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Article (Scientific journals)
On the Streptomyces albus G DD carboxypeptidase mechanism of action of penicillin, vancomycin, and ristocetin
Leyh-Bouille, Mélina; Ghuysen, Jean-Marie  ; Nieto, Manuel et al.
1970 • In Biochemistry, 9 (15), p. 2971-2975
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Keywords :
carboxypeptidases; chemical phenomena; chemistry; penicillins; ristocetin; streptomyces; vancomycin; antagonists & inhibitors; enzymology
Abstract :
[en] The activity of the D-alanyl-D carboxypeptidase from the penicillin-resistant Streptomyces albus G is not or very little affected by penicillins and related antibiotics. The molecular basis for the mechanism of action of penicillin is discussed. The Streptomyces albus G D-alanyl-D carboxypeptidase appears as a model for the study of a mechanism of penicillin resistance that does not involve the enzymatic degradation of the antibiotic. Vancomycin and ristocetin are shown to inhibit the hydrolysis of sensitive peptides by the Streptomyces albus G D-alanyl-D carboxypeptidase and the mechanism of inhibition is discussed.
Disciplines :
Biochemistry, biophysics & molecular biology
Microbiology
Author, co-author :
Leyh-Bouille, Mélina;  Université de Liège - ULiège > Service de Bactériologie
Ghuysen, Jean-Marie ;  Université de Liège - ULiège > Service de Bactériologie
Nieto, Manuel;  National Institute for Medical research - London
Perkins, Harold R.;  National Institute for Medical research - London
Schleifer, Karl H;  Ludwig-Maximilians-Universität München - LMU > Botanisches Institut
Kandler, Otto;  Ludwig-Maximilians-Universität München - LMU > Botanisches Institut
Language :
English
Title :
On the Streptomyces albus G DD carboxypeptidase mechanism of action of penicillin, vancomycin, and ristocetin
Publication date :
21 July 1970
Journal title :
Biochemistry
ISSN :
0006-2960
eISSN :
1520-4995
Publisher :
American Chemical Society, Washington, United States - District of Columbia
Volume :
9
Issue :
15
Pages :
2971-2975
Peer reviewed :
Peer Reviewed verified by ORBi
Funders :
FRFC - Fonds de la Recherche Fondamentale Collective

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