在青霉素酶催化反应过程中获取底物特异性参数。
Acquisition of substrate-specific parameters during the catalytic reaction of penicillinase.
作者信息
Citri N, Samuni A, Zyk N
出版信息
Proc Natl Acad Sci U S A. 1976 Apr;73(4):1048-52. doi: 10.1073/pnas.73.4.1048.
Abstract
The progress of the catalytic reaction of penicillinase (EC 3.5.2.6; penicillin amido-beta-lactamhydrolase) depends on the structure of the side-chain in derivatives of 6-aminopenicillanic acid (the parent substrate). Side-chains of one class promote the rate of the reaction and cause no deviation from the linear kinetics observed with the parent compound. By contrast, side-chains of the other class induce a time-dependent, reversible change in the parameters of the catalytic reaction. The rate decelerates considerably and then becomes constant; the decrease in kcat is accompanied by a corresponding decrease in Km. The initial parameters of the biphasic reaction, determined by stopped-flow spectrophotometry, approach those of the unsubstituted 6-aminopenicillanic acid. The final parameters, which are specific for each derivative, are not acquired when the native conformation of the enzyme is stabilized by homologous antibodies.
摘要
青霉素酶（EC 3.5.2.6；青霉素酰胺基-β-内酰胺水解酶）催化反应的进程取决于6-氨基青霉烷酸（母体底物）衍生物中侧链的结构。一类侧链可促进反应速率，且不会偏离母体化合物所观察到的线性动力学。相比之下，另一类侧链会引起催化反应参数随时间的可逆变化。反应速率大幅下降，然后趋于恒定；催化常数（kcat）的降低伴随着米氏常数（Km）的相应降低。通过停流分光光度法测定的双相反应的初始参数接近未取代的6-氨基青霉烷酸的参数。当酶的天然构象通过同源抗体稳定时，不会获得每种衍生物特有的最终参数。
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