Functional analysis of fengycin synthetase FenD

Tsuey Pin Lin; Chyi Liang Chen; Hui Chuan Fu; Cheng Yeu Wu; Guang Huey Lin; Shih Hao Huang; Li Kwan Chang; Shih Tung Liu

doi:10.1016/j.bbaexp.2005.02.005

Functional analysis of fengycin synthetase FenD

Tsuey Pin Lin, Chyi Liang Chen, Hui Chuan Fu, Cheng Yeu Wu, Guang Huey Lin, Shih Hao Huang, Li Kwan Chang, Shih Tung Liu^*

^*Corresponding author for this work

Research output: Contribution to journal › Journal Article › peer-review

16 Scopus citations

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.

Original language	English
Pages (from-to)	159-164
Number of pages	6
Journal	BBA - Gene Structure and Expression
Volume	1730
Issue number	2
DOIs	https://doi.org/10.1016/j.bbaexp.2005.02.005
State	Published - 15 08 2005

Keywords

Fengycin
Nonribosomal peptide synthesis
Peptide synthetase

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10.1016/j.bbaexp.2005.02.005

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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.",

keywords = "Fengycin, Nonribosomal peptide synthesis, Peptide synthetase",

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doi = "10.1016/j.bbaexp.2005.02.005",

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TY - JOUR

T1 - Functional analysis of fengycin synthetase FenD

AU - Lin, Tsuey Pin

AU - Chen, Chyi Liang

AU - Fu, Hui Chuan

AU - Wu, Cheng Yeu

AU - Lin, Guang Huey

AU - Huang, Shih Hao

AU - Chang, Li Kwan

AU - Liu, Shih Tung

PY - 2005/8/15

Y1 - 2005/8/15

N2 - 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.

AB - 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.

KW - Fengycin

KW - Nonribosomal peptide synthesis

KW - Peptide synthetase

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U2 - 10.1016/j.bbaexp.2005.02.005

DO - 10.1016/j.bbaexp.2005.02.005

M3 - 文章

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AN - SCOPUS:23644438251

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SP - 159

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JO - BBA - Gene Structure and Expression

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IS - 2

ER -

Functional analysis of fengycin synthetase FenD

Abstract

Keywords

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