Characterization of a β-lactamase produced in Mycobacterium fortuitum D316
- 1 November 1990
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 271 (3) , 729-734
- https://doi.org/10.1042/bj2710729
Abstract
A .beta.-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 .beta.-iodopenicillanate inactivation, the enzyme appeared to be a class A .beta.-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 ''.beta.-lactamase-stable'' cephalosporins.This publication has 24 references indexed in Scilit:
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