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A methyltransferase initiates terpene cyclization in teleocidin B biosynthesis

Teleocidin B is an indole terpenoid isolated from Streptomyces. Due to its unique chemical structure and ability to activate protein kinase C, it has attracted interest in the areas of organic chemistry and cell biology. Here, we report the identification of genes encoding enzymes for teleocidin B b... Full description

Journal Title: Journal of the American Chemical Society 16 July 2014, Vol.136(28), pp.9910-3
Main Author: Awakawa, Takayoshi
Other Authors: Zhang, Lihan , Wakimoto, Toshiyuki , Hoshino, Shotaro , Mori, Takahiro , Ito, Takuya , Ishikawa, Jun , Tanner, Martin E , Abe, Ikuro
Format: Electronic Article Electronic Article
Language: English
Subjects:
ID: E-ISSN: 1520-5126 ; PMID: 24992358 Version:1 ; DOI: 10.1021/ja505224r
Link: http://pubmed.gov/24992358
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recordid: medline24992358
title: A methyltransferase initiates terpene cyclization in teleocidin B biosynthesis
format: Article
creator:
  • Awakawa, Takayoshi
  • Zhang, Lihan
  • Wakimoto, Toshiyuki
  • Hoshino, Shotaro
  • Mori, Takahiro
  • Ito, Takuya
  • Ishikawa, Jun
  • Tanner, Martin E
  • Abe, Ikuro
subjects:
  • Anti-Bacterial Agents -- Biosynthesis
  • Lyngbya Toxins -- Biosynthesis
  • Methyltransferases -- Chemistry
  • Streptomyces -- Enzymology
  • Terpenes -- Metabolism
ispartof: Journal of the American Chemical Society, 16 July 2014, Vol.136(28), pp.9910-3
description: Teleocidin B is an indole terpenoid isolated from Streptomyces. Due to its unique chemical structure and ability to activate protein kinase C, it has attracted interest in the areas of organic chemistry and cell biology. Here, we report the identification of genes encoding enzymes for teleocidin B biosynthesis, including nonribosomal peptide synthetase (tleA), P-450 monooxygenase (tleB), prenyltransferase (tleC), and methyltransferase (tleD). The tleD gene, which is located outside of the tleABC cluster on the chromosome, was identified by transcriptional analysis and heterologous expression. Remarkably, TleD not only installs a methyl group on the geranyl moiety of the precursor but also facilitates the nucleophilic attack from the electron-rich indole to the resultant cation, to form the indole-fused six-membered ring. This is the first demonstration of a cation, generated from methylation, triggering successive terpenoid ring closure.
language: eng
source:
identifier: E-ISSN: 1520-5126 ; PMID: 24992358 Version:1 ; DOI: 10.1021/ja505224r
fulltext: fulltext
issn:
  • 15205126
  • 1520-5126
url: Link


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titleA methyltransferase initiates terpene cyclization in teleocidin B biosynthesis
creatorAwakawa, Takayoshi ; Zhang, Lihan ; Wakimoto, Toshiyuki ; Hoshino, Shotaro ; Mori, Takahiro ; Ito, Takuya ; Ishikawa, Jun ; Tanner, Martin E ; Abe, Ikuro
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subjectAnti-Bacterial Agents -- Biosynthesis ; Lyngbya Toxins -- Biosynthesis ; Methyltransferases -- Chemistry ; Streptomyces -- Enzymology ; Terpenes -- Metabolism
descriptionTeleocidin B is an indole terpenoid isolated from Streptomyces. Due to its unique chemical structure and ability to activate protein kinase C, it has attracted interest in the areas of organic chemistry and cell biology. Here, we report the identification of genes encoding enzymes for teleocidin B biosynthesis, including nonribosomal peptide synthetase (tleA), P-450 monooxygenase (tleB), prenyltransferase (tleC), and methyltransferase (tleD). The tleD gene, which is located outside of the tleABC cluster on the chromosome, was identified by transcriptional analysis and heterologous expression. Remarkably, TleD not only installs a methyl group on the geranyl moiety of the precursor but also facilitates the nucleophilic attack from the electron-rich indole to the resultant cation, to form the indole-fused six-membered ring. This is the first demonstration of a cation, generated from methylation, triggering successive terpenoid ring closure.
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titleA methyltransferase initiates terpene cyclization in teleocidin B biosynthesis
descriptionTeleocidin B is an indole terpenoid isolated from Streptomyces. Due to its unique chemical structure and ability to activate protein kinase C, it has attracted interest in the areas of organic chemistry and cell biology. Here, we report the identification of genes encoding enzymes for teleocidin B biosynthesis, including nonribosomal peptide synthetase (tleA), P-450 monooxygenase (tleB), prenyltransferase (tleC), and methyltransferase (tleD). The tleD gene, which is located outside of the tleABC cluster on the chromosome, was identified by transcriptional analysis and heterologous expression. Remarkably, TleD not only installs a methyl group on the geranyl moiety of the precursor but also facilitates the nucleophilic attack from the electron-rich indole to the resultant cation, to form the indole-fused six-membered ring. This is the first demonstration of a cation, generated from methylation, triggering successive terpenoid ring closure.
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titleA methyltransferase initiates terpene cyclization in teleocidin B biosynthesis
authorAwakawa, Takayoshi ; Zhang, Lihan ; Wakimoto, Toshiyuki ; Hoshino, Shotaro ; Mori, Takahiro ; Ito, Takuya ; Ishikawa, Jun ; Tanner, Martin E ; Abe, Ikuro
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abstractTeleocidin B is an indole terpenoid isolated from Streptomyces. Due to its unique chemical structure and ability to activate protein kinase C, it has attracted interest in the areas of organic chemistry and cell biology. Here, we report the identification of genes encoding enzymes for teleocidin B biosynthesis, including nonribosomal peptide synthetase (tleA), P-450 monooxygenase (tleB), prenyltransferase (tleC), and methyltransferase (tleD). The tleD gene, which is located outside of the tleABC cluster on the chromosome, was identified by transcriptional analysis and heterologous expression. Remarkably, TleD not only installs a methyl group on the geranyl moiety of the precursor but also facilitates the nucleophilic attack from the electron-rich indole to the resultant cation, to form the indole-fused six-membered ring. This is the first demonstration of a cation, generated from methylation, triggering successive terpenoid ring closure.
doi10.1021/ja505224r
pmid24992358
date2014-07-16