Purification of the fengycin synthetase multienzyme system from Bacillus subtilis b213.
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.
Steller
S
S
Max-Volmer-lnstitut für Biophysikalische Chemie und Biochemie, Fachgebiet Biochemie und Molekulare Biologie, Technische Universität Berlin, Germany.
Vater
J
J
D000595:Amino Acid Sequence; D001412:Bacillus subtilis / Q000201:enzymology*; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D008074:Lipoproteins / Q000737:chemistry; D010446:Peptide Fragments / Q000737:chemistry; D010453:Peptide Synthases / Q000302:isolation & purification*
D008074:Lipoproteins; D010446:Peptide Fragments; D010453:Peptide Synthases; C110972:fengycin synthetase