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
- S-adenosyl-L-methionine + 2,7,4'-trihydroxyisoflavanone S-adenosyl-L-homocysteine + 2,7-dihydroxy-4'-methoxyisoflavanone
| 2,7,4'-Trihydroxyisoflavanone 4'-O-methyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.1.1.212 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
This enzyme specifically methylates 2,7,4'-trihydroxyisoflavanone on the 4'-position.
References
- 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.
- 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.
- 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.
- 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.
External links
- 2,7,4'-trihydroxyisoflavanone+4'-O-methyltransferase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
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