Biology:Quercetin 3-O-methyltransferase

From HandWiki
quercetin 3-O-methyltransferase
Identifiers
EC number2.1.1.76
CAS number75603-21-3
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO

In enzymology, a quercetin 3-O-methyltransferase (EC 2.1.1.76) is an enzyme that catalyzes the chemical reaction

S-adenosyl-L-methionine + 3,5,7,3',4'-pentahydroxyflavone [math]\displaystyle{ \rightleftharpoons }[/math] S-adenosyl-L-homocysteine + 3-methoxy-5,7,3',4'-tetrahydroxyflavone

Thus, the two substrates of this enzyme are S-adenosyl methionine and 3,5,7,3',4'-pentahydroxyflavone, whereas its two products are S-adenosylhomocysteine and 3-methoxy-5,7,3',4'-tetrahydroxyflavone.

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:3,5,7,3',4'-pentahydroxyflavone 3-O-methyltransferase. Other names in common use include flavonol 3-O-methyltransferase, and flavonoid 3-methyltransferase. This enzyme participates in flavonoid biosynthesis.

References

  • "A proteomic analysis of arsenical drug resistance in Trypanosoma brucei". Proteomics 6 (9): 2726–32. 2006. doi:10.1002/pmic.200500419. PMID 16526094. 
  • "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. 
  • Ibrahim RK; De Luca V (1982). "Polymethylated flavonol synthesis is catalyzed by distinct O-methyltransferases". Naturwissenschaften 69 (1): 41–42. doi:10.1007/BF00441101.