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

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Short description: Class of enzymes
2,7,4'-Trihydroxyisoflavanone 4'-O-methyltransferase
Identifiers
EC number2.1.1.212
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum

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 [math]\displaystyle{ \rightleftharpoons }[/math] S-adenosyl-L-homocysteine + 2,7-dihydroxy-4'-methoxyisoflavanone

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

References

  1. "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. February 2003. doi:10.1093/pcp/pcg034. PMID 12610212. 
  2. "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. November 2006. doi:10.1007/s11103-006-9050-x. PMID 17001495. 
  3. "Structural basis for dual functionality of isoflavonoid O-methyltransferases in the evolution of plant defense responses". The Plant Cell 18 (12): 3656–69. December 2006. doi:10.1105/tpc.106.041376. PMID 17172354. 
  4. "Catalytic specificity of pea O-methyltransferases suggests gene duplication for (+)-pisatin biosynthesis". Phytochemistry 67 (23): 2525–30. December 2006. doi:10.1016/j.phytochem.2006.09.010. 

External links