Literature summary extracted from
Wang, Y.; Bhuiya, M.; Zhou, R.; Yu, O.
Pterostilbene production by microorganisms expressing resveratrol O-methyltransferase (2015), Ann. Microbiol., 65, 817-826.
Application
EC Number |
Application |
Comment |
Organism |
---|
2.1.1.240 |
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 |
Vitis vinifera |
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
2.1.1.240 |
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) |
Vitis vinifera |
Protein Variants
EC Number |
Protein Variants |
Comment |
Organism |
---|
2.1.1.240 |
D174A |
site-directed mutagenesis, almost inactive mutant |
Vitis vinifera |
2.1.1.240 |
F167A |
site-directed mutagenesis, inactive mutant |
Vitis vinifera |
2.1.1.240 |
H261A |
site-directed mutagenesis, inactive mutant |
Vitis vinifera |
2.1.1.240 |
W258A |
site-directed mutagenesis, inactive mutant |
Vitis vinifera |
Molecular Weight [Da]
EC Number |
Molecular Weight [Da] |
Molecular Weight Maximum [Da] |
Comment |
Organism |
---|
2.1.1.240 |
52000 |
- |
x * 52000, recombinant SUMO-ROMT enzyme, SDS-PAGE |
Vitis vinifera |
Natural Substrates/ Products (Substrates)
EC Number |
Natural Substrates |
Organism |
Comment (Nat. Sub.) |
Natural Products |
Comment (Nat. Pro.) |
Rev. |
Reac. |
---|
2.1.1.240 |
S-adenosyl-L-methionine + 3-methoxy-4',5-dihydroxy-trans-stilbene |
Vitis vinifera |
i.e. pinostilbene |
S-adenosyl-L-homocysteine + pterostilbene |
- |
? |
|
2.1.1.240 |
S-adenosyl-L-methionine + trans-resveratrol |
Vitis vinifera |
- |
S-adenosyl-L-homocysteine + 3-methoxy-4',5-dihydroxy-trans-stilbene |
- |
? |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
2.1.1.240 |
Vitis vinifera |
B6VJS4 |
gene ROMT |
- |
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
2.1.1.240 |
S-adenosyl-L-methionine + 3-methoxy-4',5-dihydroxy-trans-stilbene |
i.e. pinostilbene |
Vitis vinifera |
S-adenosyl-L-homocysteine + pterostilbene |
- |
? |
|
2.1.1.240 |
S-adenosyl-L-methionine + trans-resveratrol |
- |
Vitis vinifera |
S-adenosyl-L-homocysteine + 3-methoxy-4',5-dihydroxy-trans-stilbene |
- |
? |
|
Subunits
EC Number |
Subunits |
Comment |
Organism |
---|
2.1.1.240 |
? |
x * 52000, recombinant SUMO-ROMT enzyme, SDS-PAGE |
Vitis vinifera |
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
2.1.1.240 |
resveratrol O-methyltransferase |
- |
Vitis vinifera |
Cofactor
EC Number |
Cofactor |
Comment |
Organism |
Structure |
---|
2.1.1.240 |
S-adenosyl-L-methionine |
- |
Vitis vinifera |
|
General Information
EC Number |
General Information |
Comment |
Organism |
---|
2.1.1.240 |
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 |
Vitis vinifera |