Reference : Fate of thiazolidine ring during fragmentation of penicillin by exocellular DD-carboxype...
Scientific journals : Article
Life sciences : Microbiology
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/87342
Fate of thiazolidine ring during fragmentation of penicillin by exocellular DD-carboxypeptidase-transpeptidase of Streptomyces R61
English
Frère, Jean-Marie mailto [Université de Liège - ULg > Faculté de Médecine, Institut de Botanique > Service de Microbiologie > >]
Ghuysen, Jean-Marie [Université de Liège - ULg > Faculté de Médecine, Institut de Botanique > Service de Microbiologie > >]
Vanderhaeghe, Hubert [Katholieke Universiteit Leuven - KUL > Rega Institut > > >]
Adriaens, Paul [Katholieke Universiteit Leuven - KUL > Rega Institut > > > >]
Degelaen, Jacques [Université Catholique de Louvain - UCL > > Laboratoire de Chimie thérapeutique > >]
De Graeve, Jean [Université de Liège - ULg > Faculté de Médecine > Laboratoire de Chimie médicale > >]
1-Apr-1976
Nature
Nature Publishing Group
260
5550
451-454
Yes (verified by ORBi)
International
0028-0836
1476-4687
Basingstoke
United Kingdom
[en] kinetics ; penicillin g/metabolism ; penicillin v/metabolism ; penicillinase/*metabolism ; penicillins/*metabolism ; streptomyces/enzymology ; thiazoles/metabolism
[en] LIKE various beta-lactamases, acylases and esterases1, the exocellular DD-carboxypeptidase-transpeptidase of Streptomyces R61 degrades benzylpenicillin and other beta-lactam antibiotics2-4. The R61 enzyme, however, markedly differs from the other penicillin-degrading enzymes in causing fragmentation of the penicillin nucleus. By using 8-14C-benzylpenicillin (benzyl labelled) as substrate, one of the fragments produced was shown to be 14C-phenylacetylglycine5. The reaction with the R61 enzyme is also peculiar in that it is a slow process. This is because of the long half life of the stoichiometnc complex transitorily formed between the antibiotic and the enzyme. Thus, for example, the value of the half life for the complex formed with benzylpenicillin is 80 min in 10 mM phosphate buffer (pH 7.0) and at 37 °C. As breakdown of the complex proceeds, however, phenylacetylglycine (when benzylpenicillin is used as substrate) is released and the enzyme concomitantly recovers its ability to bind penicillin. We have now characterised the fragment (hereby designated as the Y product) arising from the thiazolidine ring of penicillin as a result of the fragmentation of the antibiotic molecule by the R61 enzyme.
Fonds de la Recherche Fondamentale Collective - FRFC
Researchers ; Professionals
http://hdl.handle.net/2268/87342
10.1038/260451a0
http://www.nature.com/nature/journal/v260/n5550/abs/260451a0.html

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