Literature DB >> 23163348

Metallo-β-lactamase structure and function.

Timothy Palzkill1.   

Abstract

β-Lactam antibiotics are the most commonly used antibacterial agents and growing resistance to these drugs is a concern. Metallo-β-lactamases are a diverse set of enzymes that catalyze the hydrolysis of a broad range of β-lactam drugs including carbapenems. This diversity is reflected in the observation that the enzyme mechanisms differ based on whether one or two zincs are bound in the active site that, in turn, is dependent on the subclass of β-lactamase. The dissemination of the genes encoding these enzymes among Gram-negative bacteria has made them an important cause of resistance. In addition, there are currently no clinically available inhibitors to block metallo-β-lactamase action. This review summarizes the numerous studies that have yielded insights into the structure, function, and mechanism of action of these enzymes.
© 2012 New York Academy of Sciences.

Entities:  

Mesh:

Substances:

Year:  2012        PMID: 23163348      PMCID: PMC3970115          DOI: 10.1111/j.1749-6632.2012.06796.x

Source DB:  PubMed          Journal:  Ann N Y Acad Sci        ISSN: 0077-8923            Impact factor:   5.691


  105 in total

Review 1.  Expansion of the zinc metallo-hydrolase family of the beta-lactamase fold.

Authors:  H Daiyasu; K Osaka; Y Ishino; H Toh
Journal:  FEBS Lett       Date:  2001-08-10       Impact factor: 4.124

2.  Analysis of the importance of the metallo-beta-lactamase active site loop in substrate binding and catalysis.

Authors:  Catherine Moali; Christine Anne; Josette Lamotte-Brasseur; Sylvie Groslambert; Bart Devreese; Jozef Van Beeumen; Moreno Galleni; Jean Marie Frère
Journal:  Chem Biol       Date:  2003-04

3.  Probing the dynamics of a mobile loop above the active site of L1, a metallo-beta-lactamase from Stenotrophomonas maltophilia, via site-directed mutagenesis and stopped-flow fluorescence spectroscopy.

Authors:  James D Garrity; James M Pauff; Michael W Crowder
Journal:  J Biol Chem       Date:  2004-07-22       Impact factor: 5.157

Review 4.  Fourteen years in resistance.

Authors:  David M Livermore
Journal:  Int J Antimicrob Agents       Date:  2012-03-03       Impact factor: 5.283

Review 5.  Cutting and stitching: the cross-linking of peptidoglycan in the assembly of the bacterial cell wall.

Authors:  John D Buynak
Journal:  ACS Chem Biol       Date:  2007-09-21       Impact factor: 5.100

6.  Loss of enzyme activity during turnover of the Bacillus cereus beta-lactamase catalysed hydrolysis of beta-lactams due to loss of zinc ion.

Authors:  Adriana Badarau; Michael I Page
Journal:  J Biol Inorg Chem       Date:  2008-05-01       Impact factor: 3.358

Review 7.  Molecular mechanisms of β-lactam resistance in Streptococcus pneumoniae.

Authors:  Regine Hakenbeck; Reinhold Brückner; Dalia Denapaite; Patrick Maurer
Journal:  Future Microbiol       Date:  2012-03       Impact factor: 3.165

8.  Metal binding Asp-120 in metallo-beta-lactamase L1 from Stenotrophomonas maltophilia plays a crucial role in catalysis.

Authors:  James D Garrity; Anne L Carenbauer; Lissa R Herron; Michael W Crowder
Journal:  J Biol Chem       Date:  2003-10-22       Impact factor: 5.157

9.  The three-dimensional structure of VIM-2, a Zn-beta-lactamase from Pseudomonas aeruginosa in its reduced and oxidised form.

Authors:  I Garcia-Saez; J-D Docquier; G M Rossolini; O Dideberg
Journal:  J Mol Biol       Date:  2007-11-13       Impact factor: 5.469

10.  Aztreonam: the first monobactam.

Authors:  R B Sykes; D P Bonner
Journal:  Am J Med       Date:  1985-02-08       Impact factor: 4.965

View more
  165 in total

1.  Characterization of a novel metallo-β-lactamases fold hydrolase from Pelagibacterium halotolerans, a marine halotolerant bacterium isolated from East China Sea.

Authors:  Beiwen Zheng; Xiawei Jiang; Zemin Xu; Yunhui Fang; Lanjuan Li
Journal:  Extremophiles       Date:  2015-11-03       Impact factor: 2.395

Review 2.  Resistance to antibiotics targeted to the bacterial cell wall.

Authors:  I Nikolaidis; S Favini-Stabile; A Dessen
Journal:  Protein Sci       Date:  2014-01-17       Impact factor: 6.725

3.  Klebsiella pneumoniae Expressing VIM-1 Metallo-β-Lactamase Is Resensitized to Cefotaxime via Thiol-Mediated Zinc Chelation.

Authors:  Harpa Karadottir; Maarten Coorens; Zhihai Liu; Yang Wang; Birgitta Agerberth; Christian G Giske; Peter Bergman
Journal:  Infect Immun       Date:  2019-12-17       Impact factor: 3.441

Review 4.  New promising β-lactamase inhibitors for clinical use.

Authors:  I Olsen
Journal:  Eur J Clin Microbiol Infect Dis       Date:  2015-04-12       Impact factor: 3.267

5.  Molecular Characterization and Computational Modelling of New Delhi Metallo-β-Lactamase-5 from an Escherichia coli Isolate (KOEC3) of Bovine Origin.

Authors:  D Purkait; A Ahuja; U Bhattacharjee; A Singha; K Rhetso; T K Dey; S Das; R K Sanjukta; K Puro; I Shakuntala; A Sen; A Banerjee; I Sharma; R S Bhatta; M Mawlong; C Guha; N R Pradhan; S Ghatak
Journal:  Indian J Microbiol       Date:  2016-02-11       Impact factor: 2.461

6.  A Cephalosporin Prochelator Inhibits New Delhi Metallo-β-lactamase 1 without Removing Zinc.

Authors:  Abigail C Jackson; Jacqueline M Zaengle-Barone; Elena A Puccio; Katherine J Franz
Journal:  ACS Infect Dis       Date:  2020-04-29       Impact factor: 5.084

7.  Copper Influences the Antibacterial Outcomes of a β-Lactamase-Activated Prochelator against Drug-Resistant Bacteria.

Authors:  Jacqueline M Zaengle-Barone; Abigail C Jackson; David M Besse; Bradford Becken; Mehreen Arshad; Patrick C Seed; Katherine J Franz
Journal:  ACS Infect Dis       Date:  2018-03-26       Impact factor: 5.084

8.  Genomic Landscape of Ornithobacterium rhinotracheale in Commercial Turkey Production in the United States.

Authors:  Emily A Smith; Elizabeth A Miller; Bonnie P Weber; Jeannette Munoz Aguayo; Cristian Flores Figueroa; Jared Huisinga; Jill Nezworski; Michelle Kromm; Ben Wileman; Timothy J Johnson
Journal:  Appl Environ Microbiol       Date:  2020-05-19       Impact factor: 4.792

9.  In Vitro Activity of the Ultra-Broad-Spectrum Beta-Lactamase Inhibitor QPX7728 in Combination with Meropenem against Clinical Isolates of Carbapenem-Resistant Acinetobacter baumannii.

Authors:  Kirk Nelson; Debora Rubio-Aparicio; Ruslan Tsivkovski; Dongxu Sun; Maxim Totrov; Michael Dudley; Olga Lomovskaya
Journal:  Antimicrob Agents Chemother       Date:  2020-10-20       Impact factor: 5.191

Review 10.  NDM Metallo-β-Lactamases and Their Bacterial Producers in Health Care Settings.

Authors:  Wenjing Wu; Yu Feng; Guangmin Tang; Fu Qiao; Alan McNally; Zhiyong Zong
Journal:  Clin Microbiol Rev       Date:  2019-01-30       Impact factor: 26.132

View more

北京卡尤迪生物科技股份有限公司 © 2022-2023.