Article (Scientific journals)
The penicillin-binding proteins in Streptococcus faecalis ATCC 9790
Coyette, Jean; Ghuysen, Jean-Marie; Fontana, Roberta
1980In European Journal of Biochemistry, 110 (2), p. 445-456
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Keywords :
binding, competitive; carrier proteins/*metabolism; cell membrane/metabolism; enterococcus faecalis/*metabolism; half-life; kinetics; molecular weight; muramoylpentapeptide carboxypeptidase/metabolism; penicillin g/metabolism; penicillins/*metabolism
Abstract :
[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.
Disciplines :
Biochemistry, biophysics & molecular biology
Microbiology
Author, co-author :
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
Language :
English
Title :
The penicillin-binding proteins in Streptococcus faecalis ATCC 9790
Publication date :
01 September 1980
Journal title :
European Journal of Biochemistry
ISSN :
0014-2956
eISSN :
1432-1033
Publisher :
Blackwell Science, Oxford, United Kingdom
Volume :
110
Issue :
2
Pages :
445-456
Peer reviewed :
Peer Reviewed verified by ORBi
Funders :
FRSM - Fonds de la Recherche Scientifique Médicale [BE]
NIH - National Institutes of Health [US-MD]
Available on ORBi :
since 27 January 2011

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