Reference : On the Streptomyces albus G DD carboxypeptidase mechanism of action of penicillin, va...
Scientific journals : Article
Life sciences : Microbiology
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/85149
On the Streptomyces albus G DD carboxypeptidase mechanism of action of penicillin, vancomycin, and ristocetin
English
Leyh-Bouille, Mélina [Université de Liège - ULg > > Service de Bactériologie > >]
Ghuysen, Jean-Marie [Université de Liège - ULg > > 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 > > > >]
21-Jul-1970
Biochemistry
American Chemical Society
9
15
2971-2975
Yes (verified by ORBi)
International
0006-2960
1520-4995
Washington
DC
[en] carboxypeptidases ; chemical phenomena ; chemistry ; penicillins ; ristocetin ; streptomyces ; vancomycin ; antagonists & inhibitors ; enzymology
[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.
Fonds de la Recherche Fondamentale Collective
Researchers ; Professionals
http://hdl.handle.net/2268/85149
also: http://hdl.handle.net/2268/91733
10.1021/bi00817a006

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