Reference : The penicillin-binding proteins in Streptococcus faecalis ATCC 9790
Scientific journals : Article
Life sciences : Microbiology
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/83038
The penicillin-binding proteins in Streptococcus faecalis ATCC 9790
English
Coyette, Jean [Université de Liège - ULiège > Faculté de Médecine > Service de Microbiologie > > >]
Ghuysen, Jean-Marie [Université de Liège - ULiège > Faculté de Médecine > Service de Microbiologie > > >]
Fontana, Roberta [Università di Sassari > Instituto di Microbiologica > > >]
1-Sep-1980
European Journal of Biochemistry
Blackwell Science
110
2
445-456
Yes (verified by ORBi)
International
0014-2956
1432-1033
Oxford
United Kingdom
[en] binding, competitive ; carrier proteins/*metabolism ; cell membrane/metabolism ; enterococcus faecalis/*metabolism ; half-life ; kinetics ; molecular weight ; muramoylpentapeptide carboxypeptidase/metabolism ; penicillin g/metabolism ; penicillins/*metabolism
[en] Streptococcus faecalis ATCC 9790 possesses seven membrane-bound penicillin-binding proteins. They have been characterized with respect to their apparent molecular weights, relative abundance, specificity profiles for 15 different beta-lactam antibiotics and stability under various conditions. In water and at 37 degrees C, all the native penicillin-binding proteins have half-lives longer than 20 h except protein 3b (half-life of about 600 min) and protein 4 (half-life of about 175 min). The short-lived 80 000-Mr protein 4 is spontaneously converted into a 73 000-Mr water-soluble, penicillin-binding protein 4. Similarly, the short-lived 82 000-Mr protein 3b seems to be the protein from which the 72 000-Mr water-soluble protein X spontaneously originates during incubation of the membranes. Release of both proteins 4 and X from the membrane is maximal under alkaline conditions; it is not inhibited by various protease inhibitors. After exposure to trypsin, the 43 000-Mr membrane-bound penicillin binding protein 6 (a DD-carboxypeptidase) gives to a 30 000-Mr water-soluble protein 6. Like the parent protein, protein 6 exhibits both DD-carboxypeptidase activity and penicillin-binding ability. With proteins 6 and 6, low dose levels of p-chloromercuribenzoate prevent both enzyme activity and combination with penicillin, thus strongly suggesting that a thiol group is involved in the enzyme active center. We have shown previously [Coyette et al. in Eur. J. Biochem. 88, 297--305 (1978) and 75, 231--239 (1977)] that the DD-carboxypeptidase protein 6 fragments the benzylpenicillin molecule with formation of phenylacetylglycine. Breakdown of the complex formed between [14C]benzylpenicillin and 14 000-Mr membrane-bound protein 1 is also 'enzyme-catalysed'. Most likely, however, the released product is penicilloate. With all the other penicillin-binding proteins whose molecular weights are intermediate between those of proteins 1 and 6, breakdown of the complexes formed with [14C]benzylpenicillin results from proteolysis and is not due to the release of the bound metabolite. None of the penicillin-binding proteins behaves, by itself, as a lethal target for beta-lactam antibiotic action on the living cells.
Fonds de la Recherche Scientifique Médicale - FRSM ; National Institutes of Health - NIH
Researchers ; Professionals
http://hdl.handle.net/2268/83038

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