), are part of fatty acid degradation by -oxidation. These enzymes have been classified into families based on similarities in their primary and tertiary structures, and these families and their structures are included in the ThYme (Thioester-active enzYmes) database. Members of each family have strong sequence similarity and have essentially the same tertiary structure, mechanism and catalytic residues.

引用

页码：803 / 811

页数：9

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