Information on EC 2.1.1.240 - trans-resveratrol di-O-methyltransferase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.1.1.240
-
RECOMMENDED NAME
GeneOntology No.
trans-resveratrol di-O-methyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2 S-adenosyl-L-methionine + trans-resveratrol = 2 S-adenosyl-L-homocysteine + pterostilbene
show the reaction diagram
S-adenosyl-L-methionine + 3-methoxy-4',5-dihydroxy-trans-stilbene = S-adenosyl-L-homocysteine + pterostilbene
show the reaction diagram
S-adenosyl-L-methionine + trans-resveratrol = S-adenosyl-L-homocysteine + 3-methoxy-4',5-dihydroxy-trans-stilbene
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Stilbenoid, diarylheptanoid and gingerol biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:trans-resveratrol 3,5-O-dimethyltransferase
The enzyme catalyses the biosynthesis of pterostilbene from resveratrol.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
additional information
three-dimensional enzyme homology modeling and docking study for identification of four key catalytic residues. Residues F167 and W258 form a sandwich to bind resveratrol, residue D174 is in close proximity to the substrate, and residue H261 might serve as a general base in the deprotonation of hydroxyl groups
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2 S-adenosyl-L-methionine + resveratrol
2 S-adenosyl-L-homocysteine + pterostilbene
show the reaction diagram
S-adenosyl-L-methionine + 3-methoxy-4',5-dihydroxy-trans-stilbene
S-adenosyl-L-homocysteine + pterostilbene
show the reaction diagram
S-adenosyl-L-methionine + resveratrol
S-adenosyl-L-homocysteine + 3-methoxy-4',5-dihydroxy-trans-stilbene
show the reaction diagram
-
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resveratrol monomethyl ether i.e. 3-methoxy-4',5-dihydroxy-trans-stilbene
-
?
S-adenosyl-L-methionine + trans-resveratrol
S-adenosyl-L-homocysteine + 3-methoxy-4',5-dihydroxy-trans-stilbene
show the reaction diagram
S-adenosyl-L-methionine + trans-resveratrol
S-adenosyl-L-homocysteine + pterostilbene
show the reaction diagram
VrROMTsyn has no or very poor enzyme activity toward resveratrol as a substrate
-
-
?
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2 S-adenosyl-L-methionine + resveratrol
2 S-adenosyl-L-homocysteine + pterostilbene
show the reaction diagram
-
the enzyme catalyses the biosynthesis of pterostilbene from resveratrol
-
-
?
S-adenosyl-L-methionine + 3-methoxy-4',5-dihydroxy-trans-stilbene
S-adenosyl-L-homocysteine + pterostilbene
show the reaction diagram
S-adenosyl-L-methionine + trans-resveratrol
S-adenosyl-L-homocysteine + 3-methoxy-4',5-dihydroxy-trans-stilbene
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
S-adenosyl-L-methionine
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.014
3-methoxy-4',5-dihydroxy-trans-stilbene
-
pH 7.5, temperature not specified in the publication
0.012
resveratrol
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pH 7.5, temperature not specified in the publication
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.086
3-methoxy-4',5-dihydroxy-trans-stilbene
Vitis vinifera
-
pH 7.5, temperature not specified in the publication
0.062
resveratrol
Vitis vinifera
-
pH 7.5, temperature not specified in the publication
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
6.14
3-methoxy-4',5-dihydroxy-trans-stilbene
Vitis vinifera
-
pH 7.5, temperature not specified in the publication
15193
5.16
resveratrol
Vitis vinifera
-
pH 7.5, temperature not specified in the publication
799
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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ROMT is induced in berries upon Botrytis cinerea infection
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
41700
x * 41700, recombinant enzyme, SDS-PAGE
42500
x * 42500, recombinant enzyme, SDS-PAGE
52000
x * 52000, recombinant SUMO-ROMT enzyme, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strain BL21-CodonPlus (DE3)-RIPL by nickel affinity chromatography
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli. Transient coexpression of ROMT and grapevine stilbene synthase in tobacco (Nicotiana benthamiana) using the agroinfiltration technique results in the accumulation of pterostilbene in tobacco tissues
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gene ROMT, recombinant expression in Escherichia coli strain BW27784 and in Saccharomyces cerevisiae, coexpression of two additional genes from the resveratrol biosynthetic pathway, 4-coumarate CoA-ligase and stilbene synthase, leads to production of a large amount of pterostilbene with a trace amount of pinostilbene, subcloning in Escherichia coli strain DH5alpha, recombinant expression of grape SUMO-fusion wild-type and mutant enzymes in Escherichia coli strain BL21 (DE3)
gene sbOMT3, recombinant expression of codon-optimized resveratrol O-methyltransferase genes sbOMT1 and sbOMT3 in Escherichia coli strain C41 (DE3), development of an artificial biosynthetic pathway 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 in Escherichia coli
gene SbROMT3syn, recombinant expression of the His-tagged enzyme in Escherichia coli strain BL21-CodonPlus (DE3)-RIPL, subcloning in Escherichia coli strain DH5alpha
gene VrROMTsyn, recombinant expression of the His-tagged enzyme in Escherichia coli strain BL21-CodonPlus (DE3)-RIPL, subcloning in Escherichia coli strain DH5alpha. Recombinantly expressed enzyme from grape produces very small amounts of methylated resveratrol derivatives in Escherichia coli
recombinant expression of the His-tagged enzyme in Escherichia coli strain BL21-CodonPlus (DE3)-RIPL, coexpression with His-tagged cinnamate/4-coumarate:coenzyme A ligase from Streptomyces coelicolor and Strep-tagged stilbene synthase from Rheum palmatum
recombinant expression of the His-tagged enzyme in Escherichia coli strain BL21-CodonPlus (DE3)-RIPL, coexpression with His-tagged cinnamate/4-coumarate:coenzyme A ligase from Streptomyces coelicolor and Strep-tagged stilbene synthase from Rheum palmatum. Method evaluation and optimization
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
ROMT gene expression in grapevine leaves is induced by different stresses, including downy mildew (Plasmopara viticola) infection, ultraviolet light, and AlCl3 treatment
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ROMT is induced in Plasmopara viticola-infected Marselan leaves and also in berries upon Botrytis cinerea infection
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D174A
site-directed mutagenesis, almost inactive mutant
F167A
site-directed mutagenesis, inactive mutant
H261A
site-directed mutagenesis, inactive mutant
W258A
site-directed mutagenesis, inactive mutant
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
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