Functional analysis of fengycin synthetase FenD
- 作者：Tsuey-Pin Lin ; Chyi-Liang Chen ; Hui-Chuan Fu ; Cheng-Yeu Wu ; Guang-Huey Lin ; Shih-Hao Huang ; Li-Kwan Chang and Shih-Tung Liu
- 关键词：Fengycin ; Peptide synthetase ; Nonribosomal peptide synthesis
- 刊名：Biochimica et Biophysica Acta (BBA)/Gene Structure and Expression
- 出版年：2005
- 期刊代码：15_01674781
- 类别：bio
- 出版时间：2005
- 卷：1730
- 期：2
- 页码：159-164
- 文件大小：152 K
摘要
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.