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CHARACTERIZATION OF A BETA-LACTAMASE PRODUCED IN MYCOBACTERIUM-FORTUITUM D316

被引：28
作者：
AMICOSANTE, G
FRANCESCHINI, N
SEGATORE, B
ORATORE, A
FATTORINI, L
OREFICI, G
VANBEEUMEN, J
FRERE, JM
机构：
[1] IST SUPER SANITA,BATTERIOL & MICOL MED,BACTERIOL LAB,I-00161 ROME,ITALY
[2] STATE UNIV GHENT,MICROBIOL LAB,B-9000 GHENT,BELGIUM
[3] STATE UNIV LIEGE,INST CHIM,ENZYMOL LAB,B-4000 LIEGE,BELGIUM
[4] STATE UNIV LIEGE,INST CHIM,SERV MICROBIOL,B-4000 LIEGE,BELGIUM
来源：
BIOCHEMICAL JOURNAL | 1990年 / 271卷 / 03期
关键词：
D O I：
10.1042/bj2710729
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：
A β-lactamase from Mycobacterium fortuitum D316 was purified and some physico-chemical properties and substrate profile determined. On the basis of its N-terminal sequence and of its sensitivity to β-iodopenicillanate inactivation, the enzyme appeared to be a class A β-lactamase, but its substrate profile was quite unexpected, since nine cephalosporins were among the eleven best substrates. The enzyme also hydrolysed ureidopenicillins and some so-called 'β-lactamase-stable' cephalosporins.
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页码：729 / 734
页数：6
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