金黄色葡萄球菌PC1的A类β-内酰胺酶在青霉素周转过程中酰基酶中间体的积累。
Accumulation of acyl-enzyme intermediates during turnover of penicillins by the class A beta-lactamase of Staphylococcus aureus PC1.
作者信息
Pratt R F, McConnell T S, Murphy S J
机构信息
Department of Chemistry, Wesleyan University, Middletown, CT 06457.
出版信息
Biochem J. 1988 Sep 15;254(3):919-22. doi: 10.1042/bj2540919.
Abstract
The interaction of dansylpenicillin with the class A Staphylococcus aureus PCI beta-lactamase yielded an accumulating intermediate with fluorescence enhanced beyond that of the substrate. Acid quenching of the reaction mixture yielded a denatured enzyme with 1 molar equivalent of dansyl group covalently bound to it. A similar quenching experiment with the PC1 beta-lactamase and [14C]benzylpenicillin yielded an enzyme with 1 molar equivalent of 14C covalently bound. These data indicate that in turnover of S-type penicillins by the PC1 beta-lactamase deacylation is rate-determining. This has not indicate previously been demonstrated for a class A beta-lactamase.
摘要
丹磺酰青霉素与A类金黄色葡萄球菌PCIβ-内酰胺酶相互作用产生了一种积累中间体，其荧光增强程度超过底物。对反应混合物进行酸淬灭得到一种变性酶，该酶共价结合有1摩尔当量的丹磺酰基团。用PC1β-内酰胺酶和[14C]苄青霉素进行类似的淬灭实验得到一种共价结合有1摩尔当量14C的酶。这些数据表明，在PC1β-内酰胺酶催化S型青霉素周转过程中，脱酰化是速率决定步骤。此前尚未在A类β-内酰胺酶中证实这一点。
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