KINETIC-ANALYSIS OF EXTENSION OF SUBSTRATE-SPECIFICITY WITH XANTHOMONAS-MALTOPHILIA, AEROMONAS-HYDROPHILA, AND BACILLUS-CEREUS METALLO-BETA-LACTAMASES

被引：74

作者：

FELICI, A ^{[1
]}

AMICOSANTE, G ^{[1
]}

机构：

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

来源：

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

关键词：

D O I：

10.1128/AAC.39.1.192

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

Twenty beta-tactam molecules, including penicillins, cephalosporins, penems, carbapenems, and monobactams, were investigated as potential substrates for Xanthomonas maltophilia ULA-511, Aeromonas hydrophila AE036, and Bacillus cereus 5/B/6 metallo-beta-lactamases. A detailed analysis of the kinetic parameters examined confirmed these enzymes to be broad-spectrum beta-lactamases with different ranges of catalytic efficiency. Cefoxitin and moxalactam, substrates for the beta-lactamases from X. maltophilia ULA-511 and B. cereus 5/B/6, behaved as inactivators of the A. hydrophila AE036 metallo-beta-lactamase,,which appeared to be unique among the enzymes tested in this study. In addition, we report a new, faster, and reliable purification procedure for the B. cereus 5/B/6 metallo-beta-lactamase, cloned in Escherichia coli HB101.

引用

页码：192 / 199

页数：8

共 19 条

[1] THE STRUCTURE OF BETA-LACTAMASES [J].