1,2-dehydroreticulinium reductase (NADPH)

Class of enzymes 1,2-dehydroreticulinium reductase (NADPH) 1.5.1.27 130590-58-8 0047128 1,2-dehydroreticulinium reductase (NADPH) (1.5.1.27) is an enzyme that catalyzes the chemical reaction 65% Q27103030 reticulinylium cation + NADPH H+ Q82096614 (R)-reticuline + NADP+ The three substrates of this enzyme are 1,2-dehydroreticulinium cation, reduced nicotinamide adenine dinucleotide phosphate (NADPH) and a proton. Its products are (R)-reticuline and oxidised NADP+. The enzyme does not catalyse the reverse (oxidation) reaction.1.5.1.27 De-Eknamkul W, Zenk MH 1992 Purification and properties of 1,2-dehydroreticulinium reductase from Papaver somniferum seedlings Phytochemistry 31 3 10.1016/0031-9422(92)80020-F 813–821 1992PChem..31..813D This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (R)-reticuline:NADP+ oxidoreductase. This enzyme is also called 1,2-dehydroreticulinium ion reductase. It participates in morphinan alkaloid biosynthesis. In the opium poppy, Papaver somniferum, this enzyme forms a fusion protein with 1,2-dehydroreticuline synthase, which converts (S)-reticuline to reticulinylium cation. The overall result is that the (S) enantiomer of reticuline is converted to {R)-reticuline, which is the precursor of salutaridine, on the pathway to morphine.Winzer Thilo Kern Marcelo King Andrew J. Larson Tony R. Teodor Roxana I. Donninger Samantha L. Li Yi Dowle Adam A. Cartwright Jared Bates Rachel Ashford David Thomas Jerry Walker Carol Bowser Tim A. Graham Ian A. Morphinan biosynthesis in opium poppy requires a P450-oxidoreductase fusion protein Science 2015 349 6245 309–312 10.1126/science.aab1852 26113639 This gene fusion event has been suggested to evolve only once, about 20 million years ago. Tian Y, Kong L, Li Q, Wang Y, Wang Y, An Z, Ma Y, Tian L, Duan B, Sun W, Gao R, Chen S, Xu Z Structural diversity, evolutionary origin, and metabolic engineering of plant specialized benzylisoquinoline alkaloids Natural Product Reports 41 11 1787–1810 November 2024 39360417 10.1039/d4np00029c Carr Samuel C. Rehman Fasih Hagel Jillian M. Chen Xue Ng Kenneth K. S. Facchini Peter J. Two ubiquitous aldo-keto reductases in the genus Papaver support a patchwork model for morphine pathway evolution Communications Biology 2024 7 1 1410 10.1038/s42003-024-07100-w free 39472466 11522673 70% Q6122828 (S)-reticuline Q82096614 (R)-reticuline salutaridine 0.5 References Biology no Category:EC 1.5.1 Category:NADPH-dependent enzymes Category:Enzymes of unknown structure