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- W1829933356 abstract "Opium poppy ( Papaver somniferum ) produces several pharmacologically important benzylisoquinoline alkaloids including the vasodilator papaverine. Pacodine and palaudine are tri‐ O ‐methylated analogs of papaverine, which contains four O ‐linked methyl groups. However, the biosynthetic origin of pacodine and palaudine has not been established. Three members of the 2‐oxoglutarate/Fe 2+ ‐dependent dioxygenases (2ODDs) family in opium poppy display widespread O ‐dealkylation activity on several benzylisoquinoline alkaloids with diverse structural scaffolds, and two are responsible for the antepenultimate and ultimate steps in morphine biosynthesis. We report a novel 2ODD from opium poppy catalyzing the efficient substrate‐ and regio‐specific 7‐ O ‐demethylation of papaverine yielding pacodine. The occurrence of papaverine 7‐ O ‐demethylase (P7ODM) expands the enzymatic scope of the 2ODD family in opium poppy and suggests an unexpected biosynthetic route to pacodine." @default.
- W1829933356 created "2016-06-24" @default.
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- W1829933356 date "2015-08-08" @default.
- W1829933356 modified "2023-10-18" @default.
- W1829933356 title "Papaverine 7‐<i>O</i>‐demethylase, a novel 2‐oxoglutarate/Fe<sup>2+</sup>‐dependent dioxygenase from opium poppy" @default.
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- W1829933356 doi "https://doi.org/10.1016/j.febslet.2015.07.042" @default.
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