Article (Scientific journals)
The penicillin-binding site in the exocellular DD-carboxypeptidase-transpeptidase of Actinomadura R39
Duez, Colette; Joris, Bernard; Frère, Jean-Marie et al.
1981In Biochemical Journal, 193, p. 83-86
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Keywords :
Penicillin-binding site; DD-peptidase; Actinomadura R39
Abstract :
[en] Heat denaturation and Pronase degradation of the complex previously formed between benzylpenicillin and the exocellular DD-carboxypeptidase-transpeptidase of Actinomadura R39 yields a heptapeptide H-Leu-Pro-Ala-Ser-Asn-Gly-Val-OH, where the benzylpenicilloyl group is ester-linked to the serine residue. This linkage is very labile and its hydrolysis causes the release of benzylpenicilloate. In contrast, the native benzylpenicilloyl-enzyme complex is very stable (half-life 70h at 370C) and its breakdown proceeds via fragmentation of the bound benzylpenicilloyl group [Fuad, Frere, Ghuysen, Duez & Iwatsubo (1976) Biochem. J. 155, 623-6291.
Disciplines :
Microbiology
Biochemistry, biophysics & molecular biology
Author, co-author :
Duez, Colette ;  Université de Liège - ULiège > Faculté de Médecine, Institut de Botanique > Service de Microbiologie
Joris, Bernard ;  Université de Liège - ULiège > Faculté de Médecine, Institut de Botanique > Service de Microbiologie
Frère, Jean-Marie ;  Université de Liège - ULiège > Faculté de Médecine, Institut de Botanique > Service de Microbiologie
Ghuysen, Jean-Marie ;  Université de Liège - ULiège > Faculté de Médecine, Institut de Botanique > Service de Microbiologie
Van Beeumen, Jos;  Rijksuniversiteit Gent Belgium - RUG > Laboratorium voor Microbiologie
Language :
English
Title :
The penicillin-binding site in the exocellular DD-carboxypeptidase-transpeptidase of Actinomadura R39
Publication date :
1981
Journal title :
Biochemical Journal
ISSN :
0264-6021
eISSN :
1470-8728
Publisher :
Portland Press, London, United Kingdom
Volume :
193
Pages :
83-86
Peer reviewed :
Peer Reviewed verified by ORBi
Funders :
NIH - National Institutes of Health [US-MD]
Available on ORBi :
since 22 July 2010

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