Characterization of iturin synthetase in the wild-type Bacillus subtilis strain producing iturin and in an iturin deficient mutant

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 activate...

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Bibliographic Details
Published in:FEMS microbiology letters 1996-02, Vol.136 (2), p.117-122
Main Authors: Feignier, Christine, Besson, Françoise, Michel, Georges
Format: Article
Language:English
Subjects:
Affinity chromatography
Amino acid activating enzyme
Amino acids
Anti-Bacterial Agents - biosynthesis
Antifungal Agents - biosynthesis
Bacillus subtilis
Bacillus subtilis - enzymology
Bacterial Proteins - isolation & purification
Bacteriology
Biological and medical sciences
Biology of microorganisms of confirmed or potential industrial interest
Biosynthesis
Biotechnology
Chromatography, Affinity
Deficient mutant
Fundamental and applied biological sciences. Psychology
Fungicides
Iturin synthetase multi‐enzyme complex
Ligases - genetics
Ligases - isolation & purification
Ligases - metabolism
Lipoproteins - biosynthesis
Lipoproteins - genetics
Metabolism. Enzymes
Microbiology
Mission oriented research
Mutation - physiology
Peptides
Peptides, Cyclic
Physiology and metabolism
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Summary: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.
ISSN:0378-1097
1574-6968
DOI:10.1111/j.1574-6968.1996.tb08036.x