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Literature summary for 2.1.1.240 extracted from
- Metabolic engineering for resveratrol derivative biosynthesis in Escherichia coli (2015), Mol. Cells, 38, 318-326.
Application
| Application | Comment | Organism |
|---|---|---|
| synthesis | the enzyme from Sorghum bicolor, SbROMT3syn, can be used as an enzyme to produce pinostilbene by methylating resveratrol in microorganisms | Sorghum bicolor |
| 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 | Vitis riparia |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| 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 | Sorghum bicolor |
| 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 | Vitis riparia |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | metabolic engineering of stilbene biosynthesis, production of resveratrol and its monomethylated derivative pinostilbene as the major product from 4-coumaric acid in Escherichia coli through coexpression of multiple enzymes (cinnamate/4-coumarate:coenzyme A ligase, stilbene synthase, resveratrol O-methyltransferase) responsible for stilbene biosynthesis. When 4-coumaric acid is fed as the precursor, maximum levels of resveratrol and pinostilbene are produced by recombinant Escherichia coli cells co-expressing Streptomyces coelicolor cinnamate/4-coumarate:coenzyme A ligase ScCCL and Rheum palmatum stilbene synthase RpSTSsyn, or Streptomyces coelicolor ScCCL, RpSTSsyn and Sorghum bicolor resveratrol O-methyltransferase SbROMT3syn, respectively. Method evaluation and optimization | Sorghum bicolor |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | required | Sorghum bicolor |  |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 41700 | - |
x * 41700, recombinant enzyme, SDS-PAGE | Vitis riparia |
| 42500 | - |
x * 42500, recombinant enzyme, SDS-PAGE | 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 | gene SbROMT3 | - |
| Vitis riparia | K7XQ68 | gene VrROMT | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His-tagged enzyme from Escherichia coli strain BL21-CodonPlus (DE3)-RIPL by nickel affinity chromatography | Sorghum bicolor |
| recombinant His-tagged enzyme from Escherichia coli strain BL21-CodonPlus (DE3)-RIPL by nickel affinity chromatography | Vitis riparia |
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 | - |
? | |
| S-adenosyl-L-methionine + trans-resveratrol | VrROMTsyn has no or very poor enzyme activity toward resveratrol as a substrate | Vitis riparia | S-adenosyl-L-homocysteine + pterostilbene | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 41700, recombinant enzyme, SDS-PAGE | Vitis riparia |
| ? | x * 42500, recombinant enzyme, SDS-PAGE | Sorghum bicolor |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| 5-pentadecatrienyl resorcinol O-methyltransferase | UniProt | Sorghum bicolor |
| 5-pentadecatrienyl resorcinol O-methyltransferase | UniProt | Vitis riparia |
| resveratrol O-methyltransferase | - |
Sorghum bicolor |
| resveratrol O-methyltransferase | - |
Vitis riparia |
| SbROMT3syn | - |
Sorghum bicolor |
| VrROMTsyn | - |
Vitis riparia |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | - |
assay at | Sorghum bicolor |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.4 | - |
assay at | Sorghum bicolor |
General Information
| General Information | Comment | Organism |
|---|---|---|
| metabolism | biosynthetic pathway of stilbene compound production from phenylalanine involving the enzyme, overview | Sorghum bicolor |
| metabolism | biosynthetic pathway of stilbene compound production from phenylalanine involving the enzyme, overview | Vitis riparia |
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Release 2023.1 (January 2023)
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