期刊
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
卷 124, 期 11, 页码 2461-2465出版社
AMER CHEMICAL SOC
DOI: 10.1021/ja016736t
关键词
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beta-Lactamases are resistance enzymes for beta-lactam antibiotics. These enzymes hydrolyze the beta-lactam moieties of these antibiotics, rendering them inactive. Of the four classes of known beta-lactamases, the enzymes of class D are the least understood. We report herein the high-resolution (1.9 Angstrom) crystal structure of the class D OXA-10 beta-lactamase inhibited by a penicillanate derivative. The structure provides evidence that the carboxylated Lys-70 (a carbamate) is intimately involved in the mechanism of the enzyme.
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