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

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][4] This enzyme catalyses the following chemical reaction

2,7,4'-Trihydroxyisoflavanone 4'-O-methyltransferase
Identifiers
EC no.2.1.1.212
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Search
PMCarticles
PubMedarticles
NCBIproteins
S-adenosyl-L-methionine + 2,7,4'-trihydroxyisoflavanone S-adenosyl-L-homocysteine + 2,7-dihydroxy-4'-methoxyisoflavanone

This enzyme specifically methylates 2,7,4'-trihydroxyisoflavanone on the 4'-position.

References

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  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. ^ 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. doi:10.1007/s11103-006-9050-x. PMC 2862459. PMID 17001495.
  3. ^ 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. doi:10.1105/tpc.106.041376. PMC 1785397. PMID 17172354.
  4. ^ 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. doi:10.1016/j.phytochem.2006.09.010.
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