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^*

^*此作品的通信作者

研究成果: 期刊稿件 › 文章 › 同行評審

16 引文斯高帕斯（Scopus）

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.

原文	英語
頁（從 - 到）	159-164
頁數	6
期刊	BBA - Gene Structure and Expression
卷	1730
發行號	2
DOIs	https://doi.org/10.1016/j.bbaexp.2005.02.005
出版狀態	已出版 - 15 08 2005

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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",

author = "Lin, {Tsuey Pin} and Chen, {Chyi Liang} and Fu, {Hui Chuan} and Wu, {Cheng Yeu} and Lin, {Guang Huey} and Huang, {Shih Hao} and Chang, {Li Kwan} and Liu, {Shih Tung}",

year = "2005",

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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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DO - 10.1016/j.bbaexp.2005.02.005

M3 - 文章

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AN - SCOPUS:23644438251

SN - 0167-4781

VL - 1730

SP - 159

EP - 164

JO - BBA - Gene Structure and Expression

JF - BBA - Gene Structure and Expression

IS - 2

ER -

Functional analysis of fengycin synthetase FenD

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