In vitro production of bacitracin by proteolysis of vegetative Bacillus licheniformis cell protein.
The action of a sporulation-specific seryl protease on antibiotic-free extracts of Bacillus licheniformis cells yields a peptide that is identified as bacitracin by its biological activity, its spectral properties, and its comigration with genuine bacitracin in both paper and thin-layer chromatography. During proteolysis, a chemical structure is generated with the spectral properties of a delta-2 thiazoline ring. The yield in vitro, 4 microgram of bacitracin per mg of protein, is less than the maximal yield from sporulating cells, 75 microgram of bacitracin per mg of cell protein, but is a linear function of the amount of protein in the reaction system. Approximately 30% of the protein yielding the antibiotic is ribosomal associated, and only 25% of that amount can be removed by washing with 1 M NH4Cl. The substrate protein is a constant fraction of the cell protein throughout exponential growth and very early sporulation stages of culture development.
D001407:Bacillus / Q000201:enzymology / Q000254:growth & development / Q000378:metabolism*; D001414:Bacitracin / Q000096:biosynthesis*; D001426:Bacterial Proteins / Q000378:metabolism*; D002474:Cell-Free System; D010447:Peptide Hydrolases / Q000378:metabolism; D011498:Protein Precursors / Q000378:metabolism; D012270:Ribosomes / Q000378:metabolism; D012694:Serine; D013171:Spores, Bacterial / Q000201:enzymology / Q000378:metabolism
D001426:Bacterial Proteins; D011498:Protein Precursors; D001414:Bacitracin; D012694:Serine; D010447:Peptide Hydrolases