Entry
Name
2,7,4'-trihydroxyisoflavanone 4'-O-methyltransferase;
SAM:2,7,4'-trihydroxyisoflavanone 4'-O-methyltransferase;
HI4'OMT;
HMM1;
MtIOMT5;
S-adenosyl-L-methionine:2,7,4'-trihydroxyisoflavanone 4'-O-methyltransferase
Class
Transferases;
Transferring one-carbon groups;
Methyltransferases
BRITE hierarchy
Sysname
S-adenosyl-L-methionine:2,4',7-trihydroxyisoflavanone 4'-O-methyltransferase
Reaction(IUBMB)
S-adenosyl-L-methionine + 2,4',7-trihydroxyisoflavanone = S-adenosyl-L-homocysteine + 2,7-dihydroxy-4'-methoxyisoflavanone [RN:
R07722 ]
Reaction(KEGG)
Substrate
S-adenosyl-L-methionine [CPD:
C00019 ];
2,4',7-trihydroxyisoflavanone [CPD:
C15567 ]
Product
S-adenosyl-L-homocysteine [CPD:
C00021 ];
2,7-dihydroxy-4'-methoxyisoflavanone [CPD:
C16190 ]
Comment
Specifically methylates 2,4',7-trihydroxyisoflavanone on the 4'-position. No activity with isoflavones [2]. The enzyme is involved in formononetin biosynthesis in legumes [1]. The protein from pea (Pisum sativum) also methylates (+)-6a-hydroxymaackiain at the 3-position (cf. EC
2.1.1.270 , (+)-6a-hydroxymaackiain 3-O-methyltransferase) [4].
History
EC 2.1.1.212 created 2011
Pathway
Orthology
K13259 2,7,4'-trihydroxyisoflavanone 4'-O-methyltransferase / isoflavone 4'-O-methyltransferase
Genes
GMX : 100807589(IOMT1) 106795493(IOMT2)
TPRA : 123881701 123913950 123913951
CAM : 101494507 101494823 101495151
» show all
Taxonomy
Reference
Authors
Akashi T, Sawada Y, Shimada N, Sakurai N, Aoki T, Ayabe S
Title
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.
Journal
Sequence
Reference
Authors
Deavours BE, Liu CJ, Naoumkina MA, Tang Y, Farag MA, Sumner LW, Noel JP, Dixon RA
Title
Functional analysis of members of the isoflavone and isoflavanone O-methyltransferase enzyme families from the model legume Medicago truncatula.
Journal
Reference
Authors
Liu CJ, Deavours BE, Richard SB, Ferrer JL, Blount JW, Huhman D, Dixon RA, Noel JP
Title
Structural basis for dual functionality of isoflavonoid O-methyltransferases in the evolution of plant defense responses.
Journal
Sequence
Reference
Authors
Akashi T, VanEtten HD, Sawada Y, Wasmann CC, Uchiyama H, Ayabe S
Title
Catalytic specificity of pea O-methyltransferases suggests gene duplication for (+)-pisatin biosynthesis.
Journal
Sequence
Other DBs
ExPASy - ENZYME nomenclature database: 2.1.1.212
LinkDB
All DBs