4.7 Article Book Chapter

Metallo-beta-lactamase structure and function

出版社

BLACKWELL SCIENCE PUBL
DOI: 10.1111/j.1749-6632.2012.06796.x

关键词

beta-lactamase; antibiotic resistance; carbapenem; zinc metallo-enzyme

资金

  1. NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES [R01AI032956, R37AI032956] Funding Source: NIH RePORTER
  2. NIAID NIH HHS [AI32956, R01 AI032956, R37 AI032956, R56 AI032956] Funding Source: Medline

向作者/读者索取更多资源

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.

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