Studies on the biosynthesis of surfactin, a lipopeptide antibiotic from Bacillus subtilis ATCC 21332.
The biosynthesis of the lipopeptide antibiotic surfactin was studied in whole cells of Bacillus subtilis ATCC 21332 which incorporate 14C-labeled precursor amino acids directly into the product. [14C]Acetate appeared in the fatty acid portion of surfactin and was also partially converted into leucine. An enzyme was isolated and partially purified from a cell-free extract of the bacillus which catalyzes ATP-Pi-exchange reactions which are mediated by the amino acid components of surfactin. This activation pattern is consistent with a peptide synthesizing multienzyme which activates its substrate amino acids simultaneously as reactive aminoacyl phosphates.
D000085:Acetates / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000378:metabolism; D000596:Amino Acids / Q000032:analysis; D000903:Antibiotics, Antineoplastic / Q000096:biosynthesis*; D001412:Bacillus subtilis / Q000378:metabolism*; D001426:Bacterial Proteins / Q000096:biosynthesis*; D002250:Carbon Radioisotopes; D002474:Cell-Free System; D055666:Lipopeptides; D010456:Peptides, Cyclic; D010710:Phosphates / Q000378:metabolism
D000085:Acetates; D000596:Amino Acids; D000903:Antibiotics, Antineoplastic; D001426:Bacterial Proteins; D002250:Carbon Radioisotopes; D055666:Lipopeptides; D010456:Peptides, Cyclic; D010710:Phosphates; C009365:surfactin peptide; D000255:Adenosine Triphosphate