Literature DB >> 9989585

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

C Prosperi-Meys1, G Llabres, D de Seny, R P Soto, M H Valladares, N Laraki, J M Frere, M Galleni.   

Abstract

The most widely used inactivators of active-site serine beta-lactamases behave as substrates of four class B metallo-beta-lactamases, but the efficiency of the catalytic process can vary by several orders of magnitude. A comparison of the kinetic parameters for the alpha and beta isomers of 6-iodopenicillanic acid shows that there is no general preference for the alpha isomer and that the efficient hydrolysis of imipenem by these enzymes must rest on other factors.

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Year:  1999        PMID： 9989585     DOI： 10.1016/s0014-5793(98)01689-5

Source DB:  PubMed          Journal:  FEBS Lett        ISSN： 0014-5793            Impact factor:   4.124


  16 in total

1.  Inhibition of beta-lactamase II of Bacillus cereus by penamaldic derivatives of penicillins.

Authors:  Pilar Gutiérrez Navarro; Bartolomé Quintero Osso; Raquel García Ortiz; Pedro J Martínez De Las Parras; María I Martínez Puentedura; M Carmen Cabeza González
Journal:  Antimicrob Agents Chemother       Date:  2004-03       Impact factor: 5.191

2.  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

3.  Identification and characterization of a new metallo-beta-lactamase, IND-5, from a clinical isolate of Chryseobacterium indologenes.

Authors:  Mariagrazia Perilli; Bibiana Caporale; Giuseppe Celenza; Cristina Pellegrini; Jean Denis Docquier; Marilina Mezzatesta; Gian Maria Rossolini; Stefania Stefani; Gianfranco Amicosante
Journal:  Antimicrob Agents Chemother       Date:  2007-04-30       Impact factor: 5.191

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

Authors:  Ørjan Samuelsen; Mariana Castanheira; Timothy R Walsh; James Spencer
Journal:  Antimicrob Agents Chemother       Date:  2008-06-16       Impact factor: 5.191

5.  Carbapenem derivatives as potential inhibitors of various beta-lactamases, including class B metallo-beta-lactamases.

Authors:  R Nagano; Y Adachi; H Imamura; K Yamada; T Hashizume; H Morishima
Journal:  Antimicrob Agents Chemother       Date:  1999-10       Impact factor: 5.191

6.  New Delhi Metallo-β-Lactamase 1 Catalyzes Avibactam and Aztreonam Hydrolysis.

Authors:  Christopher T Lohans; Jürgen Brem; Christopher J Schofield
Journal:  Antimicrob Agents Chemother       Date:  2017-11-22       Impact factor: 5.191

7.  Beta-lactamase inhibitors derived from single-domain antibody fragments elicited in the camelidae.

Authors:  K E Conrath; M Lauwereys; M Galleni; A Matagne; J M Frère; J Kinne; L Wyns; S Muyldermans
Journal:  Antimicrob Agents Chemother       Date:  2001-10       Impact factor: 5.191

Review 8.  Current challenges in antimicrobial chemotherapy: focus on ß-lactamase inhibition.

Authors:  Carine Bebrone; Patricia Lassaux; Lionel Vercheval; Jean-Sébastien Sohier; Adrien Jehaes; Eric Sauvage; Moreno Galleni
Journal:  Drugs       Date:  2010-04-16       Impact factor: 9.546

9.  Biochemical and structural characterization of the subclass B1 metallo-β-lactamase VIM-4.

Authors:  Patricia Lassaux; Daouda A K Traoré; Elodie Loisel; Adrien Favier; Jean-Denis Docquier; Jean Sébastien Sohier; Clémentine Laurent; Carine Bebrone; Jean-Marie Frère; Jean-Luc Ferrer; Moreno Galleni
Journal:  Antimicrob Agents Chemother       Date:  2010-12-13       Impact factor: 5.191

10.  N-arylsulfonyl hydrazones as inhibitors of IMP-1 metallo-beta-lactamase.

Authors:  Stefan Siemann; Darryl P Evanoff; Laura Marrone; Anthony J Clarke; Thammaiah Viswanatha; Gary I Dmitrienko
Journal:  Antimicrob Agents Chemother       Date:  2002-08       Impact factor: 5.191
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