The formation of functional penicillin-binding proteins.

Article Details

Citation

Copy to clipboard

Hamilton TE, Lawrence PJ

The formation of functional penicillin-binding proteins.

J Biol Chem. 1975 Aug 25;250(16):6578-85.

PubMed ID

808545 [ View in PubMed

]

Abstract

A method was developed which permitted determination of the [14C]benzylpenicillin and [14C]Cephapirin binding capacity of rapidly growing Bacillus subtilis cells in liquid culture. Over the concentration range of the binding plateau (0.1 to 0.8 mug/ml), [14C]benzylpenicillin significantly inhibited formation of functional penicillin-binding proteins, but had comparatively little effect on total bacterial protein synthesis. The data suggest that penicillin covalently bound to the cells in a chemically stable manner alone is not sufficient to inhibit formation of functional binding proteins and that unbound penicillin in the growth medium is necessary. The concentration of unbound antibiotic in the culture medium, in turn, is a function of the cell-bound penicillinase activity whose significance increases with cell density. [14C]Cephapirin, a cephalosporin resistant to this cell-bound penicillinase almost completely inhibited the formation of functional Cephapirin-binding proteins, but had relatively little effect on total protein synthesis. At concentrations 250-fold higher than that required to inhibit formation of functional binding proteins. Cephapirin did not inhibit particulate D-alanine carboxypeptidase activity and presumably did not bind covalently to this penicillin-binding protein.

DrugBank Data that Cites this Article

Drug Targets

Drug	Target	Kind	Organism	Pharmacological Action	Actions
Cefapirin	Penicillin-binding protein 1A	Protein	Clostridium perfringens (strain 13 / Type A)	Yes	Inhibitor	Details