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2
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Hysteretic enzymes.滞后酶
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The E. coli beta-lactamase attenuator mediates growth rate-dependent regulation.大肠杆菌β-内酰胺酶衰减子介导生长速率依赖性调控。
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Mechanism of substrate-induced inactivation of beta-lactamase I.底物诱导β-内酰胺酶I失活的机制。
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Kinetics of protein modification reactions.蛋白质修饰反应的动力学
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Purification of beta-lactamases by affinity chromatography on phenylboronic acid-agarose.通过苯基硼酸 - 琼脂糖亲和层析法纯化β - 内酰胺酶。
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The reversible deactivation of beta-lactamase from Staphylococcus aureus by quinacillin and cephaloridine and its modification by antibodies.喹那西林和头孢菌素对金黄色葡萄球菌β-内酰胺酶的可逆失活作用及其抗体修饰
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C类β-内酰胺酶催化的β-内酰胺水解非化学计量爆发动力学。

The kinetics of non-stoichiometric bursts of beta-lactam hydrolysis catalysed by class C beta-lactamases.

作者信息

Page M G

机构信息

Pharma Division, Preclinical Research, F. Hoffmann-La Roche Ltd., Basel, Switzerland.

出版信息

Biochem J. 1993 Oct 1;295 ( Pt 1)(Pt 1):295-304. doi: 10.1042/bj2950295.

DOI:10.1042/bj2950295
PMID:8216231
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1134852/
Abstract

Class C beta-lactamases from Pseudomonas aeruginosa and several species of the Enterobacteriaceae have been observed to undergo a rapid burst in hydrolysis of beta-lactam antibiotics before relaxation to a steady-state rate of hydrolysis. The amplitude of the burst corresponds to the hydrolysis of between 1 and 10,000 mol of the substrate per mol of enzyme. The decay of the rate of hydrolysis in the burst phase comprises two exponential reactions, which indicates that there are three different reactive states of the enzymes. Examination of the kinetics of acylation by slowly reacting beta-lactams suggests that there are three forms of the free enzyme in slow equilibrium. Thus it would appear that the burst kinetics exhibited by class C enzymes can be attributed to redistribution of the enzyme between different conformations induced by the reaction with substrate.

摘要

已观察到铜绿假单胞菌和几种肠杆菌科细菌的C类β-内酰胺酶在弛豫到稳定水解速率之前，会对β-内酰胺抗生素进行快速的水解爆发。爆发的幅度相当于每摩尔酶水解1至10,000摩尔底物。爆发阶段水解速率的衰减包括两个指数反应，这表明酶存在三种不同的反应状态。对缓慢反应的β-内酰胺进行酰化动力学研究表明，游离酶有三种形式处于缓慢平衡状态。因此，C类酶表现出的爆发动力学似乎可归因于酶在与底物反应诱导的不同构象之间的重新分布。