Reference : Streptomyces DD-carboxypeptidases as transpeptidases. The specificity for amino compound...
Scientific journals : Article
Life sciences : Microbiology
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/83535
Streptomyces DD-carboxypeptidases as transpeptidases. The specificity for amino compounds acting as carboxyl acceptors
English
Perkins, Harnold R. [National Institute for Medical Research > > > > >]
Nieto, Manuel [National Institute for Medical Research > > > > >]
Frère, Jean-Marie mailto [Université de Liège - ULg > Faculté de Médecine, Institut de Botanique > Service de Microbiologie > > >]
Leyh-Bouille, Mélina [Université de Liège - ULg > Faculté de Médecine, Institut de Botanique > Service de Microbiologie > > >]
Ghuysen, Jean-Marie [Université de Liège - ULg > Faculté de Médecine, Institut de Botanique > Service de Microbiologie > > >]
1-Apr-1973
Biochemical Journal
Portland Press
131
4
707-718
Yes (verified by ORBi)
International
0264-6021
1470-8728
London
United Kingdom
[en] carbon isotopes ; carboxypeptidases metabolism ; chromatography paper ; cycloserine ; dipeptides chemical synthesis ; electrophoresis paper ; kinetics ; oligopeptides chemical synthesis metabolism ; peptides/metabolism ; pimelic acids ; streptomyces/enzymology ; time factors ; tritium
[en] The ability of the water-soluble dd-carboxypeptidases of Streptomyces strains albus G, R61, K11 and R39 to perform transpeptidation was studied. The donor was diacetyl-l-lysyl-d-alanyl-d-alanine, and a whole range of amino acids, peptides and structurally related amino compounds were tested for acceptor function. No compound tested was an acceptor for the enzyme from strain albus G whereas the enzymes from strains R61 and K11 could utilize with varying efficiency a wide range of substances including peptides with N-terminal glycine or d-alanine, omega-amino acids, aminohexuronic acids, 6-aminopenicillanic acid and d-cycloserine. Certain peptides, when present in higher concentration, inhibited the transpeptidation observed at lower concentration. The enzyme from strain R39 would not use any dipeptide as an acceptor, but a few compounds that were not glycine or alpha-amino acids of the d-configuration did function thus. These were d-cycloserine and the lactams of meso- or racemic-diaminoadipic acid.
Fonds de la Recherche Fondamentale Collective
Researchers ; Professionals
http://hdl.handle.net/2268/83535

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