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.
Characterization of a β-lactamase produced in Mycobacterium fortuitum D316
AMICOSANTE, Gianfranco;FRANCESCHINI, Nicola;SEGATORE, Bernardetta;ORATORE, Arduino;
1990-01-01
Abstract
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.File in questo prodotto:
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