Mechanistic imperatives for the evolution of glutathione transferases

被引：45

作者：

Armstrong, RN ^{[1
]}

机构：

[1] Vanderbilt Univ, Sch Med, Dept Biochem, Nashville, TN 37232 USA

[2] Vanderbilt Univ, Sch Med, Dept Chem, Nashville, TN 37232 USA

[3] Vanderbilt Univ, Sch Med, Ctr Mol Toxicol, Nashville, TN 37232 USA

来源：

CURRENT OPINION IN CHEMICAL BIOLOGY | 1998年 / 2卷 / 05期

关键词：

D O I：

10.1016/S1367-5931(98)80093-8

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：

Several significant advances in the understanding of the catalytic mechanisms, structures and evolution of glutathione transferases have occurred in the past year. These advances include new mechanistic information concerning the canonical soluble enzymes, the finding that the fosfomycin-specific enzyme, FosA, is a metalloglutathione transferase and a higher resolution projection structure of the microsomal enzyme.

引用

页码：618 / 623

页数：6

共 55 条

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