Metallo-β-lactamase structure and function

被引:402
作者
Palzkill, Timothy [1 ]
机构
[1] Baylor Coll Med, Dept Pharmacol, Houston, TX 77030 USA
来源
ANTIMICROBIAL THERAPEUTICS REVIEWS: THE BACTERIAL CELL WALL AS AN ANTIMICROBIAL TARGET | 2013年 / 1277卷
关键词
beta-lactamase; antibiotic resistance; carbapenem; zinc metallo-enzyme; STANDARD NUMBERING SCHEME; PENICILLIN-BINDING PROTEINS; SITE-DIRECTED MUTAGENESIS; CRYSTAL-STRUCTURE; BACILLUS-CEREUS; PSEUDOMONAS-AERUGINOSA; ACTIVE-SITE; STENOTROPHOMONAS-MALTOPHILIA; ANTIBIOTIC-RESISTANCE; SUBSTRATE-BINDING;
D O I
10.1111/j.1749-6632.2012.06796.x
中图分类号
R9 [药学];
学科分类号
1007 ;
摘要
beta-Lactam antibiotics are the most commonly used antibacterial agents and growing resistance to these drugs is a concern. Metallo-beta-lactamases are a diverse set of enzymes that catalyze the hydrolysis of a broad range of beta-lactam drugs including carbapenems. This diversity is reflected in the observation that the enzyme mechanisms differ based on whether one or two zincs are bound in the active site that, in turn, is dependent on the subclass of beta-lactamase. The dissemination of the genes encoding these enzymes among Gram-negative bacteria has made them an important cause of resistance. In addition, there are currently no clinically available inhibitors to block metallo-beta-lactamase action. This review summarizes the numerous studies that have yielded insights into the structure, function, and mechanism of action of these enzymes.
引用
收藏
页码:91 / 104
页数:14
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