Cysteinyl peptide inhibitors of Bacillus cereus zinc β-lactamase
Cysteinyl peptide inhibitors of Bacillus cereus zinc β-lactamase
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DOI：
10.1016/s0968-0896(00)00257-1
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发表时间：
2001-02-01
影响因子：
3.5
通讯作者：
Page, MI
中科院分区：
文献类型：
--
作者：
Bounaga, S;Galleni, M;Page, MI
已合成的几种半胱氨酸多肽被证明是蜡状芽孢杆菌金属β-内酰胺酶的可逆竞争抑制物。PK(I)的pH依赖关系表明，硫醇阴离子取代了活性中心锌(II)上的氢氧离子。D，D-肽与酶的结合比其他非对映异构体更好，这与预测的活性部位的立体化学相一致。(C)2001爱思唯尔科学有限公司。保留所有权利。
Several cysteinyl peptides have been synthesised and shown to be reversible competitive inhibitors of the Bacillus cereus metallo-beta -lactamase. The pH dependence of pK(i) indicates that the thiol anion displaces hydroxide ion from the active site zinc(II). D,D-Peptides bind to the enzyme better than other diastereoisomers, which is compatible with the predicted stereochemistry of the active site. (C) 2001 Elsevier Science Ltd. All rights reserved.