The induction of enhanced glucosamine incorporation into the cell-envelope of Escherichia coli K-12 by the antibiotic tetaine.
Henryk Chmara, Edward Borowski
Abstract
Henryk Chmara, Edward Borowski
Abstract
The dipeptide antibiotic tetaine and its C-terminal aminoacid-anticapsin are powerfull inhibitors of glucosamine-synthetase EC 5.3.1.19 activity in cell-free extract from Escherichia coli K-12. Tetaine strongly inhibits the incorporation of diaminopimelic acid into the peptidoglycan of bacteria. In media with carbon source other than glucose tetaine induced of enhanced glucosamine incorporation into the cell-envelope of Escherichia coli K-12. Compounds from cell-envelope with enhanced labeled glucosamine contents are solubilisable by pronase treatment.
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The dipeptide antibiotic tetaine and its C-terminal aminoacid-anticapsin are powerfull inhibitors of glucosamine-synthetase EC 5.3.1.19 activity in cell-free extract from Escherichia coli K-12. Tetaine strongly inhibits the incorporation of diaminopimelic acid into the peptidoglycan of bacteria. In media with carbon source other than glucose tetaine induced of enhanced glucosamine incorporation into the cell-envelope of Escherichia coli K-12. Compounds from cell-envelope with enhanced labeled glucosamine contents are solubilisable by pronase treatment.
Key concepts: Glucosamine, Cell envelope, Escherichia coli, Peptidoglycan, Diaminopimelic acid, Pronase, Bacterial cell structure, Bacteria