| Literature DB >> 27821452 |
Zhen Shen1,2, Baixing Ding1,2, Yingmin Bi1,2, Shi Wu1,2, Su Xu1,2, Xiaogang Xu1,2, Qinglan Guo1,2, Minggui Wang3,2.
Abstract
A novel β-lactamase, CTX-M-190, derived from CTX-M-55 by a single substitution of Ser for Thr at position 133 (Ser133Thr), was identified in a natural Escherichia coli clinical isolate. CTX-M-190 exhibited potent hydrolytic activity against cefotaxime, with a kcat/Km ratio of 14.5 μM-1 s-1, and was highly resistant to inhibition by the β-lactamase inhibitors tazobactam and sulbactam, whose 50% inhibitory concentrations were 77- and 55-fold higher, respectively, for CTX-M-190 than for CTX-M-55. blaCTX-M-190 was located within the genetic platform ISEcp1-blaCTX-M-orf477, which was harbored by a 70-kb IncI1 plasmid.Entities:
Keywords: CTX-M-190; Escherichia coli; inhibitor-resistant β-lactamase; sulbactam; tazobactam
Mesh:
Substances:
Year: 2016 PMID: 27821452 PMCID: PMC5192109 DOI: 10.1128/AAC.01848-16
Source DB: PubMed Journal: Antimicrob Agents Chemother ISSN: 0066-4804 Impact factor: 5.191