EC 2.1.1.212 - 2,7,4'-trihydroxyisoflavanone 4'-O-methyltransferase

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IntEnz Enzyme Nomenclature
EC 2.1.1.212

Names

Accepted name:
2,7,4'-trihydroxyisoflavanone 4'-O-methyltransferase
Other names:
SAM:2,7,4'-trihydroxyisoflavanone 4'-O-methyltransferase
HI4'OMT
HMM1
MtIOMT5
Systematic name:
S-adenosyl-L-methionine:2,4',7-trihydroxyisoflavanone 4'-O-methyltransferase

Reaction

Comments:

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].

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , DIAGRAM , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0102670
UniProtKB/Swiss-Prot:

References

  1. 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.
    Plant Cell Physiol. 44: 103-112 (2003). [PMID: 12610212]
  2. Deavours, B. E., Liu, C. J., Naoumkina, M. A., Tang, Y., Farag, M. A., Sumner, L. W., Noel, J. P., Dixon, R. A.
    Functional analysis of members of the isoflavone and isoflavanone O-methyltransferase enzyme families from the model legume Medicago truncatula.
    Plant Mol. Biol. 62: 715-733 (2006). [PMID: 17001495]
  3. Liu, C. J., Deavours, B. E., Richard, S. B., Ferrer, J. L., Blount, J. W., Huhman, D., Dixon, R. A., Noel, J. P.
    Structural basis for dual functionality of isoflavonoid O-methyltransferases in the evolution of plant defense responses.
    Plant Cell 18: 3656-3669 (2006). [PMID: 17172354]
  4. Akashi, T., VanEtten, H.D., Sawada, Y., Wasmann, C.C., Uchiyama, H. and Ayabe, S.
    Catalytic specificity of pea O-methyltransferases suggests gene duplication for (+)-pisatin biosynthesis.
    Phytochemistry 67: 2525-2530 (2006).

[EC 2.1.1.212 created 2011]