In vitro reconstruction of tetronate RK-682 biosynthesis

The protein phosphatase inhibitor RK-682 is one of a number of potentially valuable tetronate polyketide natural products. Understanding how the tetronate ring is formed has been frustrated by the inaccessibility of the putative substrates. We report the heterologous expression of rk genes in Saccha...

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Detalles Bibliográficos
Autores principales: Sun, Yuhui, Hahn, Frank, Demydchuk, Yuliya, Chettle, James, Tosin, Manuela, Osada, Hiroyuki, Leadlay, Peter F.
Formato: Texto
Lenguaje:English
Publicado: 2009
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2811812/
https://www.ncbi.nlm.nih.gov/pubmed/20081823
http://dx.doi.org/10.1038/nchembio.285
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author Sun, Yuhui
Hahn, Frank
Demydchuk, Yuliya
Chettle, James
Tosin, Manuela
Osada, Hiroyuki
Leadlay, Peter F.
author_facet Sun, Yuhui
Hahn, Frank
Demydchuk, Yuliya
Chettle, James
Tosin, Manuela
Osada, Hiroyuki
Leadlay, Peter F.
author_sort Sun, Yuhui
collection PubMed
description The protein phosphatase inhibitor RK-682 is one of a number of potentially valuable tetronate polyketide natural products. Understanding how the tetronate ring is formed has been frustrated by the inaccessibility of the putative substrates. We report the heterologous expression of rk genes in Saccharopolyspora erythraea and reconstitution of the RK-682 pathway using recombinant enzymes, and show that RkD is the enzyme required for RK-682 formation from acyl carrier protein-bound substrates.
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spelling pubmed-28118122010-08-01 In vitro reconstruction of tetronate RK-682 biosynthesis Sun, Yuhui Hahn, Frank Demydchuk, Yuliya Chettle, James Tosin, Manuela Osada, Hiroyuki Leadlay, Peter F. Nat Chem Biol Article The protein phosphatase inhibitor RK-682 is one of a number of potentially valuable tetronate polyketide natural products. Understanding how the tetronate ring is formed has been frustrated by the inaccessibility of the putative substrates. We report the heterologous expression of rk genes in Saccharopolyspora erythraea and reconstitution of the RK-682 pathway using recombinant enzymes, and show that RkD is the enzyme required for RK-682 formation from acyl carrier protein-bound substrates. 2009-12-20 2010-02 /pmc/articles/PMC2811812/ /pubmed/20081823 http://dx.doi.org/10.1038/nchembio.285 Text en Users may view, print, copy, download and text and data- mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use: http://www.nature.com/authors/editorial_policies/license.html#terms
spellingShingle Article
Sun, Yuhui
Hahn, Frank
Demydchuk, Yuliya
Chettle, James
Tosin, Manuela
Osada, Hiroyuki
Leadlay, Peter F.
In vitro reconstruction of tetronate RK-682 biosynthesis
title In vitro reconstruction of tetronate RK-682 biosynthesis
title_full In vitro reconstruction of tetronate RK-682 biosynthesis
title_fullStr In vitro reconstruction of tetronate RK-682 biosynthesis
title_full_unstemmed In vitro reconstruction of tetronate RK-682 biosynthesis
title_short In vitro reconstruction of tetronate RK-682 biosynthesis
title_sort in vitro reconstruction of tetronate rk-682 biosynthesis
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2811812/
https://www.ncbi.nlm.nih.gov/pubmed/20081823
http://dx.doi.org/10.1038/nchembio.285
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AT chettlejames invitroreconstructionoftetronaterk682biosynthesis
AT tosinmanuela invitroreconstructionoftetronaterk682biosynthesis
AT osadahiroyuki invitroreconstructionoftetronaterk682biosynthesis
AT leadlaypeterf invitroreconstructionoftetronaterk682biosynthesis

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