1.1.1.248: salutaridine reductase (NADPH)

This is an abbreviated version!
For detailed information about salutaridine reductase (NADPH), go to the full flat file.

Word Map on EC 1.1.1.248

Reaction

salutaridinol
+
NADP+
=
salutaridine
+
NADPH
+
H+

Synonyms

More, PsSAR, reductase, salutaridine 7-, SalR, salutaridine 7-reductase, salutaridine reductase

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.1 With NAD+ or NADP+ as acceptor
                1.1.1.248 salutaridine reductase (NADPH)

Cloned

Cloned on EC 1.1.1.248 - salutaridine reductase (NADPH)

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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloned into the pMyr vector and expressed as fusion protein with a myristylation sequence, which anchors the target protein to the yeast membrane. Fusion proteins (pSOS/SalAT and pMyr/SalR) coexpressed in the Saccharomyces cerevisiae cdc25H strain. SalR amplified from the recombinant plasmid SalR/pQE-30. The 0.9-kb DNA fragment ligated into an NheI/EcoRI-digested pET28a expression vector. SalR/pET28a expression construct transformed into Escherichia coli BL21(DE3)RIL
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expression in Escherichia coli
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gene salR, DNA and amino acid sequence determination and analysis, expression profile, overexpression in Escherichia coli strain SG13009 as His6-tagged enzyme
gene salR, expression of N-terminally His-tagged enzyme in Escherichia coli, a selenomethionine-substituted SalR is produced by inhibition of the methionine biosynthetic pathway with the same expression vector and Escherichia coli strain used for expression of wild-type SalR
heterologously overexpressed in its active form from Papaver somniferum
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overexpression in Escherichia coli SG13009
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real-time quantitative PCR expression analysis
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salR, DNA and amino acid sequence determination and analysis, overexpression of the His-tagged enzyme in Escherichia coli
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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
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