Literature DB >> 18559652

Kinetic characterization of VIM-7, a divergent member of the VIM metallo-beta-lactamase family.

Ørjan Samuelsen1, Mariana Castanheira, Timothy R Walsh, James Spencer.   

Abstract

Purified recombinant VIM-7 possesses efficient penicillinase and carbapenemase activities comparable to those of VIM-2. Cephalosporinase activity was variable and generally lower than those of VIM-1 and VIM-2. A homology model suggests that the VIM-7 Tyr-218 Phe substitution may be responsible for the reduced catalytic efficiency against certain cephalosporins, including ceftazidime and cefepime.

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Year:  2008        PMID： 18559652      PMCID： PMC2493091          DOI： 10.1128/AAC.00166-08

Source DB:  PubMed          Journal:  Antimicrob Agents Chemother        ISSN： 0066-4804            Impact factor:   5.191


  15 in total

1.  Standard numbering scheme for class B beta-lactamases.

Authors:  M Galleni; J Lamotte-Brasseur; G M Rossolini; J Spencer; O Dideberg; J M Frère
Journal:  Antimicrob Agents Chemother       Date:  2001-03       Impact factor: 5.191

2.  On functional and structural heterogeneity of VIM-type metallo-beta-lactamases.

Authors:  Jean-Denis Docquier; Josette Lamotte-Brasseur; Moreno Galleni; Gianfranco Amicosante; Jean-Marie Frère; Gian Maria Rossolini
Journal:  J Antimicrob Chemother       Date:  2003-02       Impact factor: 5.790

3.  Evolution of an integron carrying blaVIM-2 in Eastern Europe: report from the SENTRY Antimicrobial Surveillance Program.

Authors:  Timothy R Walsh; Mark A Toleman; Waleria Hryniewicz; Peter M Bennett; Ronald N Jones
Journal:  J Antimicrob Chemother       Date:  2003-06-12       Impact factor: 5.790

4.  ESyPred3D: Prediction of proteins 3D structures.

Authors:  Christophe Lambert; Nadia Léonard; Xavier De Bolle; Eric Depiereux
Journal:  Bioinformatics       Date:  2002-09       Impact factor: 6.937

5.  Interaction between class B beta-lactamases and suicide substrates of active-site serine beta-lactamases.

Authors:  C Prosperi-Meys; G Llabres; D de Seny; R P Soto; M H Valladares; N Laraki; J M Frere; M Galleni
Journal:  FEBS Lett       Date:  1999-01-25       Impact factor: 4.124

6.  Purification and biochemical characterization of the VIM-1 metallo-beta-lactamase.

Authors:  N Franceschini; B Caravelli; J D Docquier; M Galleni; J M Frère; G Amicosante; G M Rossolini
Journal:  Antimicrob Agents Chemother       Date:  2000-11       Impact factor: 5.191

7.  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

8.  Biochemical characterization of the acquired metallo-beta-lactamase SPM-1 from Pseudomonas aeruginosa.

Authors:  Tanya A Murphy; Alan M Simm; Mark A Toleman; Ronald N Jones; Timothy R Walsh
Journal:  Antimicrob Agents Chemother       Date:  2003-02       Impact factor: 5.191

9.  Crystal structure of Pseudomonas aeruginosa SPM-1 provides insights into variable zinc affinity of metallo-beta-lactamases.

Authors:  Tanya A Murphy; Lucy E Catto; Stephen E Halford; Andrea T Hadfield; Wladek Minor; Timothy R Walsh; James Spencer
Journal:  J Mol Biol       Date:  2006-01-23       Impact factor: 5.469

10.  blaVIM-7, an evolutionarily distinct metallo-beta-lactamase gene in a Pseudomonas aeruginosa isolate from the United States.

Authors:  Mark A Toleman; Kenneth Rolston; Ronald N Jones; Timothy R Walsh
Journal:  Antimicrob Agents Chemother       Date:  2004-01       Impact factor: 5.191
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  15 in total

1.  Crystal structure of the mobile metallo-β-lactamase AIM-1 from Pseudomonas aeruginosa: insights into antibiotic binding and the role of Gln157.

Authors:  Hanna-Kirsti S Leiros; Pardha S Borra; Bjørn Olav Brandsdal; Kine Susann Waade Edvardsen; James Spencer; Timothy R Walsh; Orjan Samuelsen
Journal:  Antimicrob Agents Chemother       Date:  2012-06-04       Impact factor: 5.191

2.  Genetic and biochemical characterization of a novel metallo-β-lactamase, TMB-1, from an Achromobacter xylosoxidans strain isolated in Tripoli, Libya.

Authors:  Allaaeddin El Salabi; Pardha Saradhi Borra; Mark A Toleman; Ørjan Samuelsen; Timothy R Walsh
Journal:  Antimicrob Agents Chemother       Date:  2012-01-30       Impact factor: 5.191

3.  Systematic analysis of metallo-β-lactamases using an automated database.

Authors:  Michael Widmann; Jürgen Pleiss; Peter Oelschlaeger
Journal:  Antimicrob Agents Chemother       Date:  2012-04-30       Impact factor: 5.191

4.  Detection and characterization of VIM-31, a new variant of VIM-2 with Tyr224His and His252Arg mutations, in a clinical isolate of Enterobacter cloacae.

Authors:  Pierre Bogaerts; Carine Bebrone; Te-Din Huang; Warda Bouchahrouf; Yves Degheldre; Ariane Deplano; Kurt Hoffmann; Youri Glupczynski
Journal:  Antimicrob Agents Chemother       Date:  2012-03-05       Impact factor: 5.191

5.  Biochemical characterization of IMP-30, a metallo-β-lactamase with enhanced activity toward ceftazidime.

Authors:  Kevin M Pegg; Eleanor M Liu; Alecander E Lacuran; Peter Oelschlaeger
Journal:  Antimicrob Agents Chemother       Date:  2013-07-08       Impact factor: 5.191

6.  Novel VIM metallo-beta-lactamase variant from clinical isolates of Enterobacteriaceae from Algeria.

Authors:  Frédéric Robin; Nadjet Aggoune-Khinache; Julien Delmas; Malek Naim; Richard Bonnet
Journal:  Antimicrob Agents Chemother       Date:  2009-11-09       Impact factor: 5.191

7.  Biochemical characterization of Sfh-I, a subclass B2 metallo-beta-lactamase from Serratia fonticola UTAD54.

Authors:  Fátima Fonseca; Christopher J Arthur; Elizabeth H C Bromley; Bart Samyn; Pablo Moerman; Maria José Saavedra; António Correia; James Spencer
Journal:  Antimicrob Agents Chemother       Date:  2011-08-29       Impact factor: 5.191

Review 8.  B1-Metallo-β-Lactamases: Where Do We Stand?

Authors:  Maria F Mojica; Robert A Bonomo; Walter Fast
Journal:  Curr Drug Targets       Date:  2016       Impact factor: 3.465

9.  Characterization of a new metallo-beta-lactamase gene, bla(NDM-1), and a novel erythromycin esterase gene carried on a unique genetic structure in Klebsiella pneumoniae sequence type 14 from India.

Authors:  Dongeun Yong; Mark A Toleman; Christian G Giske; Hyun S Cho; Kristina Sundman; Kyungwon Lee; Timothy R Walsh
Journal:  Antimicrob Agents Chemother       Date:  2009-09-21       Impact factor: 5.191

10.  His224 alters the R2 drug binding site and Phe218 influences the catalytic efficiency of the metallo-β-lactamase VIM-7.

Authors:  Hanna-Kirsti S Leiros; Susann Skagseth; Kine Susann Waade Edvardsen; Marit Sjo Lorentzen; Gro Elin Kjæreng Bjerga; Ingar Leiros; Ørjan Samuelsen
Journal:  Antimicrob Agents Chemother       Date:  2014-06-09       Impact factor: 5.191
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