2.1.1.240: trans-resveratrol di-O-methyltransferase
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For detailed information about trans-resveratrol di-O-methyltransferase, go to the full flat file.
Word Map on EC 2.1.1.240
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2.1.1.240
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stilbene
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pterostilbene
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vitis
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vinifera
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grape
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grapevine
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synthesis
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phytoalexins
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pinostilbene
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sorghum
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health-promoting
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bicolor
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piceatannol
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plasmopara
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rhubarb
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o-methylation
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viticola
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nutraceutical
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fungitoxic
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bioproduction
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riparia
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agroinfiltration
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peanut
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mono-methylated
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fungicidal
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berries
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di-methylated
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floral
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biotechnology
- 2.1.1.240
- stilbene
- pterostilbene
-
vitis
- vinifera
- grape
-
grapevine
- synthesis
-
phytoalexins
- pinostilbene
- sorghum
-
health-promoting
- bicolor
- piceatannol
-
plasmopara
- rhubarb
-
o-methylation
- viticola
-
nutraceutical
-
fungitoxic
-
bioproduction
- riparia
-
agroinfiltration
- peanut
-
mono-methylated
-
fungicidal
- berries
-
di-methylated
-
floral
- biotechnology
Reaction
2 S-adenosyl-L-methionine
+
Synonyms
5-pentadecatrienyl resorcinol O-methyltransferase, MT, resveratrol O-methyltransferase, ROMT, SbOMT3, SbROMT3syn, SbROMT3syn protein, VrROMT, VrROMTsyn, VrROMTsyn protein, VvRO
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2.1.1.240 trans-resveratrol di-O-methyltransferaseAdvanced search results
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Application on EC 2.1.1.240 - trans-resveratrol di-O-methyltransferase
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APPLICATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
biotechnology
large-scale production of plant metabolites via microbial approaches is a promising alternative to chemical synthesis and extraction from plant sources Development of an Escherichia coli system containing an artificial biosynthetic pathway, involving the enzyme, that produces methylated resveratrol analogues, such as pinostilbene (3,4'-dihydroxy-5-methoxystilbene), 3,5-dihydroxy-4'-methoxystilbene, 3,4'-dimethoxy-5-hydroxystilbene, and 3,5,4'-trimethoxystilbene, from simple carbon sources
synthesis
synthesis
the enzyme from Sorghum bicolor, SbROMT3syn, can be used as an enzyme to produce pinostilbene by methylating resveratrol in microorganisms
synthesis
the enzyme is useful for conversion of 4-coumaric acid to pterostilbene via co-expression of 4CL::STS and ROMT in recombinant Escherichia coli and Saccharomyces cerevisiae, overview
synthesis
the Vitis riparia enzyme VrROMTsyn cannot be used as an enzyme to produce pinostilbene by methylating resveratrol in microorganisms, since it has no or very poor enzyme activity toward resveratrol as a substrate
synthesis
introduction of enzyme into a resveratrol-producing Corynebacterium glutamicum strain allows synthesis of 42 mg/l (0.16 mM) of the di-O-methylated pterostilbene from p-coumaric acid. A fusion of O-methyltransferase with the maltose-binding protein of Escherichia coli lacking its signal peptide increases the solubility of the O-methyltransferase. Expression of heterologous dioxygenase genes in (2S)-flavanone-producing Corynebacterium glutamicum strains enables the production of flavanonols and flavonols starting from p-coumaric acid and caffeic acid. For the flavonols kaempferol and quercetin, maximum product titers of 23 mg/l (0.08 mM) and 10 mg/l (0.03 mM) can be achieved
synthesis
the enzyme is used for production of large amounts of easily recoverable extracellular resveratrol in a bacterial system, method, overview. Constitutive expression of either Vitis vinifera resveratrol O-methyltransferase (VvROMT) or human cytochrome P450 hydroxylase 1B1 (HsCYP1B1) lead to pterostilbene or piceatannol, respectively, after the engineered cell cultures are treated with elicitors. i.e. methylated cyclodextrins and methyl jasmonate. Functionality of both gene products is first assessed in planta by Nicotiana benthamiana agroinfiltration assays, in which tobacco cells transiently express stilbene synthase and VvROMT or HsCYP1B1
