Izoflavon 7-O-metiltransferaza

Izoflavon 7-O-metiltransferaza
Identifikatori
EC broj2.1.1.150
CAS broj136111-54-1
Baze podataka
IntEnzIntEnz pregled
BRENDABRENDA pristup
ExPASyNiceZyme pregled
KEGGKEGG pristup
MetaCycmetabolički put
PRIAMprofil
Strukture PBPRCSB PDB PDBe PDBj PDBsum

Izoflavon 7-O-metiltransferaza (EC 2.1.1.150) je enzim sa sistematskim imenom S-adenozil-L-metionin:hidroksiizoflavon 7-O-metiltransferaza.[1][2][3][4][5][6] Ovaj enzim katalizuje sledeću hemijsku reakciju

S-adenozil-L-metionin + 7-hidroksiizoflavon S-adenozil-L-homocistein + 7-metoksiizoflavon

Enzim iz lucerke može da metiliše daidzein, genistein i 6,7,4'-trihidroksiizoflavon. On nije aktivan na flavonima i flavanonima.

Reference

  1. ^ Edwards, R. & Dixon, R.A. (1991). „Isoflavone O-methyltransferase activities in elicitor-treated cell suspension cultures of Medicago sativa”. Phytochemistry. 30: 2597—2606. 
  2. ^ He, X.Z. & Dixon, R.A. (2000). „Genetic manipulation of isoflavone 7-O-methyltransferase enhances biosynthesis of 4′-O-methylated isoflavonoid phytoalexins and disease resistance in alfalfa”. Plant Cell. 12: 1689—1702. PMID 11006341. 
  3. ^ He, X.-Z. & Dixon, R.A. (1996). „Affinity chromatography, substrate/product specificity, and amino acid sequence analysis of an isoflavone O-methyltransferase from alfalfa (Medicago sativa L.)”. Arch. Biochem. Biophys. 336: 121—129. PMID 8951042. 
  4. ^ He, X.Z., Reddy, J.T. and Dixon, R.A. (1998). „Stress responses in alfalfa (Medicago sativa L). XXII. cDNA cloning and characterization of an elicitor-inducible isoflavone 7-O-methyltransferase”. Plant Mol. Biol. 36: 43—54. PMID 9484461. 
  5. ^ Liu, C.-J. & Dixon, R.A. (2001). „Elicitor-induced association of isoflavone O-methyltransferase with endomembranes prevents the formation and 7-O-methylation of daidzein during isoflavonoid phytoalexin biosynthesis”. Plant Cell. 13: 2643—2658. PMID 11752378. 
  6. ^ Zubieta, C., He, X.-Z., Dixon, R.A. and Noel, J.P. (2001). „Structures of two natural product methyltransferases reveal the basis for substrate specificity in plant O-methyltransferases”. Nat. Struct. Biol. 8: 271—279. PMID 11224575. 

Literatura

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