Biosynthesis of bacillomycin D by Bacillus subtilis. Evidence for amino acid-activating enzymes by the use of affinity chromatography.
Bacillomycin D is an antifungal lipopeptide produced by B. subtilis. The formation of the peptidyl bonds of bacillomycin D occurs non-ribosomally, as demonstrated by the use of chloramphenicol, an inhibitor of protein biosynthesis. Amino acid-activating enzymes were found in B. subtilis cell lysates purified by affinity chromatography on a gel containing L-Pro, an amino acid of bacillomycin D. Presence of ATP during this purification increases the binding of enzymatic proteins and their activity. An enzyme, with an apparent molecular weight of 230 kDa, catalyzed ATP-PPi exchange reactions, which were mediated by specific amino acids, corresponding to a partial sequence of bacillomycin D.
Besson
F
F
Laboratoire de Biochimie Microbienne (CNRS UMR 24), Université Claude-Bernard Lyon I, Villeurbanne, France.
Michel
G
G
D000255:Adenosine Triphosphate / Q000378:metabolism; D000595:Amino Acid Sequence; D000604:Amino Acyl-tRNA Synthetases / Q000302:isolation & purification / Q000378:metabolism*; D000900:Anti-Bacterial Agents / Q000096:biosynthesis*; D023181:Antimicrobial Cationic Peptides; D001412:Bacillus subtilis / Q000378:metabolism*; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010455:Peptides; D010456:Peptides, Cyclic / Q000096:biosynthesis; D046249:Transfer RNA Aminoacylation
D000900:Anti-Bacterial Agents; D023181:Antimicrobial Cationic Peptides; D010455:Peptides; D010456:Peptides, Cyclic; C027845:bacillomycin D; D000255:Adenosine Triphosphate; D000604:Amino Acyl-tRNA Synthetases