Literature DB >> 11869237

beta-Lactamases: quality and resistance.

Antone A. Medeiros1.   

Abstract

beta-Lactamase-mediated resistance to beta-lactam antibiotics is a feature of great clinical significance. beta-Lactamases are a diverse group of bacterial enzymes that vary in their abilities to hydrolyze beta-lactam antibiotics. beta-Lactamases possess an active site containing either a serine moiety or a zinc atom; serine beta-lactamases are currently of greater clinical prevalence. This review considers the molecular classification of beta-lactamases, the structure of the serine beta-lactamase active site and the mechanisms by which beta-lactamase production may become derepressed. The spread of beta-lactamases in the clinical setting and some important structural mutations that have extended the hydrolysis profiles of serine beta-lactamases are also discussed.

Entities:  

Year:  1997        PMID: 11869237

Source DB:  PubMed          Journal:  Clin Microbiol Infect        ISSN: 1198-743X            Impact factor:   8.067


  7 in total

1.  Caz-hi, and extended-spectrum TEM beta-lactamase (TEM-61), is derived from Caz-lo (TEM-11) by in vivo selection.

Authors:  T De Baere; M Vaneechoutte; G Verschraegen
Journal:  Antimicrob Agents Chemother       Date:  1998-12       Impact factor: 5.191

2.  Characterization of antibiotic resistance determinants in oral biofilms.

Authors:  Seon-Mi Kim; Hyeong C Kim; Seok-Woo S Lee
Journal:  J Microbiol       Date:  2011-09-02       Impact factor: 3.422

3.  Substrate selectivity and a novel role in inhibitor discrimination by residue 237 in the KPC-2 beta-lactamase.

Authors:  Krisztina M Papp-Wallace; Magdalena Taracila; John M Hornick; Andrea M Hujer; Kristine M Hujer; Anne M Distler; Andrea Endimiani; Robert A Bonomo
Journal:  Antimicrob Agents Chemother       Date:  2010-04-26       Impact factor: 5.191

4.  In vivo functional analysis of a class A β-lactamase-related protein essential for clavulanic acid biosynthesis in Streptomyces clavuligerus.

Authors:  Santosh K Srivastava; Kelcey S King; Nader F AbuSara; Chelsea J Malayny; Brandon M Piercey; Jaime A Wilson; Kapil Tahlan
Journal:  PLoS One       Date:  2019-04-23       Impact factor: 3.240

5.  N-Aryl mercaptoacetamides as potential multi-target inhibitors of metallo-β-lactamases (MBLs) and the virulence factor LasB from Pseudomonas aeruginosa.

Authors:  Samir Yahiaoui; Katrin Voos; Jörg Haupenthal; Thomas A Wichelhaus; Denia Frank; Lilia Weizel; Marco Rotter; Steffen Brunst; Jan S Kramer; Ewgenij Proschak; Christian Ducho; Anna K H Hirsch
Journal:  RSC Med Chem       Date:  2021-07-29

Review 6.  The Role of the Ω-Loop in Regulation of the Catalytic Activity of TEM-Type β-Lactamases.

Authors:  Alexey Egorov; Maya Rubtsova; Vitaly Grigorenko; Igor Uporov; Alexander Veselovsky
Journal:  Biomolecules       Date:  2019-12-11

Review 7.  Emerging Strategies to Combat β-Lactamase Producing ESKAPE Pathogens.

Authors:  Corneliu Ovidiu Vrancianu; Irina Gheorghe; Elena-Georgiana Dobre; Ilda Czobor Barbu; Roxana Elena Cristian; Marcela Popa; Sang Hee Lee; Carmen Limban; Ilinca Margareta Vlad; Mariana Carmen Chifiriuc
Journal:  Int J Mol Sci       Date:  2020-11-12       Impact factor: 6.208

  7 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.