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Literature summary for 2.1.1.B127 extracted from
- Molecular cloning and functional characterization of an O-methyltransferase catalyzing 4-O-methylation of resveratrol in Acorus calamus (2019), J. Biosci. Bioeng., 127, 539-543 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene AcOMT1, DNA and amino acid sequence determination and analysis, sequence comparison and phylogenetic analysis, semi-quantitative RT-PCR enzyme expression analysis, recombinant expression of N-terminal His9-tagged enzyme in Escherichia coli strain Rosetta 2(DE3) pLysS | Acorus calamus |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.0018 | - |
resveratrol | recombinant enzyme, pH 7.0, 30°C | Acorus calamus |  |
| 0.0042 | - |
isorhapontigenin | recombinant enzyme, pH 7.0, 30°C | Acorus calamus | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| additional information | enzyme AcOMT1 does not show Mg2+ ion requirement unlike plant class I members | Acorus calamus |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 2 S-adenosyl-L-methionine + trans-resveratrol | Acorus calamus | - |
2 S-adenosyl-L-homocysteine + pterostilbene | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Acorus calamus | A0A5A4PXL6 | - |
- |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| leaf | - |
Acorus calamus | - |
| additional information | tissue-specific expression of AcOMT1, expression analysis, AcOMT1 transcripts primarily accumulate in the roots and leaves | Acorus calamus | - |
| rhizome | - |
Acorus calamus | - |
| root | - |
Acorus calamus | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 2 S-adenosyl-L-methionine + trans-resveratrol | - |
Acorus calamus | 2 S-adenosyl-L-homocysteine + pterostilbene | - |
? | |
| additional information | recombinant AcOMT1 shows high 4'-O-methylation activity toward resveratrol and its derivative, isorhapontigenin. The reaction product enzymatically formed from resveratrol by AcOMT1 is determined and confirmed as 4'-O-methylresveratrol. Substrate specificity, overview. Activity of AcOMT1 is the greatest toward isorhapontigenin, followed by resveratrol. Recombinant AcOMT1 exhibits lower activity toward other resveratrol derivatives, piceatannol, oxyresveratrol, and pinostilbene (with 9-24% of the activity observed with resveratrol), and no activity toward pterostilbene or pinosylvin. AcOMT1 shows high 4'-O-methylation activity toward stilbenes with non-methylated phloroglucinol rings. the enzyme shows very low activity with isoeugenol, chavicol, eugenol, 4-coumaric acid, and caffeic acid (below 5% of the activity with resveratrol). Reaction products are analyzed using GC-MS | Acorus calamus | ? | - |
- |
|
| S-adenosyl-L-methionine + cyclohexanol | moderate activity | Acorus calamus | S-adenosyl-L-homocysteine + 4-methoxycyclohexanol | - |
? | |
| S-adenosyl-L-methionine + isorhapontigenin | i.e. 5-[(E)-2-(4-hydroxy-3-methoxyphenyl)ethenyl]benzene-1,3-diol, best substrate | Acorus calamus | S-adenosyl-L-homocysteine + 4'-O-methylisorhapontigenin | - |
? | |
| S-adenosyl-L-methionine + naringenin | moderate activity | Acorus calamus | S-adenosyl-L-homocysteine + 4'-O-methylnaringenin | - |
? | |
| S-adenosyl-L-methionine + oxyresveratrol | i.e. 4-[(E)-2-(3,5-dihydroxyphenyl)ethenyl]benzene-1,3-diol, low activity | Acorus calamus | S-adenosyl-L-homocysteine + 4'-O-methyloxyresveratrol | - |
? | |
| S-adenosyl-L-methionine + piceatannol | i.e. 4-[(E)-2-(3,5-dihydroxyphenyl)ethenyl]benzene-1,2-diol, moderate activity | Acorus calamus | S-adenosyl-L-homocysteine + 4'-O-methylpiceatannol | - |
? | |
| S-adenosyl-L-methionine + pinostilbene | i.e. 3-[(E)-2-(4-hydroxyphenyl)ethenyl]-5-methoxyphenol, low activity | Acorus calamus | S-adenosyl-L-homocysteine + 4'-O-methylpinostilbene | - |
? | |
| S-adenosyl-L-methionine + resveratrol | i.e. 5-[(E)-2-(4-hydroxyphenyl)ethenyl]benzene-1,3-diol, high activity | Acorus calamus | S-adenosyl-L-homocysteine + 4'-O-methylresveratrol | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 38000, recombinant His9-tagged enzyme, SDS-PAGE | Acorus calamus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| AcOMT1 | - |
Acorus calamus |
| resveratrol 4'-O-methyltransferase | - |
Acorus calamus |
| resveratrol-specific OMT | - |
Acorus calamus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | - |
assay at | Acorus calamus |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7 | - |
- |
Acorus calamus |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| S-adenosyl-L-methionine | - |
Acorus calamus | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | AcOMT1 is closely related to plant class II OMTs, which can catalyze the methylation of phenolic compounds independently of divalent cations, and fall into distinct clades to caffeoyl-CoA 3-O-methyltransferase (CCoAOMT) belonging to plant class I OMTs | Acorus calamus |
| physiological function | the enzyme from Acorus calamus acts as an O-methyltransferase catalyzing 4-O-methylation of resveratrol | Acorus calamus |
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