Unknown

Dataset Information

0

CTX-M-190, a Novel ?-Lactamase Resistant to Tazobactam and Sulbactam, Identified in an Escherichia coli Clinical Isolate.


ABSTRACT: A novel ?-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 ?M-1 s-1, and was highly resistant to inhibition by the ?-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.

SUBMITTER: Shen Z 

PROVIDER: S-EPMC5192109 | biostudies-literature | 2017 Jan

REPOSITORIES: biostudies-literature

altmetric image

Publications

CTX-M-190, a Novel β-Lactamase Resistant to Tazobactam and Sulbactam, Identified in an Escherichia coli Clinical Isolate.

Shen Zhen Z   Ding Baixing B   Bi Yingmin Y   Wu Shi S   Xu Su S   Xu Xiaogang X   Guo Qinglan Q   Wang Minggui M  

Antimicrobial agents and chemotherapy 20161227 1


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 k<sub>cat</sub>/K<sub>m</sub> ratio of 14.5 μM<sup>-1</sup> s<sup>-1</sup>, and was highly resistant to inhibition by the β-lactamase inhibitors tazobactam and sulbactam, whose 50% inhibitory concentrations were 77- and 55-fold higher, resp  ...[more]

Similar Datasets

| S-EPMC3273006 | biostudies-literature
| S-EPMC3322752 | biostudies-literature
| S-EPMC3458832 | biostudies-literature
| S-EPMC127230 | biostudies-literature
| S-EPMC434168 | biostudies-literature
| S-EPMC6355572 | biostudies-literature
| S-EPMC7577136 | biostudies-literature
| S-EPMC2600198 | biostudies-literature
| S-EPMC4187903 | biostudies-literature