Literature summary for 2.1.1.240 extracted from

Wang, Y.; Bhuiya, M.; Zhou, R.; Yu, O.
Pterostilbene production by microorganisms expressing resveratrol O-methyltransferase (2015), Ann. Microbiol., 65, 817-826.

Search for more literature for 2.1.1.240

Application

Application	Comment	Organism
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)

Cloned (Comment)	Organism
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

Cloned (Comment)

Organism

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

Protein Variants	Comment	Organism
D174A	site-directed mutagenesis, almost inactive mutant	Vitis vinifera
F167A	site-directed mutagenesis, inactive mutant	Vitis vinifera
H261A	site-directed mutagenesis, inactive mutant	Vitis vinifera
W258A	site-directed mutagenesis, inactive mutant	Vitis vinifera

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
52000	-	x * 52000, recombinant SUMO-ROMT enzyme, SDS-PAGE	Vitis vinifera

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
S-adenosyl-L-methionine + 3-methoxy-4',5-dihydroxy-trans-stilbene	Vitis vinifera	i.e. pinostilbene	S-adenosyl-L-homocysteine + pterostilbene	-	?
S-adenosyl-L-methionine + trans-resveratrol	Vitis vinifera	-	S-adenosyl-L-homocysteine + 3-methoxy-4',5-dihydroxy-trans-stilbene	-	?

Organism

Organism	UniProt	Comment	Textmining
Vitis vinifera	B6VJS4	gene ROMT	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
S-adenosyl-L-methionine + 3-methoxy-4',5-dihydroxy-trans-stilbene	i.e. pinostilbene	Vitis vinifera	S-adenosyl-L-homocysteine + pterostilbene	-	?
S-adenosyl-L-methionine + trans-resveratrol	-	Vitis vinifera	S-adenosyl-L-homocysteine + 3-methoxy-4',5-dihydroxy-trans-stilbene	-	?

Subunits

Subunits	Comment	Organism
?	x * 52000, recombinant SUMO-ROMT enzyme, SDS-PAGE	Vitis vinifera

Synonyms

Synonyms	Comment	Organism
resveratrol O-methyltransferase	-	Vitis vinifera

Cofactor

Cofactor	Comment	Organism	Structure
S-adenosyl-L-methionine	-	Vitis vinifera

General Information

General Information	Comment	Organism
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