salutaridinol/papaver

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Enhanced morphinan alkaloid production in hairy root cultures of Papaver bracteatum by over-expression of salutaridinol 7-o-acetyltransferase gene via Agrobacterium rhizogenes mediated transformation.

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Papaver bracteatum is an important medicinal plant valued for its high content of thebaine and an alternative to P. somniferum for benzylisoquinoline alkaloid production. Salutaridinol 7-o-acetyltransferase (SalAT) is a key gene in morphinan alkaloids biosynthesis pathway. Over expression of SalAT

Molecular characterization of the salutaridinol 7-O-acetyltransferase involved in morphine biosynthesis in opium poppy Papaver somniferum.

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Salutaridinol 7-O-acetyltransferase (EC ) catalyzes the conversion of the phenanthrene alkaloid salutaridinol to salutaridinol-7-O-acetate, the immediate precursor of thebaine along the morphine biosynthetic pathway. We have isolated a cDNA clone that corresponds to the internal amino acid sequences

Crystallization and preliminary X-ray diffraction analysis of salutaridine reductase from the opium poppy Papaver somniferum.

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The opium poppy Papaver somniferum is the source of the narcotic analgesics morphine and codeine. Salutaridine reductase (SalR; EC 1.1.1.248) reduces the C-7 keto group of salutaridine to the C-7 (S)-hydroxyl group of salutaridinol in the biosynthetic pathway that leads to morphine in the opium

Atomic structure of salutaridine reductase from the opium poppy (Papaver somniferum).

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The opium poppy (Papaver somniferum L.) is one of the oldest known medicinal plants. In the biosynthetic pathway for morphine and codeine, salutaridine is reduced to salutaridinol by salutaridine reductase (SalR; EC 1.1.1.248) using NADPH as coenzyme. Here, we report the atomic structure of SalR to

Acetyl coenzyme A:salutaridinol-7-O-acetyltransferase from papaver somniferum plant cell cultures. The enzyme catalyzing the formation of thebaine in morphine biosynthesis.

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Acetyl coenzyme A:salutaridinol-7-O-acetyltransferase, a highly substrate-specific enzyme, has been purified nearly 3,000-fold to homogeneity from Papaver somniferum plant cell suspension cultures. Purification was achieved by fractionated ammonium sulfate precipitation, dye-ligand affinity

RNAi suppression of the morphine biosynthetic gene salAT and evidence of association of pathway enzymes.

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Papaver somniferum L. was transformed with an RNAi construct designed to reduce transcript levels of the gene encoding the morphine biosynthetic enzyme, salutaridinol 7-O-acetyltransferase (SalAT). RNA interference of salAT led to accumulation of the intermediate compounds, salutaridine and

Structural insights into thebaine synthase 2 catalysis

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Thebaine synthase 2 (THS2) that can transform (7S)-salutaridinol 7-O-acetate to thebaine catalyzes the final step of thebaine biosynthesis in Papaver somniferum. Here, the crystal structures of THS2 and its complex with thebaine are reported, revealing the interaction network in the

Biosynthesis of the morphine alkaloids.

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Tracer experiments, supported throughout by the analogous chemical transformations, have firmly established the biosynthetic sequence tyrosine -->norlaudanosoline --> reticuline --> salutaridine --> salutaridinol-I -->thebaine --> codeine --> morphine in Papaver somniferum. In general, the farther a

Genetic and chemical components analysis of Papaver setigerum naturalized in Korea.

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Of the 110 species of genus Papaver, only Papaver somniferum and P. setigerum are controlled poppies in Korea. All poppy samples share similar morphology therefore it is important to check if they contain controlled substances such as morphine and codeine for forensic purpose. Since the alkaloid

Developmental and inducible accumulation of gene transcripts involved in alkaloid biosynthesis in opium poppy.

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Opium poppy (Papaver somniferum) produces a large number of benzylisoquinoline alkaloids, including morphine and sanguinarine, derived from tyrosine via the branch-point intermediate (S)-reticuline. Molecular clones for the three methlytransferases involved in (S)-reticuline biosynthesis,

The roles of latex and the vascular bundle in morphine biosynthesis in the opium poppy, Papaver somniferum.

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The opium poppy, Papaver somniferum, is one of mankind's oldest medicinal plants. Opium poppy today is the commercial source of the narcotic analgesics morphine and codeine. Along with these two morphinans, opium poppy produces approximately eighty alkaloids belonging to various

Comparative transcript and alkaloid profiling in Papaver species identifies a short chain dehydrogenase/reductase involved in morphine biosynthesis.

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Plants of the order Ranunculales, especially members of the species Papaver, accumulate a large variety of benzylisoquinoline alkaloids with about 2500 structures, but only the opium poppy (Papaver somniferum) and Papaver setigerum are able to produce the analgesic and narcotic morphine and the

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