Journal
SCIENCE
Volume 349, Issue 6245, Pages 309-312Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.aab1852
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Funding
- UK Biotechnology and Biological Sciences Research Council [BB/K018809/1]
- Garfield Weston Foundation
- Biotechnology and Biological Sciences Research Council [BB/K018809/1, BB/L004917/1] Funding Source: researchfish
- BBSRC [BB/L004917/1, BB/K018809/1] Funding Source: UKRI
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Morphinan alkaloids from the opium poppy are used for pain relief. The direction of metabolites to morphinan biosynthesis requires isomerization of (S)-to (R)-reticuline. Characterization of high-reticuline poppy mutants revealed a genetic locus, designated STORR [(S)-to (R)-reticuline] that encodes both cytochrome P450 and oxidoreductase modules, the latter belonging to the aldo-keto reductase family. Metabolite analysis of mutant alleles and heterologous expression demonstrate that the P450 module is responsible for the conversion of (S)-reticuline to 1,2-dehydroreticuline, whereas the oxidoreductase module converts 1,2-dehydroreticuline to (R)-reticuline rather than functioning as a P450 redox partner. Proteomic analysis confirmed that these two modules are contained on a single polypeptide in vivo. This modular assembly implies a selection pressure favoring substrate channeling. The fusion protein STORR may enable microbial-based morphinan production.
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