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体外重建四嗪酸盐 RK-682 生物合成。

In vitro reconstruction of tetronate RK-682 biosynthesis.

机构信息

Department of Biochemistry, University of Cambridge, Cambridge, UK.

出版信息

Nat Chem Biol. 2010 Feb;6(2):99-101. doi: 10.1038/nchembio.285. Epub 2009 Dec 20.

DOI:10.1038/nchembio.285
PMID:20081823
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2811812/
Abstract

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 we show that RkD is the enzyme required for RK-682 formation from acyl carrier protein-bound substrates.

摘要

蛋白磷酸酶抑制剂 RK-682 是一类具有潜在价值的四酮聚酮天然产物之一。由于推测的底物难以接近,因此无法了解四酮环的形成方式。我们报告了在红色糖多孢菌中异源表达 rk 基因,并使用重组酶重新构建了 RK-682 途径,结果表明 RkD 是将酰基辅酶 A 结合的底物转化为 RK-682 所需的酶。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/23ee/2811812/785965248281/ukmss-28007-f0004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/23ee/2811812/06839b2f5bad/ukmss-28007-f0001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/23ee/2811812/c5aedba13d3c/ukmss-28007-f0002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/23ee/2811812/077f6fdf6011/ukmss-28007-f0003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/23ee/2811812/785965248281/ukmss-28007-f0004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/23ee/2811812/06839b2f5bad/ukmss-28007-f0001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/23ee/2811812/c5aedba13d3c/ukmss-28007-f0002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/23ee/2811812/077f6fdf6011/ukmss-28007-f0003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/23ee/2811812/785965248281/ukmss-28007-f0004.jpg

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