| Literature DB >> 8537283 |
T R Walsh1, L Hall, A P MacGowan, P M Bennett.
Abstract
Two beta-lactamase genes from Aeromonas sobria, strain 163a, have been cloned and sequenced, one encoding a typical class C cephalosporinase, designated CepS, the other a class D penicillinase, designated AmpS. CepS is predicted to be a mature protein of 38 kDa with a pI value of 7.0. The amino acid sequence of CepS is most similar to that of AmpC from Pseudomonas aeruginosa (54.7%). AmpS is predicted to be a mature protein of 27 kDa with a pI value of 7.9 that mostly closely resembles BLAD from Klebsiella pneumoniae (42.2%), and OXA-1 from Escherichia coli (36.6%), beta-lactamases that are encoded by genes carried on multiresistant transposons. AmpS differs significantly from the other class D beta-lactamases in that it hydrolyses cloxacillin poorly and is inducible. Both genes exhibit a high overall GC content and possess a high NNC and NNG codon preference, similar to that of genes from Pseudomonas spp.Entities:
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Year: 1995 PMID: 8537283 DOI: 10.1093/jac/36.1.41
Source DB: PubMed Journal: J Antimicrob Chemother ISSN: 0305-7453 Impact factor: 5.790