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.

引用

页码：729 / 734

页数：6

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