共 26 条
Nucleophile recognition as an alternative inhibition mode for benzoic acid based carbonic anhydrase inhibitors
被引:47
作者:

Martin, David P.
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机构:
Univ Calif San Diego, Dept Chem & Biochem, La Jolla, CA 92093 USA Univ Calif San Diego, Dept Chem & Biochem, La Jolla, CA 92093 USA

Cohen, Seth M.
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h-index: 0
机构:
Univ Calif San Diego, Dept Chem & Biochem, La Jolla, CA 92093 USA Univ Calif San Diego, Dept Chem & Biochem, La Jolla, CA 92093 USA
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.
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页码:5259 / 5261
页数:3
相关论文
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