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- W4254485246 abstract "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." @default.
- W4254485246 created "2022-05-12" @default.
- W4254485246 creator A5025211861 @default.
- W4254485246 date "1996-02-15" @default.
- W4254485246 modified "2023-10-14" @default.
- W4254485246 title "Characterization of iturin synthetase in the wild-type Bacillus subtilis strain producing iturin and in an iturin deficient mutant" @default.
- W4254485246 doi "https://doi.org/10.1016/0378-1097(95)00485-8" @default.
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