학술논문
The penicillin-binding site in the exocellular dd-carboxypeptidase-transpeptidase of Actinomadura R39
Document Type
Article
Author
Source
Biochemical Journal; January 1981, Vol. 193 Issue: 1 p83-86, 4p
Subject
Language
ISSN
02646021; 14708728
Abstract
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 70 h at 37 degrees C) and its breakdown proceeds via fragmentation of the bound benzylpenicilloyl group [Fuad, Frère, Ghuysen, Duez & Iwatsubo (1976) Biochem. J. 155, 623-629].