Biology:3,7-dimethylquercetin 4'-O-methyltransferase
| 3,7-dimethylquercitin 4'-O-methyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 2.1.1.83 | ||||||||
| CAS number | 96477-60-0 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
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In enzymology, a 3,7-dimethylquercetin 4'-O-methyltransferase (EC 2.1.1.83) is an enzyme that catalyzes the chemical reaction
- S-adenosyl-L-methionine + 5,3',4'-trihydroxy-3,7-dimethoxyflavone [math]\displaystyle{ \rightleftharpoons }[/math] S-adenosyl-L-homocysteine + 5,3'-dihydroxy-3,7,4'-trimethoxyflavone
Thus, the two substrates of this enzyme are S-adenosyl methionine and 5,3',4'-trihydroxy-3,7-dimethoxyflavone (rhamnazin), whereas its two products are S-adenosylhomocysteine and 5,3'-dihydroxy-3,7,4'-trimethoxyflavone (ayanin).
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:5,3',4'-trihydroxy-3,7-dimethoxyflavone 4'-O-methyltransferase. Other names in common use include flavonol 4'-O-methyltransferase, flavonol 4'-methyltransferase, 4'-OMT, S-adenosyl-L-methionine:3',4',5-trihydroxy-3,7-dimethoxyflavone, 4'-O-methyltransferase, and 3,7-dimethylquercitin 4'-O-methyltransferase [mis-spelt].
References
- "Enzymatic synthesis of polymethylated flavonols in Chrysosplenium americanum. I. Partial purification and some properties of S-adenosyl-L-methionine:flavonol 3-, 6-, 7-, and 4'-O-methyltransferases". Arch. Biochem. Biophys. 238 (2): 596–605. 1985. doi:10.1016/0003-9861(85)90205-X. PMID 3994393.
- "Enzymatic synthesis of polymethylated flavonols in Chrysosplenium americanum. II. Substrate interaction and product inhibition studies of flavonol 3-, 6-, and 4'-O-methyltransferases". Arch. Biochem. Biophys. 238 (2): 606–18. 1985. doi:10.1016/0003-9861(85)90206-1. PMID 3994394.
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