β-内酰胺酶I酰基酶机制的动力学表征
Kinetic characterization of the acyl-enzyme mechanism for beta-lactamase I.
作者信息
Martin M T, Waley S G
机构信息
Sir William Dunn School of Pathology, University of Oxford, U.K.
出版信息
Biochem J. 1988 Sep 15;254(3):923-5. doi: 10.1042/bj2540923.
Abstract
beta-Lactamase I catalyses the hydrolysis of penicillins by an acyl-enzyme mechanism. A procedure was developed for determining the rate constants for the acylation and deacylation steps for the good substrates benzylpenicillin and phenoxymethylpenicillin; this depends on determining the fraction of enzyme that is present as acyl-enzyme in the steady state.
摘要
β-内酰胺酶I通过酰基-酶机制催化青霉素的水解。已开发出一种程序来测定良好底物苄青霉素和苯氧甲基青霉素的酰化和脱酰化步骤的速率常数；这取决于确定在稳态下以酰基-酶形式存在的酶的比例。
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The preparation and some properties of penicillenic acid derivatives relevant to penicillin hypersensitivity.与青霉素过敏相关的青霉烯酸衍生物的制备及某些性质
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Single-turnover and steady-state kinetics of hydrolysis of cephalosporins by beta-lactamase I from Bacillus cereus.蜡样芽孢杆菌β-内酰胺酶I催化头孢菌素水解的单周转和稳态动力学
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10
Tertiary structural similarity between a class A beta-lactamase and a penicillin-sensitive D-alanyl carboxypeptidase-transpeptidase.A类β-内酰胺酶与青霉素敏感的D-丙氨酰羧肽酶-转肽酶之间的三级结构相似性。
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