Glutathione transferases in bacteria

被引：267

作者：

Allocati, Nerino ^{[1
]}

Federici, Luca ^{[1
,2
]}

Masulli, Michele ^{[1
]}

Di Ilio, Carmine ^{[1
,2
]}

机构：

[1] Univ G DAnnunzio, Dipartimento Sci Biomed, I-66013 Chieti, Italy

[2] Univ G DAnnunzio, Ctr Studi Invecchiamento, CeSI, I-66013 Chieti, Italy

来源：

FEBS JOURNAL | 2009年 / 276卷 / 01期

关键词：

bacterial glutathione transferase; chemical stress; DCM dehalogenase; detoxification; drug resistance; fosfomycin resistance proteins; glutathione; HCCA isomerase; oxidative stress; TCHQ dehalogenase; FOSFOMYCIN RESISTANCE PROTEIN; SITE-DIRECTED MUTAGENESIS; AROMATIC-HYDROCARBON DEGRADATION; METHIONINE SULFOXIDE REDUCTASE; MEMBRANE-ASSOCIATED PROTEINS; SP STRAIN LB400; S-TRANSFERASE; ESCHERICHIA-COLI; OCHROBACTRUM-ANTHROPI; DICHLOROMETHANE DEHALOGENASE;

D O I：

10.1111/j.1742-4658.2008.06743.x

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：

Bacterial glutathione transferases (GSTs) are part of a superfamily of enzymes that play a key role in cellular detoxification. GSTs are widely distributed in prokaryotes and are grouped into several classes. Bacterial GSTs are implicated in a variety of distinct processes such as the biodegradation of xenobiotics, protection against chemical and oxidative stresses and antimicrobial drug resistance. In addition to their role in detoxification, bacterial GSTs are also involved in a variety of distinct metabolic processes such as the biotransformation of dichloromethane, the degradation of lignin and atrazine, and the reductive dechlorination of pentachlorophenol. This review article summarizes the current status of knowledge regarding the functional and structural properties of bacterial GSTs.

引用

页码：58 / 75

页数：18

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