Reference : Streptomyces K15 DD-peptidase-catalysed reactions with suicide β-lactam carbonyl donors
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
Life sciences : Microbiology
http://hdl.handle.net/2268/83009
Streptomyces K15 DD-peptidase-catalysed reactions with suicide β-lactam carbonyl donors
English
Leyh-Bouille, Mélina [Université de Liège - ULg > Faculté de Médecine, Institut de Chimie > Service de Microbiologie > >]
Nguyen-Distèche, Martine mailto [Université de Liège - ULg > Faculté de Médecine, Institut de Chimie > Service de Microbiologie > >]
Pirlot, Suzanne [Université de Liège - ULg > Faculté de Médecine, Institut de Chimie > Service de Microbiologie > > >]
Veithen, Angelica [Université de Liège - ULg > Faculté de Médecine, Institut de Chimie > Service de Microbiologie > > >]
Bourguignon, Catherine [Université de Liège - ULg > Faculté de Médecine, Institut de Chimie > Service de Microbiologie > > >]
Ghuysen, Jean-Marie [Université de Liège - ULg > Faculté de Médecine, Institut de Chimie > Service de Microbiologie > > >]
1-Apr-1986
Biochemical Journal
Portland Press
235
1
177-182
Yes (verified by ORBi)
0264-6021
1470-8728
London
United Kingdom
[en] acylation ; anti-bacterial agents/*metabolism ; carboxypeptidases/*metabolism ; cefoxitin/metabolism ; kinetics ; muramoylpentapeptide carboxypeptidase/*metabolism ; oligopeptides/metabolism ; penicillin g/metabolism ; streptomyces/*enzymology ; structure-activity relationship ; substrate specificity
[en] The values of the kinetic parameters that govern the interactions between the Streptomyces K15 DD-peptidase and beta-lactam compounds were determined by measuring the inactivating effect that these compounds exert on the transpeptidase activity of the enzyme and, in the case of [14C]benzylpenicillin and [14C]cefoxitin, by measuring the amounts of acyl-enzyme formed during the reaction. K15 DD-peptidase binds benzylpenicillin or cefoxitin at a molar ratio of 1:1. Benzylpenicilloate is the major product released during breakdown of the acyl-enzyme formed with benzylpenicillin. Benzylpenicillin is not a better acylating agent than the amide Ac2-L-Lys-D-Ala-D-Ala and ester Ac2-L-Lys-D-Ala-D-lactatecarbonyl-donor substrates. beta-Lactam compounds possessing a methoxy group on the alpha-face of the molecule show high inactivating potency.
Fonds de la Recherche Scientifique Médicale - FRSM
Researchers ; Professionals
http://hdl.handle.net/2268/83009

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