Literature DB >> 9087509

Sensitivity of Aeromonas hydrophila carbapenemase to delta3-cephems: comparative study with other metallo-beta-lactamases.

A Felici1, M Perilli, N Franceschini, G M Rossolini, M Galleni, J M Frere, A Oratore, G Amicosante.   

Abstract

Ceftriaxone and ceftriaxone S-oxide behaved as inactivators against the metallo-beta-lactamase of Aeromonas hydrophila AE036 and as substrates for the zinc beta-lactamase produced by Bacillus cereus (569/H/9) and Stenotrophomonas maltophilia ULA 511. Moreover, RO 09-1428, a catechol-cephalosporin, was not recognized by the A. hydrophila enzyme. Panipenem, cephalosporin C, cephalosporin C-gamma-lactone, and loracarbef were substrates for the three studied beta-lactamases.

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Year:  1997        PMID： 9087509      PMCID： PMC163814     

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


  10 in total

1.  Automated analysis of enzyme inactivation phenomena. Application to beta-lactamases and DD-peptidases.

Authors:  F De Meester; B Joris; G Reckinger; C Bellefroid-Bourguignon; J M Frère; S G Waley
Journal:  Biochem Pharmacol       Date:  1987-07-15       Impact factor: 5.858

2.  The importance of the negative charge of beta-lactam compounds for the inactivation of the active-site serine DD-peptidase of Streptomyces R61.

Authors:  L Varetto; J M Frère; J M Ghuysen
Journal:  FEBS Lett       Date:  1987-12-10       Impact factor: 4.124

3.  The structure of beta-lactamases.

Authors:  R P Ambler
Journal:  Philos Trans R Soc Lond B Biol Sci       Date:  1980-05-16       Impact factor: 6.237

4.  The renal membrane dipeptidase (dehydropeptidase I) inhibitor, cilastatin, inhibits the bacterial metallo-beta-lactamase enzyme CphA.

Authors:  S Keynan; N M Hooper; A Felici; G Amicosante; A J Turner
Journal:  Antimicrob Agents Chemother       Date:  1995-07       Impact factor: 5.191

5.  Kinetic interactions of tazobactam with beta-lactamases from all major structural classes.

Authors:  K Bush; C Macalintal; B A Rasmussen; V J Lee; Y Yang
Journal:  Antimicrob Agents Chemother       Date:  1993-04       Impact factor: 5.191

Review 6.  Metallo-beta-lactamases--a new therapeutic challenge.

Authors:  D J Payne
Journal:  J Med Microbiol       Date:  1993-08       Impact factor: 2.472

7.  Crystal structure of the wide-spectrum binuclear zinc beta-lactamase from Bacteroides fragilis.

Authors:  N O Concha; B A Rasmussen; K Bush; O Herzberg
Journal:  Structure       Date:  1996-07-15       Impact factor: 5.006

8.  Kinetic analysis of extension of substrate specificity with Xanthomonas maltophilia, Aeromonas hydrophila, and Bacillus cereus metallo-beta-lactamases.

Authors:  A Felici; G Amicosante
Journal:  Antimicrob Agents Chemother       Date:  1995-01       Impact factor: 5.191

9.  An overview of the kinetic parameters of class B beta-lactamases.

Authors:  A Felici; G Amicosante; A Oratore; R Strom; P Ledent; B Joris; L Fanuel; J M Frère
Journal:  Biochem J       Date:  1993-04-01       Impact factor: 3.857

10.  The 3-D structure of a zinc metallo-beta-lactamase from Bacillus cereus reveals a new type of protein fold.

Authors:  A Carfi; S Pares; E Duée; M Galleni; C Duez; J M Frère; O Dideberg
Journal:  EMBO J       Date:  1995-10-16       Impact factor: 11.598
  10 in total
  1 in total

1.  Overexpression, purification, and characterization of the cloned metallo-beta-lactamase L1 from Stenotrophomonas maltophilia.

Authors:  M W Crowder; T R Walsh; L Banovic; M Pettit; J Spencer
Journal:  Antimicrob Agents Chemother       Date:  1998-04       Impact factor: 5.191
  1 in total

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