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Characterization of a beta-lactamase produced in Mycobacterium fortuitum D316
G Amicosante1, N Franceschini, B Segatore
1Università degli Studi dell'Aquila, Dipartimento di Scienze e Tecnologie Biomediche e Biometria, L'Aquila, Italy.
The Biochemical Journal
|November 1, 1990
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.