2,7,4'-Trihydroxyisoflavanone 4'-O-methyltransferase

2,7,4'-Trihydroxyisoflavanone 4'-O-methyltransferase
Identifiers
EC no.2.1.1.212
Databases
BRENDAenzyme data
ExPASyNiceZyme view
KEGGenzyme entry
MetaCycmetabolic pathway
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2,7,4'-Trihydroxyisoflavanone 4'-O-methyltransferase (EC 2.1.1.212, SAM:2,7,4'-trihydroxyisoflavanone 4'-O-methyltransferase, HI4'OMT, HMM1, MtIOMT5) is an enzyme with systematic name S-adenosyl-L-methionine:2,7,4'-trihydroxyisoflavanone 4'-O-methyltransferase.[1][2][3] This enzyme catalyses the following chemical reaction

2D representation of the chemical structure of Q27123131.
2,4',7-trihydroxyisoflavanone
+ SAM
 
 
 
 
Rightward reaction arrow
 
 
 
2D representation of the chemical structure of Q27132128.
2,7-dihydroxy-4'-methoxyisoflavanone
+ SAH
 

This is a methylation reaction in which the isoflavanone, 2,4',7-trihydroxyisoflavanone, is converted a specific methyl ether, 2,7-dihydroxy-4'-methoxyisoflavanone. The methyl group comes from the cofactor, S-adenosyl methionine (SAM), which becomes S-adenosyl-L-homocysteine (SAH). The enzyme was characterised from the legume, Medicago truncatula.[4]

References

  1. ↑ Akashi T, Sawada Y, Shimada N, Sakurai N, Aoki T, Ayabe S (February 2003). "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 Physiology. 44 (2): 103–12. doi:10.1093/pcp/pcg034. PMID 12610212.
  2. ↑ Liu CJ, Deavours BE, Richard SB, Ferrer JL, Blount JW, Huhman D, Dixon RA, Noel JP (December 2006). "Structural basis for dual functionality of isoflavonoid O-methyltransferases in the evolution of plant defense responses". The Plant Cell. 18 (12): 3656–69. Bibcode:2006PlanC..18.3656L. doi:10.1105/tpc.106.041376. PMC 1785397. PMID 17172354.
  3. ↑ Akashi T, VanEtten HD, Sawada Y, Wasmann CC, Uchiyama H, Ayabe S (December 2006). "Catalytic specificity of pea O-methyltransferases suggests gene duplication for (+)-pisatin biosynthesis". Phytochemistry. 67 (23): 2525–30. Bibcode:2006PChem..67.2525A. doi:10.1016/j.phytochem.2006.09.010. PMID 17067644.
  4. ↑ Deavours BE, Liu CJ, Naoumkina MA, Tang Y, Farag MA, Sumner LW, Noel JP, Dixon RA (November 2006). "Functional analysis of members of the isoflavone and isoflavanone O-methyltransferase enzyme families from the model legume Medicago truncatula". Plant Molecular Biology. 62 (4–5): 715–33. Bibcode:2006PMolB..62..715D. doi:10.1007/s11103-006-9050-x. PMC 2862459. PMID 17001495.