Transferring one-carbon groups;
S-adenosyl-L-methionine + 2,4',7-trihydroxyisoflavanone = S-adenosyl-L-homocysteine + 2,7-dihydroxy-4'-methoxyisoflavanone [RN:
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
, (+)-6a-hydroxymaackiain 3-O-methyltransferase) .
EC 18.104.22.168 created 2011
K13259 2,7,4'-trihydroxyisoflavanone 4'-O-methyltransferase / isoflavone 4'-O-methyltransferase
GMX: 100807589(IOMT1) 106795493(IOMT2)
MTR: MTR_4g088190 MTR_4g088200
CAM: 101494507 101494823 101495151
LJA: Lj4g3v0484930.1(Lj4g3v0484930.1) Lj4g3v0485870.1(Lj4g3v0485870.1) » show all
Akashi T, Sawada Y, Shimada N, Sakurai N, Aoki T, Ayabe S
cDNA cloning and biochemical characterization of S-adenosyl-L-methionine: 2,7,4'-trihydroxyisoflavanone 4'-O-methyltransferase, a critical enzyme of the legume isoflavonoid phytoalexin pathway.
Deavours BE, Liu CJ, Naoumkina MA, Tang Y, Farag MA, Sumner LW, Noel JP, Dixon RA
Functional analysis of members of the isoflavone and isoflavanone O-methyltransferase enzyme families from the model legume Medicago truncatula.
Liu CJ, Deavours BE, Richard SB, Ferrer JL, Blount JW, Huhman D, Dixon RA, Noel JP
Structural basis for dual functionality of isoflavonoid O-methyltransferases in the evolution of plant defense responses.
Akashi T, VanEtten HD, Sawada Y, Wasmann CC, Uchiyama H, Ayabe S
Catalytic specificity of pea O-methyltransferases suggests gene duplication for (+)-pisatin biosynthesis.
ExPASy - ENZYME nomenclature database: 22.214.171.124