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Article Abstract
We report the identification of the gene cluster responsible for the formation of the -terphenyl derivatives terfestatins B and C and echoside B from the Appalachian strain RM-5-8. We characterize the function of TerB/C, catalysts that work together as a dual enzyme system in the biosynthesis of natural terphenyls. TerB acts as a reductase and TerC as a dehydratase to enable the conversion of polyporic acid to a terphenyl triol intermediate. X-ray crystallography of the apo and substrate-bound forms for both enzymes provides additional mechanistic insights. Validation of the TerC structural model via mutagenesis highlights a critical role of arginine 143 and aspartate 173 in catalysis. Cumulatively, this work highlights a set of enzymes acting in harmony to control and direct reactive intermediates and advances fundamental understanding of the previously unresolved early steps in terphenyl biosynthesis.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8751757 | PMC |
| http://dx.doi.org/10.1021/acschembio.1c00701 | DOI Listing |
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