| Literature DB >> 7305936 |
C Duez, B Joris, J M Frère, J M Ghuysen, J Van Beeumen.
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].Entities:
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Year: 1981 PMID: 7305936 PMCID: PMC1162578 DOI: 10.1042/bj1930083
Source DB: PubMed Journal: Biochem J ISSN: 0264-6021 Impact factor: 3.857