BRL 42715、β-内酰胺酶和D-丙氨酰-D-丙氨酸肽酶之间相互作用的动力学研究
Kinetic study of interaction between BRL 42715, beta-lactamases, and D-alanyl-D-alanine peptidases.
作者信息
Matagne A, Ledent P, Monnaie D, Felici A, Jamin M, Raquet X, Galleni M, Klein D, François I, Frère J M
机构信息
Laboratoire d'Enzymologie, Université de Liège, Sart-Tilman, Belgium.
出版信息
Antimicrob Agents Chemother. 1995 Jan;39(1):227-31. doi: 10.1128/AAC.39.1.227.
Abstract
A detailed kinetic study of the interactions between BRL 42715, a beta-lactamase-inhibiting penem, and various beta-lactamases (EC 3.5.2.6) and D-alanyl-D-alanine peptidases (DD-peptidases, EC 3.4.16.4) is presented. The compound was a very efficient inactivator of all active-site serine beta-lactamases but was hydrolyzed by the class B, Zn(2+)-containing enzymes, with very different kcat values. Inactivation of the Streptomyces sp. strain R61 extracellular DD-peptidase was not observed, and the Actinomadura sp. strain R39 DD-peptidase exhibited a low level of sensitivity to the compound.
摘要
本文介绍了β-内酰胺酶抑制性青霉烯类药物BRL 42715与各种β-内酰胺酶（EC 3.5.2.6）和D-丙氨酰-D-丙氨酸肽酶（DD-肽酶，EC 3.4.16.4）之间相互作用的详细动力学研究。该化合物是所有活性位点丝氨酸β-内酰胺酶的高效失活剂，但会被B类含锌（2+）酶水解，其催化常数（kcat）值差异很大。未观察到链霉菌属R61菌株细胞外DD-肽酶的失活，而马杜拉放线菌属R39菌株的DD-肽酶对该化合物表现出较低的敏感性。
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