Integron-sequestered dihydrofolate reductase: a recently redeployed enzyme

被引：21

作者：

Alonso, Hernan ^{[1
]}

Gready, Jill E. ^{[1
]}

机构：

[1] Australian Natl Univ, Div Mol Biosci, John Curtin Sch Med Res, Canberra, ACT 0200, Australia

来源：

TRENDS IN MICROBIOLOGY | 2006年 / 14卷 / 05期

关键词：

D O I：

10.1016/j.tim.2006.03.003

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 introduction and wide use of antibacterial drugs has resulted in the emergence of resistant organisms. DfrB dihydrofolate reductase (DHFR) is a bacterial enzyme that is uniquely associated with mobile gene cassettes within integrons, and confers resistance to the drug trimethoprim. This enzyme has intrigued microbiologists since it was discovered more than thirty years ago because of its simple structure, enzymatic inefficiency and its virtual insensitivity to trimethoprim. Here, for the first time, a comprehensive discussion of genetic, evolutionary, structural and functional studies of this enzyme is presented together. This information supports the ideas that DfrB DHFR is a poorly adapted catalyst and has recently been recruited to perform a novel enzymatic activity in response to selective pressure.

引用

页码：236 / 242

页数：7

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