title: Functional analysis of fengycin synthetase FenD.
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.
authors.affiliation: Department of Health and Nutrition, Chia Nan University of Pharmacy and Science, Tainan 701, Taiwan.
authors.forename: Tsuey-Pin
authors.initials: TP
authors.lastname: Lin
authors.forename: Chyi-Liang
authors.initials: CL
authors.lastname: Chen
authors.forename: Hui-Chuan
authors.initials: HC
authors.lastname: Fu
authors.forename: Cheng-Yeu
authors.initials: CY
authors.lastname: Wu
authors.forename: Guang-Huey
authors.initials: GH
authors.lastname: Lin
authors.forename: Shih-Hao
authors.initials: SH
authors.lastname: Huang
authors.forename: Li-Kwan
authors.initials: LK
authors.lastname: Chang
authors.forename: Shih-Tung
authors.initials: ST
authors.lastname: Liu
mesh_terms: D000595:Amino Acid Sequence; D001412:Bacillus subtilis / Q000201:enzymology* / Q000235:genetics*; D017124:Conserved Sequence; D004926:Escherichia coli / Q000235:genetics; D055666:Lipopeptides; D008074:Lipoproteins / Q000096:biosynthesis; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D046908:Peptide Biosynthesis, Nucleic Acid-Independent; D010453:Peptide Synthases / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D010957:Plasmids
chemical_list: D055666:Lipopeptides; D008074:Lipoproteins; C049972:fengycin; D010453:Peptide Synthases; C110972:fengycin synthetase