Reference : Des-, syn- and anti-oxyimino-Δ3-cephalosporins. Intrinsic reactivity and reaction wit...
Scientific journals : Article
Life sciences : Microbiology
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/83015
Des-, syn- and anti-oxyimino-Δ3-cephalosporins. Intrinsic reactivity and reaction with RTEM-2 serine β-lactamase and D-alanyl-D-alanine-cleaving serine and zinc-containing peptidases
English
Laurent, Guy [Facultés Universitaires Notre-Dame de la Paix - Namur - FUNDP > Laboratoire de Chimie Moleculaire Structurale > > > >]
Durant, François [Facultés Universitaires Notre-Dame de la Paix - Namur - FUNDP > Laboratoire de Chimie Moleculaire Structurale > > >]
Frère, Jean-Marie mailto [Université de Liège - ULiège > Faculté de Médecine, Institut de Chimie > Service de Microbiologie > >]
Klein, Daniel [Université de Liège - ULiège > Faculté de Médecine, Institut de Chimie > Service de Microbiologie > >]
Ghuysen, Jean-Marie [Université de Liège - ULiège > Faculté de Médecine, Institut de Chimie > Service de Microbiologie > > >]
15-Mar-1984
Biochemical Journal
Portland Press
218
3
933-937
Yes (verified by ORBi)
International
0264-6021
1470-8728
London
United Kingdom
[en] carboxypeptidases/antagonists & inhibitors ; cephalosporins ; chemical phenomena ; chemistry ; hydrolysis ; kinetics ; penicillinase ; serine-type d-ala-d-ala carboxypeptidase ; structure-activity relationship ; substrate specificity
[en] The presence and configuration (syn or anti) of an oxyimino group in the 7 (beta)-acyl side chain of 3-cephems do not modify the intrinsic reactivity of the beta-lactam ring, but have highly enzyme-specific effects. When compared with the corresponding desoxyimino beta-lactam compound: (i) with the plasmid-mediated Escherichia coli RTEM-2 serine beta-lactamase, the substrate activity of the anti isomer is increased and that of the syn isomer is decreased; (ii) with the Streptomyces R61 serine D-alanyl-D-alanine cleaving peptidase (a highly penicillin-sensitive enzyme), the rate of enzyme acylation is not or only little affected when the oxyimino group is in the syn configuration, but is decreased when the oxyimino group is in the anti configuration; (iii) with the Actinomadura R39 serine D-alanyl-D-alanine-cleaving peptidase (an exceedingly highly penicillin-sensitive enzyme), the rate of enzyme acylation is unaffected whatever the configuration of the substituent. The oxidation of the sulphur atom of the dihydrothiazine ring on the beta-face of the molecule makes it both a poorer inactivator of the DD-peptidases and a poorer substrate of the beta-lactamase. The Streptomyces albus G Zn2+-containing D-alanyl-D-alanine-cleaving peptidase (a highly penicillin-resistant enzyme) remains highly resistant to all compounds tested.
Fonds de la Recherche Scientifique Médicale - FRSM
Researchers ; Professionals
http://hdl.handle.net/2268/83015
also: http://hdl.handle.net/2268/83040

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