Literature DB >> 2661324

TEM-E1: a novel beta-lactamase conferring resistance to ceftazidime.

D J Payne1, M S Marriott, S G Amyes.   

Abstract

A novel beta-lactamase, conferring resistance to ceftazidime, has been identified to be encoded by a 31 kb plasmid (pUK720) in a clinical E. coli strain isolated in Belgium. The beta-lactamase, new designated TEM-E1, has a pI of approximately 5.4 and lies in between the iso-electric focused bands of the beta-lactamases TEM-1 and TEM-7. The TEM-E1 beta-lactamase has a similar molecular weight of 22,000 to the TEM-1 and it is also inhibited by clavulanic acid. However, the TEM-E1 enzyme differs from TEM-1 by its low rates and efficiency of hydrolysis for ceftazidime and cefotaxime, TEM-E1 has similar efficiency of hydrolysis values for ceftazidime and cefotaxime, but only confers resistance to ceftazidime.

Entities:  

Mesh:

Substances:

Year:  1989        PMID: 2661324     DOI: 10.1016/0378-1097(89)90466-7

Source DB:  PubMed          Journal:  FEMS Microbiol Lett        ISSN: 0378-1097            Impact factor:   2.742


  2 in total

Review 1.  Beta-lactamase nomenclature.

Authors:  George A Jacoby
Journal:  Antimicrob Agents Chemother       Date:  2006-04       Impact factor: 5.191

Review 2.  More extended-spectrum beta-lactamases.

Authors:  G A Jacoby; A A Medeiros
Journal:  Antimicrob Agents Chemother       Date:  1991-09       Impact factor: 5.191

  2 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.