Article (Scientific journals)
Penicillin-sensitive DD-carboxypeptidase from Streptomyces strain R 61
Leyh-Bouille, Mélina; Coyette, Jacques; Ghuysen, Jean-Marie et al.
1971In Biochemistry, 10 (11), p. 2163-2170
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Keywords :
alanine; carboxypeptidases antagonists & inhibitors; cephalothin; chromatography deae-cellulose; chromatographyl; corynebacterium; edetic acid; electrophoresis; hydrogen-ion concentration; ion exchange resins; kinetics; magnesium; penicillins; peptides; streptomyces enzymology; gel
Abstract :
[en] The D-alanyl-D-alanine carboxypeptidase excreted by the penicillin-sensitive Streptomyces strain R 61 is an anionic protein at pH 6.5. It does not require cations for its action. By comparison with the penicillin-resistant DD-carboxypeptidase from Streptomyces albus G, the penicillin-sensitive R 61 enzyme has high Km values with all the peptides which were used but the alignment of catalytic groups is more effective in promoting hydrolysis of the peptides (high Vmax values). Moreover, the substrate structures required by the two enzymes show some differences. In contrast to the albus G DD -carboxypeptidase which is either not, or very little, affected by penicillins, the R 61 enzyme is inhibited by low dose levels of penicillin G and by cephalothin
Disciplines :
Biochemistry, biophysics & molecular biology
Microbiology
Author, co-author :
Leyh-Bouille, Mélina;  Université de Liège - ULiège > Institut de Botanique > Service de Microbiologie
Coyette, Jacques;  Université de Liège - ULiège > Institut de Botanique > Service de Microbiologie
Ghuysen, Jean-Marie ;  Université de Liège - ULiège > Institut de Botanique > Service de Microbiologie
Idczak, Josiane
Perkins, Harold R.;  National Institute for Medical Research - London
Nieto, Manuel;  National Institute for Medical Research - London
Language :
English
Title :
Penicillin-sensitive DD-carboxypeptidase from Streptomyces strain R 61
Publication date :
25 May 1971
Journal title :
Biochemistry
ISSN :
0006-2960
eISSN :
1520-4995
Publisher :
American Chemical Society, Washington, United States - District of Columbia
Volume :
10
Issue :
11
Pages :
2163-2170
Peer reviewed :
Peer Reviewed verified by ORBi
Funders :
FRFC - Fonds de la Recherche Fondamentale Collective [BE]
Available on ORBi :
since 17 February 2011

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