Functional analysis of fengycin synthetase FenD

Biochim Biophys Acta. 2005 Aug 15;1730(2):159-64. doi: 10.1016/j.bbaexp.2005.02.005. Epub 2005 Mar 2.

Abstract

Fengycin is a cyclic lipopeptidic antibiotic produced nonribosomally by Bacillus subtilis. A fengycin synthetase mutant of B. subtilis F29-3 was generated with Tn917lux, which contains a transposon inserted in a 7716-bp gene, fenD. The mutation can be genetically complemented by transforming a plasmid carrying a wild-type fenD, confirming the participation of the gene in fengycin synthesis. Sequencing and biochemical analysis reveal that this gene encodes an enzyme that includes two amino acid-activating modules, FenD1 and FenD2, which activate l-Tyr and l-Thr, the third and the fourth amino acids in fengycin, respectively.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Bacillus subtilis / enzymology*
  • Bacillus subtilis / genetics*
  • Conserved Sequence
  • Escherichia coli / genetics
  • Lipopeptides
  • Lipoproteins / biosynthesis
  • Molecular Sequence Data
  • Mutagenesis, Site-Directed
  • Peptide Biosynthesis, Nucleic Acid-Independent
  • Peptide Synthases / chemistry
  • Peptide Synthases / genetics*
  • Peptide Synthases / metabolism*
  • Plasmids

Substances

  • Lipopeptides
  • Lipoproteins
  • fengycin
  • Peptide Synthases
  • fengycin synthetase