Structure and mechanism of bacterial dehalogenases: different ways to cleave a carbon-halogen bond

被引：76

作者：

de Jong, RM ^{[1
]}

Dijkstra, BW ^{[1
]}

机构：

[1] Univ Groningen, Groningen Biomol Sci & Biotechnol Inst, Dept Biophys Chem, NL-9747 AG Groningen, Netherlands

来源：

CURRENT OPINION IN STRUCTURAL BIOLOGY | 2003年 / 13卷 / 06期

关键词：

D O I：

10.1016/j.sbi.2003.10.009

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 dehalogenases make use of fundamentally different strategies to cleave carbon-halogen bonds. The structurally characterized haloalkane dehalogenases, haloacid dehalogenases and 4-chlorobenzoate-coenzyme A dehalogenases use substitution mechanisms that proceed via a covalent aspartyl intermediate. Recent X-ray crystallographic analysis of a haloalcohol dehalogenase and a trans-3-chloroacrylic acid dehalogenase has provided detailed insight into a different intramolecular substitution mechanism and a hydratase-like mechanism, respectively. The available information on the various dehalogenases supports different views on the possible evolutionary origins of their activities.

引用

页码：722 / 730

页数：9

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