Literature DB >> 1633864

A rapid-kinetic study of the class C beta-lactamase of Enterobacter cloacae 908R.

D Monnaie1, R Virden, J M Frère.   

Abstract

The individual rate constants for acylation and deacylation (k2 and k3, respectively) of the class C beta-lactamase of Enterobacter cloacae 908R by ampicillin and carbenicillin have been determined. For several other beta-lactams, the value of k2 was too high to be determined and the k2/k3 ratio could be larger than 10,000. Branched pathways were also shown to occur with several penicillins and cephalosporins.

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Year:  1992        PMID： 1633864     DOI： 10.1016/0014-5793(92)80979-q

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


  6 in total

1.  Substrate-induced inactivation of the OXA2 beta-lactamase.

Authors:  P Ledent; J M Frère
Journal:  Biochem J       Date:  1993-11-01       Impact factor: 3.857

2.  A dramatic change in the rate-limiting step of beta-lactam hydrolysis results from the substitution of the active-site serine residue by a cysteine in the class-C beta-lactamase of Enterobacter cloacae 908R.

Authors:  A Dubus; D Monnaie; C Jacobs; S Normark; J M Frère
Journal:  Biochem J       Date:  1993-06-01       Impact factor: 3.857

3.  Interactions between active-site-serine beta-lactamases and compounds bearing a methoxy side chain on the alpha-face of the beta-lactam ring: kinetic and molecular modelling studies.

Authors:  A Matagne; J Lamotte-Brasseur; G Dive; J R Knox; J M Frère
Journal:  Biochem J       Date:  1993-08-01       Impact factor: 3.857

4.  The kinetics of non-stoichiometric bursts of beta-lactam hydrolysis catalysed by class C beta-lactamases.

Authors:  M G Page
Journal:  Biochem J       Date:  1993-10-01       Impact factor: 3.857

5.  Catalytic mechanism of active-site serine beta-lactamases: role of the conserved hydroxy group of the Lys-Thr(Ser)-Gly triad.

Authors:  A Dubus; J M Wilkin; X Raquet; S Normark; J M Frère
Journal:  Biochem J       Date:  1994-07-15       Impact factor: 3.857

6.  The role of lysine-67 in a class C beta-lactamase is mainly electrostatic.

Authors:  D Monnaie; A Dubus; J M Frère
Journal:  Biochem J       Date:  1994-08-15       Impact factor: 3.857
  6 in total

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