Fosfomycin resistance proteins: A nexus of glutathione transferases and epoxide hydrolases in a metalloenzyme superfamily

被引：70

作者：

Rigsby, RE ^{[1
]}

Fillgrove, KL ^{[1
]}

Beihoffer, LA ^{[1
]}

Armstrong, RN ^{[1
]}

机构：

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

来源：

GLUTHIONE TRANSFERASES AND GAMMA-GLUTAMYL TRANSPEPTIDASES | 2005年 / 401卷

关键词：

D O I：

10.1016/S0076-6879(05)01023-2

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Three similar but mechanistically distinct fosfomycin resistance proteins that catalyze the opening of the oxirane ring of the antibiotic are known. FosA is a Mn(II) and K(+)-dependent glutathione transferase. FosB is a Mg(2+)-dependent L-cysteine thiol transferase. FosX is a Mn(II)-dependent fosfomycin-specific epoxide hydrolase. The expression, purification, kinetic, and physical characteristics of six fosfomycin resistance proteins including the FosA proteins from transposon TN2921 and Pseudomonas aeruginosa, the FosB proteins from Bacillus subtilis and Staphylococcus aureus, and the FosX proteins from Mesorhizobium. loti and Listeria monocytogenes are reported.

引用

页码：367 / 379

页数：13

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