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.
Characterization of a β-lactamase produced in Mycobacterium fortuitum D316
- Views Icon Views
- Share Icon Share
- Cite Icon Cite
G Amicosante, N Franceschini, B Segatore, A Oratore, L Fattorini, G Orefici, J Van Beeumen, J M Frere; Characterization of a β-lactamase produced in Mycobacterium fortuitum D316. Biochem J 1 November 1990; 271 (3): 729–734. doi: https://doi.org/10.1042/bj2710729
Download citation file: