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

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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
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PMCarticles
PubMedarticles
NCBIproteins

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

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

  1. ^ Akashi, T.; Sawada, Y.; Shimada, N.; Sakurai, N.; Aoki, T.; Ayabe, S. (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 Physiol. 44: 103–112. doi:10.1093/pcp/pcg034. 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. (2006). "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. doi:10.1007/s11103-006-9050-x. 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. (2006). "Structural basis for dual functionality of isoflavonoid O-methyltransferases in the evolution of plant defense responses". Plant Cell. 18: 3656–3669. doi:10.1105/tpc.106.041376. PMID 17172354.
  4. ^ Akashi, T.; VanEtten, H.D.; Sawada, Y.; Wasmann, C.C.; Uchiyama, H.; Ayabe, S. (2006). "Catalytic specificity of pea O-methyltransferases suggests gene duplication for (+)-pisatin biosynthesis". Phytochemistry. 67: 2525–2530. doi:10.1016/j.phytochem.2006.09.010.