In enzymology, a kaempferol 4'-O-methyltransferase (EC 2.1.1.155) is an enzyme that catalyzes the chemical reaction
| Kaempferol 4'-O-methyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.1.1.155 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
- S-adenosyl-L-methionine + kaempferol S-adenosyl-L-homocysteine + kaempferide
Thus, the two substrates of this enzyme are S-adenosyl methionine and kaempferol, whereas its two products are S-adenosylhomocysteine and kaempferide.
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:kaempferol 4'-O-methyltransferase. Other names in common use include S-adenosyl-L-methionine:flavonoid 4'-O-methyltransferase, and F 4'-OMT.
References
edit- Curir P, Lanzotti V, Dolci M, Dolci P, Pasini C, Tollin G (2003). "Purification and properties of a new S-adenosyl-L-methionine:flavonoid 4'-O-methyltransferase from carnation (Dianthus caryophyllus L.)". Eur. J. Biochem. 270 (16): 3422–31. doi:10.1046/j.1432-1033.2003.03729.x. PMID 12899699.
