Journal
NATURE CHEMICAL BIOLOGY
Volume 6, Issue 2, Pages 99-101Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/NCHEMBIO.285
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Funding
- Biotechnology and Biological Sciences Research Council, Deutsche Forschungsgemeinschaft Research Fellowship [BB/D018943/1]
- Marie Curie Intra-European Fellowship
- Cambridge University
- BBSRC [BB/D018943/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/D018943/1] Funding Source: researchfish
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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.
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