Kluge B, Vater J, Salnikow J, Eckart K
Institut für Biochemie und Molekulare Biologie, Technische Universität Berlin, Germany.
FEBS Lett. 1988 Apr 11;231(1):107-10. doi: 10.1016/0014-5793(88)80712-9.
The biosynthesis of the lipopeptide antibiotic surfactin was studied in whole cells of Bacillus subtilis ATCC 21332 which incorporate 14C-labeled precursor amino acids directly into the product. [14C]Acetate appeared in the fatty acid portion of surfactin and was also partially converted into leucine. An enzyme was isolated and partially purified from a cell-free extract of the bacillus which catalyzes ATP-Pi-exchange reactions which are mediated by the amino acid components of surfactin. This activation pattern is consistent with a peptide synthesizing multienzyme which activates its substrate amino acids simultaneously as reactive aminoacyl phosphates.
在枯草芽孢杆菌ATCC 21332的全细胞中研究了脂肽抗生素表面活性素的生物合成，该菌可将14C标记的前体氨基酸直接掺入产物中。[14C]乙酸盐出现在表面活性素的脂肪酸部分，并且也部分转化为亮氨酸。从该芽孢杆菌的无细胞提取物中分离并部分纯化了一种酶，该酶催化由表面活性素的氨基酸成分介导的ATP-磷酸交换反应。这种激活模式与一种肽合成多酶一致，该多酶同时将其底物氨基酸激活为活性氨酰磷酸。
