Reference : Streptomyces K15 DD-peptidase-catalysed reactions with ester and amide carbonyl donors
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
Life sciences : Microbiology
http://hdl.handle.net/2268/83010
Streptomyces K15 DD-peptidase-catalysed reactions with ester and amide carbonyl donors
English
Nguyen-Distèche, Martine mailto [Université de Liège - ULg > Faculté de Médecine, Institut de Chimie > Service de Microbiologie > >]
Leyh-Bouille, Mélina [Université de Liège - ULg > Institut de Botanique > Service de Microbiologie > >]
Pirlot, Suzanne [Université de Liège - ULg > Faculté de Médecine, Institut de Chimie > Service de Microbiologie > >]
Frère, Jean-Marie mailto [Université de Liège - ULg > Faculté de Médecine, Institut de Chimie > Service de Microbiologie > >]
Ghuysen, Jean-Marie [Université de Liège - ULg > Institut de Botanique > Service de Microbiologie > >]
1-Apr-1986
Biochemical Journal
Portland Press
235
1
167-176
Yes (verified by ORBi)
International
0264-6021
1470-8728
London
United Kingdom
[en] acylation ; carboxypeptidases/*metabolism ; d-amino-acid oxidase/pharmacology ; dipeptides/*metabolism ; hydrolysis ; kinetics ; lactates/*metabolism ; muramoylpentapeptide carboxypeptidase/*metabolism ; oligopeptides/*metabolism ; penicillin g/metabolism ; streptomyces/*enzymology ; substrate specificity
[en] In water, the purified 26 000-Mr membrane-bound DD-peptidase of Streptomyces K15 hydrolyses the ester carbonyl donor Ac2-L-Lys-D-Ala-D-lactate (release of D-lactate) and the amide carbonyl donor Ac2-L-Lys-D-Ala-D-Ala (release of D-alanine) with accumulation of acyl- (Ac2-L-Lys-D-alanyl-)enzyme. Whereas hydrolysis of the ester substrate proceeds to completion, hydrolysis of the amide substrate is negligible because of the capacity of the K15 DD-peptidase for utilizing the released D-alanine in a transfer reaction (Ac2-L-Lys-D-Ala-D-Ala + D-Ala----Ac2-L-Lys-D-Ala-D-Ala + D-Ala) that maintains the concentration of the amide substrate at a constant level. In the presence of an amino acceptor X-NH2 (Gly-Gly or Gly-L-Ala) related to the Streptomyces peptidoglycan, both amide and ester carbonyl donors are processed without detectable accumulation of acyl-enzyme. Under proper conditions, the acceptor activity of water and, in the case of the amide substrate, the acceptor activity of the released D-alanine can be totally overcome so that the two substrates are quantitatively converted into transpeptidated product Ac2-L-Lys-D-Ala-NH-X (and hydrolysis is prevented). Experimental evidence suggests that the amino acceptor modifies both the binding of the carbonyl donor to the enzyme and the ensuing rate of enzyme acylation.
Fonds de la Recherche Scientifique Médicale - FRSM ; Fonds de la Recherche Scientifique (Communauté française de Belgique) - F.R.S.-FNRS
Researchers ; Professionals
http://hdl.handle.net/2268/83010

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