2447-54-3Relevant articles and documents
One step enzymatic synthesis of dihydrosanguinarine from protopine
Tanahashi,Zenk
, p. 5625 - 5628 (1988)
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A novel C-C radical-radical coupling reaction promoted by visible light: Facile synthesis of 6-substituted: N -methyl 5,6-dihydrobenzophenanthridine alkaloids
Liu, Zhaoying,Huang, Yajun,Xie, Hongqi,Liu, Wei,Zeng, Jianguo,Cheng, Pi
, p. 50500 - 50505 (2016/06/09)
A novel photoredox-mediated direct intermolecular C-H functionalization of N-methyl 5,6-dihydrobenzophenanthridine is developed utilizing the visible light-induced reductive quenching pathway of photocatalyst Ir(ppy)3. In the proposed coupling mechanism, an α-amino C-radical is generated at the 6-position of N-methyl 5,6-dihydrobenzophenanthridine which is capable of coupling with α-EWG (electron withdrawing group) substituted C-radicals. The utility of this methodology has been demonstrated via rapid access to the analogue of natural 6-substituted N-methyl 5,6-dihydrobenzophenanthridine alkaloids.
Characterization of a flavoprotein oxidase from opium poppy catalyzing the final steps in sanguinarine and papaverine biosynthesis
Hagel, Jillian M.,Beaudoin, Guillaume A. W.,Fossati, Elena,Ekins, Andrew,Martin, Vincent J. J.,Facchini, Peter J.
, p. 42972 - 42983 (2013/03/13)
Benzylisoquinoline alkaloids are a diverse class of plant specialized metabolites that includes the analgesic morphine, the antimicrobials sanguinarine and berberine, and the vasodilator papaverine. The two-electron oxidation of dihydrosanguinarine catalyzed by dihydrobenzophenanthridine oxidase (DBOX) is the final step in sanguinarine biosynthesis. The formation of the fully conjugated ring system in sanguinarine is similar to the four-electron oxidations of (S)-canadine to berberine and (S)-tetrahydropapaverine to papaverine. We report the isolation and functional characterization of an opium poppy (Papaver somniferum) cDNA encoding DBOX, a flavoprotein oxidase with homology to ( S)-tetrahydroprotoberberine oxidase and the berberine bridge enzyme. A query of translated opium poppy stem transcriptome databases using berberine bridge enzyme yielded several candidate genes, including an (S)-tetrahydroprotoberberine oxidase-like sequence selected for heterologous expression in Pichia pastoris. The recombinant enzyme preferentially catalyzed the oxidation of dihydrosanguinarine to sanguinarine but also converted (RS)-tetrahydropapaverine to papaverine and several protoberberine alkaloids to oxidized forms, including (RS)-canadine to berberine. The Km values of 201 and 146 μM for dihydrosanguinarine and the protoberberine alkaloid (S)-scoulerine, respectively, suggested high concentrations of these substrates in the plant. Virus-induced gene silencing to reduce DBOX transcript levels resulted in a corresponding reduction in sanguinarine, dihydrosanguinarine, and papaverine accumulation in opium poppy roots in support of DBOX as a multifunctional oxidative enzyme in BIA metabolism.