| Literature DB >> 10681064 |
Abstract
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 14C-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.Entities:
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Year: 2000 PMID： 10681064 DOI： 10.1016/s0378-4347(99)00481-8
Source DB: PubMed Journal: J Chromatogr B Biomed Sci Appl ISSN： 1387-2273