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阴沟肠杆菌908R中C类β-内酰胺酶的快速动力学研究。

A rapid-kinetic study of the class C beta-lactamase of Enterobacter cloacae 908R.

作者信息

Monnaie D, Virden R, Frère J M

机构信息

Laboratoire d'enzymologie, Université de Liège, Belgium.

出版信息

FEBS Lett. 1992 Jul 20;306(2-3):108-12. doi: 10.1016/0014-5793(92)80979-q.

DOI:10.1016/0014-5793(92)80979-q
PMID:1633864
Abstract

The individual rate constants for acylation and deacylation (k2 and k3, respectively) of the class C beta-lactamase of Enterobacter cloacae 908R by ampicillin and carbenicillin have been determined. For several other beta-lactams, the value of k2 was too high to be determined and the k2/k3 ratio could be larger than 10,000. Branched pathways were also shown to occur with several penicillins and cephalosporins.

摘要

已测定氨苄西林和羧苄西林对阴沟肠杆菌908R的C类β-内酰胺酶进行酰化和去酰化反应的个体速率常数(分别为k2和k3)。对于其他几种β-内酰胺类药物,k2的值过高无法测定,且k2/k3比值可能大于10,000。还发现几种青霉素和头孢菌素存在分支途径。

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1
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2
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引用本文的文献

1
A dramatic change in the rate-limiting step of beta-lactam hydrolysis results from the substitution of the active-site serine residue by a cysteine in the class-C beta-lactamase of Enterobacter cloacae 908R.阴沟肠杆菌908R的C类β-内酰胺酶中,活性位点丝氨酸残基被半胱氨酸取代,导致β-内酰胺水解限速步骤发生显著变化。
Biochem J. 1993 Jun 1;292 ( Pt 2)(Pt 2):537-43. doi: 10.1042/bj2920537.
2
Interactions between active-site-serine beta-lactamases and compounds bearing a methoxy side chain on the alpha-face of the beta-lactam ring: kinetic and molecular modelling studies.活性位点丝氨酸β-内酰胺酶与β-内酰胺环α-面上带有甲氧基侧链的化合物之间的相互作用:动力学和分子模拟研究
Biochem J. 1993 Aug 1;293 ( Pt 3)(Pt 3):607-11. doi: 10.1042/bj2930607.
3
Substrate-induced inactivation of the OXA2 beta-lactamase.底物诱导的OXA2β-内酰胺酶失活
Biochem J. 1993 Nov 1;295 ( Pt 3)(Pt 3):871-8. doi: 10.1042/bj2950871.
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The kinetics of non-stoichiometric bursts of beta-lactam hydrolysis catalysed by class C beta-lactamases.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。
Biochem J. 1993 Oct 1;295 ( Pt 1)(Pt 1):295-304. doi: 10.1042/bj2950295.
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The role of lysine-67 in a class C beta-lactamase is mainly electrostatic.赖氨酸67在C类β-内酰胺酶中的作用主要是静电作用。
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