Reference : Isolation of DD carboxypeptidase from Streptomyces albus G culture filtrates
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/85153
Isolation of DD carboxypeptidase from Streptomyces albus G culture filtrates
English
Ghuysen, Jean-Marie [Université de Liège - ULg > > Service de Bactériologie > >]
Leyh-Bouille, Mélina [Université de Liège - ULg > > Service de Bactériologie > >]
Bonaly, Roger [Faculté de Pharmacie de Nancy > > > >]
Nieto, Manuel [National Instiute for Medical Research > > > >]
Perkins, Harold R. [National Instiute for Medical Research > > > >]
Schleifer, Karl H. [Ludwig-Maximilians-Universität München - LMU > Botanisches Institut > > >]
Kandler, Otto [Ludwig-Maximilians-Universität München - LMU > Botanisches Institut > > > >]
21-Jul-1970
Biochemistry
American Chemical Society
9
15
2955-2961
Yes (verified by ORBi)
International
0006-2960
1520-4995
Washington
DC
[en] alanine ; buffers ; calcium ; carboxypeptidases ; cell wall ; chelating agents ; chemical phenomena ; chemistry ; chromatography ; culture media ; densitometry ; endopeptidases ; enzyme activation ; escherichia coli enzymology ; hydrogen-ion concentration ; kinetics ; magnesium ; peptides ; stereoisomerism ; streptomyces enzymology ; isolation & purification ; ion exchange
[en] Streptomyces albus G secretes a soluble DD carboxypeptidase whose catalytic activities are similar to those of the particulate DD carboxypeptidase from Escherichia coli. Both enzymes hydrolyze the C-terminal D-alanyl-D-alanine linkage of UDP-N-acetylmuramyl-L-alanyl-γ-D-glutamyl-(L)-meso-diaminopimelyl-(L)-D-alanyl-D-aIanine and the enzyme-peptide interactions have identical Michaelis constants. Like the E. coli enzyme, the Streptomyces DD carboxypeptidase exhibits endopeptidase activities. The Streptomyces enzyme is lytic for those walls in which the peptidoglycan interpeptide bonds are mediated through C-terminal D-alanyl-D linkages. There is no strict requirement for a specific structure of the C-terminal D-amino acid residue. The tripeptide Nα , Nє -bisacetyl-L-lysyl-D-alanyl-D-alanine is an excellent substrate for the Streptomyces DD carboxypeptidase.
Fonds de la Recherche Fondamentale Collective
Researchers ; Professionals
http://hdl.handle.net/2268/85153
10.1021/bi00817a004

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