KEGG   ENZYME: 2.1.1.212Help
Entry
EC 2.1.1.212                Enzyme                                 

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)
R07722;
(other) R02931 R06564
Show
Substrate
S-adenosyl-L-methionine [CPD:C00019];
2,4',7-trihydroxyisoflavanone
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
Isoflavonoid biosynthesis
Biosynthesis of secondary metabolites
Orthology
K13259  
2,7,4'-trihydroxyisoflavanone 4'-O-methyltransferase / isoflavone 4'-O-methyltransferase
Reference
1  [PMID:12610212]
  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
Plant. Cell. Physiol. 44 (2003) 103-12.
  Organism
Glycyrrhiza echinata, Lotus japonicus
  Sequence
Reference
2  [PMID:17001495]
  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
Plant. Mol. Biol. 62 (2006) 715-33.
Reference
3  [PMID:17172354]
  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
Plant. Cell. 18 (2006) 3656-69.
  Organism
Medicago truncatula
  Sequence
[up:Q29U70]
Reference
4  [PMID:17067644]
  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
Phytochemistry. 67 (2006) 2525-30.
  Organism
Glycyrrhiza echinata
  Sequence
[up:Q84KK6]
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 

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