The penicillin-binding site in the exocellular DD-carboxypeptidase-transpeptidase of Actinomadura R39.
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Duez C, Joris B, Frere JM, Ghuysen JM, Van Beeumen J
The penicillin-binding site in the exocellular DD-carboxypeptidase-transpeptidase of Actinomadura R39.
Biochem J. 1981 Jan 1;193(1):83-6.
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- 7305936 [ View in PubMed]
- 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, Frere, Ghuysen, Duez & Iwatsubo (1976) Biochem. J. 155, 623-629].