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. 1990 Nov 1;271(3):729–734. doi: 10.1042/bj2710729

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

G Amicosante 1, N Franceschini 1, B Segatore 1, A Oratore 1, L Fattorini 1, G Orefici 1, J Van Beeumen 1, J M Frere 1
PMCID: PMC1149623  PMID: 2123098

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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Selected References

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