KINETIC-STUDY OF INTERACTION BETWEEN BRL-42715, BETA-LACTAMASES, AND D-ALANYL-D-ALANINE PEPTIDASES

被引：30

作者：

MATAGNE, A

LEDENT, P

MONNAIE, D

FELICI, A

JAMIN, M

RAQUET, X

GALLENI, M

KLEIN, D

FRANCOIS, I

FRERE, JM

机构：

[1] UNIV LIEGE,CTR INGN PROT,INST CHIM,ENZYMOL LAB,B-4000 SART,BELGIUM

[2] UNIV AQUILA,CATTEDRA CHIM BIOL,DIPARTIMENTO SCI & TECNOL BIOMED & BIOMETRIA,I-67010 COPPITO,ITALY

[3] SMITHKLINE BEECHAM PHARMACEUT,CHEMOTHERAPEUT RES CTR,DIV RES,BETCHWORTH RH3 7AJ,SURREY,ENGLAND

来源：

ANTIMICROBIAL AGENTS AND CHEMOTHERAPY | 1995年 / 39卷 / 01期

关键词：

D O I：

10.1128/AAC.39.1.227

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

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 3.4.1.16.4) is presented. The compound was a very efficient inactivator of all active-site serine beta-lactamases but was hydrolyzed by the class B, Zn2+-containing enzymes, with very different k(cat) 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.

引用

页码：227 / 231

页数：5

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