Metallo-β-lactamase structure and function
Article first published online: 16 NOV 2012
© 2012 New York Academy of Sciences.
Annals of the New York Academy of Sciences
Volume 1277, Antimicrobial Therapeutics Reviews pages 91–104, January 2013
How to Cite
Palzkill, T. (2013), Metallo-β-lactamase structure and function. Annals of the New York Academy of Sciences, 1277: 91–104. doi: 10.1111/j.1749-6632.2012.06796.x
- Issue published online: 24 JAN 2013
- Article first published online: 16 NOV 2012
- antibiotic resistance;
- zinc metallo-enzyme
β-Lactam antibiotics are the most commonly used antibacterial agents and growing resistance to these drugs is a concern. Metallo-β-lactamases are a diverse set of enzymes that catalyze the hydrolysis of a broad range of β-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 β-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-β-lactamase action. This review summarizes the numerous studies that have yielded insights into the structure, function, and mechanism of action of these enzymes.