Feignier C, Besson F, Michel G
Laboratoire de Biochimie Microbienne, Université Claude Bernard-Lyon, Villeurbanne, France.
FEMS Microbiol Lett. 1996 Feb 15;136(2):117-22. doi: 10.1111/j.1574-6968.1996.tb08036.x.
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.
负责枯草芽孢杆菌抗真菌脂肽iturin生物合成的多酶系统通过在不同亲和凝胶上的色谱法进行了部分纯化。在野生型菌株中，iturin合成酶的两个亚基（ITs和ITagp）得到了表征：ITs仅激活iturin氨基酸成分之一的L-丝氨酸，而ITagp激活L-天冬酰胺、D-天冬酰胺、L-谷氨酰胺和L-脯氨酸，这些氨基酸对应于iturin的部分序列。在一个iturin缺陷型突变体中，ITagp亚基的活性发生了改变。
