INTERACTION OF CLAVULANATE WITH CLASS-C BETA-LACTAMASES

被引：20
作者：
MONNAIE, D
FRERE, JM
机构：
[1] UNIV LIEGE,CTR INGN PROTEINES,B6 SART TILMAN,B-4000 LIEGE,BELGIUM
[2] UNIV LIEGE,ENZYMOL LAB,B-4000 LIEGE,BELGIUM
来源：
FEBS LETTERS | 1993年 / 334卷 / 03期
关键词：
BETA-LACTAMASE; CLAVULANIC ACID; AMPC; ENTEROBACTER CLOACAE 908R; SERRATIA-MARCESCENS; ESCHERICHIA-COLI K12;
D O I：
10.1016/0014-5793(93)80692-N
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
The interactions between clavulanate and three class C enzymes have been studied in detail. In all cases, the reactions followed branched pathways where 25-150 turnovers occurred before inactivation was completed. Reactivation rates were quite low. The poor efficiency of clavulanate as a class C inactivator appeared to rest upon a very slow acylation of the protein, and of a relatively high turnover rate.
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页码：269 / 271
页数：3
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