Nucleophile recognition as an alternative inhibition mode for benzoic acid based carbonic anhydrase inhibitors

被引:47
作者
Martin, David P. [1 ]
Cohen, Seth M. [1 ]
机构
[1] Univ Calif San Diego, Dept Chem & Biochem, La Jolla, CA 92093 USA
基金
美国国家卫生研究院;
关键词
MATRIX-METALLOPROTEINASE INHIBITORS; ERYTHROCYTE ISOZYMES I; VITRO INHIBITION; ACTIVE-SITE; SERIES; BINDING; PHENOLS;
D O I
10.1039/c2cc32013d
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
A series of hydroxybenzoic acid derivatives have shown inhibitory activity against carbonic anhydrase (CA). X-ray crystallography shows that these molecules inhibit not by binding the active site metal ion but by strong hydrogen bonding to the metal-bound water nucleophile. The binding mode observed for these molecules is distinct when compared to other non-metal-binding CA inhibitors.
引用
收藏
页码:5259 / 5261
页数:3
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