CATH Classification

Domain Context

CATH Clusters

Superfamily Vaccinia Virus protein VP39
Functional Family O-methyltransferase ZRP4

Enzyme Information

2.1.1.212
2,7,4'-trihydroxyisoflavanone 4'-O-methyltransferase.
based on mapping to UniProt Q29U70
S-adenosyl-L-methionine + 2,4',7-trihydroxyisoflavanone = S-adenosyl-L- homocysteine + 2,7-dihydroxy-4'-methoxyisoflavanone.
-!- Specifically methylates 2,4',7-trihydroxyisoflavanone on the 4'-position. -!- No activity with isoflavones. -!- The enzyme is involved in formononetin biosynthesis in legumes. -!- The protein from pea (Pisum sativum) also methylates (+)- 6a-hydroxymaackiain at the 3-position (cf. EC 2.1.1.270).
2.1.1.46
Isoflavone 4'-O-methyltransferase.
based on mapping to UniProt Q29U70
S-adenosyl-L-methionine + a 4'-hydroxyisoflavone = S-adenosyl-L- homocysteine + a 4'-methoxyisoflavone.
-!- The enzyme catalyzes the methylation of daidzein and genistein. -!- It does not methylate naringenin, apigenin, luteolin or kaempferol.

UniProtKB Entries (1)

Q29U70
I4OMT_MEDTR
Medicago truncatula
Isoflavone 4'-O-methyltransferase

PDB Structure

PDB 1ZGJ
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
Structural basis for dual functionality of isoflavonoid O-methyltransferases in the evolution of plant defense responses.
Liu, C.J., Deavours, B.E., Richard, S.B., Ferrer, J.L., Blount, J.W., Huhman, D., Dixon, R.A., Noel, J.P.
Plant Cell