Walsh T R, Hall L, MacGowan A P, Bennett P M
Department of Microbiology and Pathology, School of Medical Sciences, University of Bristol, UK.
J Antimicrob Chemother. 1995 Jul;36(1):41-52. doi: 10.1093/jac/36.1.41.
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.
已对温和气单胞菌163a菌株的两个β-内酰胺酶基因进行了克隆和测序,一个编码典型的C类头孢菌素酶,命名为CepS,另一个编码D类青霉素酶,命名为AmpS。预测CepS是一种成熟蛋白,分子量为38 kDa,pI值为7.0。CepS的氨基酸序列与铜绿假单胞菌的AmpC最为相似(54.7%)。预测AmpS是一种成熟蛋白,分子量为27 kDa,pI值为7.9,与肺炎克雷伯菌的BLAD(42.2%)和大肠杆菌的OXA-1(36.6%)最为相似,这些β-内酰胺酶由多耐药转座子携带的基因编码。AmpS与其他D类β-内酰胺酶的显著不同之处在于,它对氯唑西林的水解能力较差且具有诱导性。这两个基因的总体GC含量都很高,并且具有较高的NNC和NNG密码子偏好性,这与假单胞菌属的基因相似。