Literature DB >> 11498383

beta -Lactamases: which ones are clinically important?

Louis B. Rice1, Robert A. Bonomo.   

Abstract

The introduction of a large array of beta-lactam antibiotics has spawned the emergence of an even larger variety of beta-lactamases designed to confer resistance to these agents. beta-lactamases are produced by both gram-positive and gram-negative bacteria, but their clinical importance is far greater among the gram-negatives. The virtual explosion in our knowledge about the variety of these enzymes can often create confusion and frustration among those not well versed in the field. In this paper, we attempt to focus the discussion of beta-lactamases on those enzymes that are of the greatest clinical importance, the Ambler Class A and C enzymes. We also discuss the growing importance of the Ambler Class B metallo beta-lactamases, which hydrolyze carbapenems and are increasing in prevalence in areas of significant carbapenem usage. Copyright 2000 Harcourt Publishers Ltd.

Entities:  

Year:  2000        PMID: 11498383     DOI: 10.1054/drup.2000.0144

Source DB:  PubMed          Journal:  Drug Resist Updat        ISSN: 1368-7646            Impact factor:   18.500


  12 in total

1.  Monitoring the zinc affinity of the metallo-beta-lactamase CphA by automated nanoESI-MS.

Authors:  Kris De Vriendt; Gonzalez Van Driessche; Bart Devreese; Carine Bebrone; Christine Anne; Jean-Marie Frère; Moreno Galleni; Jozef Van Beeumen
Journal:  J Am Soc Mass Spectrom       Date:  2006-01-10       Impact factor: 3.109

2.  Improved annotation of antibiotic resistance determinants reveals microbial resistomes cluster by ecology.

Authors:  Molly K Gibson; Kevin J Forsberg; Gautam Dantas
Journal:  ISME J       Date:  2014-07-08       Impact factor: 10.302

3.  Structure-based optimization of a non-beta-lactam lead results in inhibitors that do not up-regulate beta-lactamase expression in cell culture.

Authors:  Donatella Tondi; Federica Morandi; Richard Bonnet; M Paola Costi; Brian K Shoichet
Journal:  J Am Chem Soc       Date:  2005-04-06       Impact factor: 15.419

4.  Identification, characterization, and regulation of a cluster of genes involved in carbapenem biosynthesis in Photorhabdus luminescens.

Authors:  Sylviane Derzelle; Eric Duchaud; Frank Kunst; Antoine Danchin; Philippe Bertin
Journal:  Appl Environ Microbiol       Date:  2002-08       Impact factor: 4.792

5.  Structure of AmpC beta-lactamase (AmpCD) from an Escherichia coli clinical isolate with a tripeptide deletion (Gly286-Ser287-Asp288) in the H10 helix.

Authors:  Yoshihiro Yamaguchi; Genta Sato; Yuriko Yamagata; Yohei Doi; Jun-ichi Wachino; Yoshichika Arakawa; Koki Matsuda; Hiromasa Kurosaki
Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun       Date:  2009-05-22

6.  Mechanism of action of NB2001 and NB2030, novel antibacterial agents activated by beta-lactamases.

Authors:  Geoffrey W Stone; Qin Zhang; Rosario Castillo; V Ramana Doppalapudi; Analia R Bueno; Jean Y Lee; Qing Li; Maria Sergeeva; Gody Khambatta; Nafsika H Georgopapadakou
Journal:  Antimicrob Agents Chemother       Date:  2004-02       Impact factor: 5.191

7.  Differential binding of Co(II) and Zn(II) to metallo-beta-lactamase Bla2 from Bacillus anthracis.

Authors:  Megan J Hawk; Robert M Breece; Christine E Hajdin; Katherine M Bender; Zhenxin Hu; Alison L Costello; Brian Bennett; David L Tierney; Michael W Crowder
Journal:  J Am Chem Soc       Date:  2009-08-05       Impact factor: 15.419

8.  Biochemical characterization of CTX-M-15 from Enterobacter cloacae and designing a novel non-β-lactam-β-lactamase inhibitor.

Authors:  Mohammad Faheem; Md Tabish Rehman; Mohd Danishuddin; Asad U Khan
Journal:  PLoS One       Date:  2013-02-21       Impact factor: 3.240

9.  Probing substrate binding to metallo-beta-lactamase L1 from Stenotrophomonas maltophilia by using site-directed mutagenesis.

Authors:  Anne L Carenbauer; James D Garrity; Gopal Periyannan; Robert B Yates; Michael W Crowder
Journal:  BMC Biochem       Date:  2002-02-13       Impact factor: 4.059

10.  Two novel CMY-2-type β-lactamases encountered in clinical Escherichia coli isolates.

Authors:  Vera Manageiro; Eugénia Ferreira; Margarida Pinto; Fernando Fonseca; Mónica Ferreira; Richard Bonnet; Manuela Caniça
Journal:  Ann Clin Microbiol Antimicrob       Date:  2015-03-18       Impact factor: 3.944

View more

北京卡尤迪生物科技股份有限公司 © 2022-2023.