Purification of the fengycin synthetase multienzyme system from Bacillus subtilis b213

被引：37

作者：

Steller, S ^{[1
]}

Vater, J ^{[1
]}

机构：

[1] Tech Univ Berlin, Fachgebiet Biochem & Mol Biol, Max Volmer Inst Biophys & Phys Chem, D-10587 Berlin, Germany

来源：

JOURNAL OF CHROMATOGRAPHY B-ANALYTICAL TECHNOLOGIES IN THE BIOMEDICAL AND LIFE SCIENCES | 2000年 / 737卷 / 1-2期

关键词：

purification; Bacillus subtilis b213; enzymes; fengycin synthetase;

D O I：

10.1016/S0378-4347(99)00481-8

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

The purification of the multienzyme system producing the lipodecapeptide fengycin in Bacillus subtilis b213 was investigated. By gel filtration of a cell free extract of this organism three enzyme fractions were obtained from which five multifunctional components of fengycin synthetase were separated by high resolution anion-exchange FPLC procedures. These proteins were characterized by their thioester formation activities with C-14-labeled substrate amino acids and by N-terminal sequencing. Correlation of these data with the DNA sequences of the pps (fen) operons in three B. subtilis strains provided detailed knowledge on the structural and functional organization of fengycin synthetase. (C) 2000 Elsevier Science B.V. All rights reserved.

引用

页码：267 / 275

页数：9

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