Characterization of iturin synthetase in the wild-type Bacillus subtilis strain producing iturin and in an iturin deficient mutant.
The multi-enzyme system responsible for the biosynthesis of iturin, an antifungal lipopeptide of Bacillus subtilis, was partially purified by chromatography on different affigels. In the wild-type strain, two subunits of the iturin synthetase (ITs and ITagp) were characterized: ITs activated only L-Ser, one of the iturin amino acid components, and ITagp activated L-Asn, D-Asn, L-Gln and L-Pro, amino acids corresponding to a partial sequence of iturin. In an iturin deficient mutant, the activity of the ITagp subunit was modified.
Feignier
C
C
Laboratoire de Biochimie Microbienne, Université Claude Bernard-Lyon, Villeurbanne, France.
Besson
F
F
Michel
G
G
D000900:Anti-Bacterial Agents / Q000096:biosynthesis*; D000935:Antifungal Agents / Q000096:biosynthesis*; D001412:Bacillus subtilis / Q000201:enzymology*; D001426:Bacterial Proteins / Q000302:isolation & purification; D002846:Chromatography, Affinity; D008025:Ligases / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D008074:Lipoproteins / Q000096:biosynthesis / Q000235:genetics; D009154:Mutation / Q000502:physiology; D010455:Peptides; D010456:Peptides, Cyclic
D000900:Anti-Bacterial Agents; D000935:Antifungal Agents; D001426:Bacterial Proteins; D008074:Lipoproteins; D010455:Peptides; D010456:Peptides, Cyclic; C013579:iturin A; D008025:Ligases