The enzyme is present in the poppy, Papaver somniferum. At pH 8-9 the product, 7-O-acetylsalutaridinol, spontaneously closes the 4->5 oxide bridge by allylic elimination to form the morphine precursor thebaine
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SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:salutaridinol 7-O-acetyltransferase
The enzyme is present in the poppy, Papaver somniferum. At pH 8-9 the product, 7-O-acetylsalutaridinol, spontaneously closes the 4->5 oxide bridge by allylic elimination to form the morphine precursor thebaine
yeast two-hybrid and co-immunoprecipitation analyses indicate an interaction between salutaridine reductase and SalAT, which suggest the occurrence of an enzyme complex
yeast two-hybrid and co-immunoprecipitation analyses indicate an interaction between salutaridine reductase and SalAT, which suggest the occurrence of an enzyme complex
yeast two-hybrid and co-immunoprecipitation analyses indicate an interaction between salutaridine reductase and SalAT, which suggest the occurrence of an enzyme complex
yeast two-hybrid and co-immunoprecipitation analyses indicate an interaction between salutaridine reductase and SalAT, which suggest the occurrence of an enzyme complex
enzyme protein is restricted to sieve elements of the phloem adjacent or proximal to laticifers. Corresponding gene transcripts are found in the companion cell paired with each sieve element
RNA interference of salAT leads to accumulation of the intermediate compounds, salutaridine and salutaridinol. SalAT transcript is shown by quantitative PCR to be diminished, while salutaridine reductase transcript levels remains unaffected
yeast two-hybrid and co-immunoprecipitation analyses indicate an interaction between salutaridine reductase and SalAT, which suggest the occurrence of an enzyme complex
silencing of the gene encoding SalAT results in the accumulation of salutaridine, which is not the corresponding enzymatic substrate. Reduction of SalAt transcript and protein levels results in an increase in salutaridine, i.e. an approximately 20-fold increase compared with controls, and a concomitant decrease in thebaine levels. Codeine and morphine accumulation are also significantly reduced
specific gene silencing of the enzymes involved in alkaloid biosynthesis in opium poppy using virus-induced gene silencing, VIGS, and Agrobacterium tumefaciens transfection
salutaridine synthase (PsSAS), salutaridine reductase (PsSAR) and salutaridinol acetyltransferase (PsSAT) are functionally coexpressed in Saccharomyces cerevisiae and optimization of the pH conditions allowed for productive spontaneous rearrangement of salutaridinol-7-O-acetate and synthesis of thebaine from (R)-reticuline. A 7-gene pathway for the production of codeine and morphine from (R)-reticuline is reconstituted. Yeast cell feeding assays using (R)-reticuline, salutaridine or codeine as substrates show that all enzymes are functionally coexpressed in yeast and that activity of salutaridine reductase and codeine-O-demethylase likely limit flux to morphine synthesis. The results of this study describe a significant advance for the synthesis of morphinans in Saccharomyces cerevisiae and pave the way for their complete synthesis in recombinant microbes
Agrobacterium-mediated transfection of Papaver somniferum with the salutaridinol 7-O-acetyltransferase gene, 21 transgenic opium poppy plants over-expressing SalAT are analysed in three separate glasshouse trials, suppression of SalAT by RNAi, SalAT involved in alkaloid accumulation
increases in pharmaceutical alkaloid content of potential economic significance have been achieved, RNAi suppression is a powerful way to obtain products that poppy does not normally accumulate
coexpression of Papaver somniferum enzymes salutaridine synthase, salutaridine reductase and salutaridinol in Saccharomyces cerevisiae allows for productive spontaneous rearrangement of salutaridinol-7-O-acetate and synthesis of thebaine from (R)-reticuline. A 7-gene pathway for the production of codeine and morphine from (R)-reticuline can be established. Yeast cell feeding assays using (R)-reticuline, salutaridine or codeine as substrates show that all enzymes are functionally coexpressed and that activity of salutaridine reductase and codeine-O-demethylase likely limit flux to morphine synthesis