| Literature DB >> 2123098 |
G Amicosante1, N Franceschini, B Segatore, A Oratore, L Fattorini, G Orefici, J Van Beeumen, J M Frere.
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.Entities:
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Year: 1990 PMID: 2123098 PMCID: PMC1149623 DOI: 10.1042/bj2710729
Source DB: PubMed Journal: Biochem J ISSN: 0264-6021 Impact factor: 3.857