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See detailThe penicillin-binding site in the exocellular DD-carboxypeptidase-transpeptidase of Actinomadura R39
Duez, Colette ULg; Joris, Bernard ULg; Frère, Jean-Marie ULg et al

in Biochemical Journal (1981), 193

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 ... [more ▼]

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. [less ▲]

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See detailThe exocellular DD-carboxypeptidase of Streptomyces albus G: A metallo (Zn2+) enzyme
Dideberg, O.; Joris, Bernard ULg; Frère, Jean-Marie ULg et al

in FEBS Letters (1980), 117(1-2), 215-218

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See detailOn the Active Centers of Serine and Zn II DD-carboxyppetidases
Charlier, Paulette ULg; Coyette, Jacques ULg; Dideberg, Otto et al

in Gregory, G.I. (Ed.) Recent advances in the Chemistry of beta-lactam antibiotics (1980)

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See detailParvalbumins from the lungfish (Protopterus dolloi).
Gerday, Charles ULg; Joris, Bernard ULg; Gerardin, Nicole ULg et al

in Biochimie (1979), 61

Five parvalbumins have been isolated from the white muscles of the lungfish. They can be divided into two sub families showing typical amino acid compositions, C-terminal amino acid residues, peptide maps ... [more ▼]

Five parvalbumins have been isolated from the white muscles of the lungfish. They can be divided into two sub families showing typical amino acid compositions, C-terminal amino acid residues, peptide maps and immuno-reactivity. The red muscles including the cardiac muscle also contain parvalbumins in amounts roughly inversely related to the concentration of myoglobin in the muscle. Parvalbumins have also been detected in the brain and kidney. [less ▲]

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