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. 1990 Nov 1;271(3):729-34.
doi: 10.1042/bj2710729.

Characterization of a beta-lactamase produced in Mycobacterium fortuitum D316

G Amicosante  1 , N Franceschini, B Segatore, A Oratore, L Fattorini, G Orefici, J Van Beeumen, J M Frere
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Characterization of a beta-lactamase produced in Mycobacterium fortuitum D316

G Amicosante et al. Biochem J. .

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.

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