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Characterization of a beta-lactamase produced in Mycobacterium fortuitum D316.


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.

SUBMITTER: Amicosante G 

PROVIDER: S-EPMC1149623 | biostudies-other | 1990 Nov

REPOSITORIES: biostudies-other

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