期刊
CURRENT PROTEIN & PEPTIDE SCIENCE
卷 10, 期 5, 页码 401-407出版社
BENTHAM SCIENCE PUBL LTD
DOI: 10.2174/138920309789351967
关键词
-
资金
- NIAID NIH HHS [R01 AI033170] Funding Source: Medline
The discovery that the mechanism of beta-lactam hydrolysis catalyzed by the class A (active site serine-dependent) beta-lactamases proceeds via an acyl-enzyme intermediate was made thirty years ago. Since this discovery, the active site circumstance that enables acylation of the active site serine and further enables hydrolytic deacylation of the acyl-serine intermediate, has received extraordinary scrutiny. The justification for this scrutiny is the direct relevance of the beta-lactamases to the manifestation of bacterial resistance to the beta-lactam antibiotics, and the subsequent (to the discovery of the beta-lactamase acyl-enzyme) recognition of the direct evolutionary relationship between the serine beta-lactamase acyl-enzyme, and the penicillin binding protein acyl-enzyme that is key to beta-lactam antibiotic activity. This short review describes the early events leading to the recognition that serine beta-lactamase catalysis proceeds via an acyl-enzyme intermediate, and summarizes several of the key mechanistic studies-including infrared spectroscopy, cryoenzymology, beta-lactam design, and x-ray crystallography-that have been exploited to understand this pivotal catalytic intermediate.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据