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Literature summary for 2.1.1.240 extracted from

  • Kang, S.Y.; Lee, J.K.; Choi, O.; Kim, C.Y.; Jang, J.H.; Hwang, B.Y.; Hong, Y.S.
    Biosynthesis of methylated resveratrol analogs through the construction of an artificial biosynthetic pathway in E. coli (2014), BMC Biotechnol., 14, 67.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.1.1.240

Application

Application Comment Organism
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 Sorghum bicolor

Cloned(Commentary)

Cloned (Comment) Organism
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 Sorghum bicolor

Protein Variants

Protein Variants Comment Organism
additional information development of an Escherichia coli system containing 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. The artificial biosynthetic pathways contain a series of codon-optimized O-methyltransferase genes from sorghum in addition to the resveratrol biosynthetic genes Sorghum bicolor

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 Sorghum bicolor i.e. pinostilbene S-adenosyl-L-homocysteine + pterostilbene
-
 ?
S-adenosyl-L-methionine + trans-resveratrol Sorghum bicolor
-
 S-adenosyl-L-homocysteine + 3-methoxy-4',5-dihydroxy-trans-stilbene
-
 ?

Organism

Organism UniProt Comment Textmining
Sorghum bicolor A8QW53
-
-

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 Sorghum bicolor S-adenosyl-L-homocysteine + pterostilbene
-
 ?
S-adenosyl-L-methionine + trans-resveratrol
-
 Sorghum bicolor S-adenosyl-L-homocysteine + 3-methoxy-4',5-dihydroxy-trans-stilbene
-
 ?

Subunits

Subunits Comment Organism
dimer
-
 Sorghum bicolor

Synonyms

Synonyms Comment Organism
5-pentadecatrienyl resorcinol O-methyltransferase UniProt Sorghum bicolor
resveratrol O-methyltransferase
-
 Sorghum bicolor
SbOMT3
-
 Sorghum bicolor

Cofactor

Cofactor Comment Organism Structure
S-adenosyl-L-methionine
-
 Sorghum bicolor

General Information

General Information Comment Organism
metabolism two resveratrol O-methyltransferase genes (sbOMT1 and sbOMT3) from Sorghum bicolor are capable of using resveratrol as a substrate that yields methylated analogues of resveratrol. The sbOMT3 O-methyltransferase catalyzes the A-ring specific 3,5-bis-O-methylation of resveratrol, which in turn yields pterostilbene (3,5-dimethoxy-4'-hydroxystilbene) in coexpression with a stilbene synthase from Arachis hypogaea. In addition, resveratrol O-methyltransferase sbOMT1, which has a potential as eugenol O-methyltransferase, predominantly catalyzes the resveratrol B-ring (4'-O-methylation), which yields 3,5-dihydroxy-4'-methoxystilbene Sorghum bicolor