2,7,4'-Trihidroksiizoflavanon 4'-O-metiltransferaza

(Preusmjereno sa stranice HI4'OMT)

2,7,4'-Trihidroksiizoflavanon 4'-O-metiltransferaza (EC 2.1.1.212, SAM:2,7,4'-trihidroksiizoflavanonska 4'-O-metiltransferaza, HI4'OMT, HMM1, MtIOMT5) je enzim sa sistematskim imenom S-adenozil-L-metionin:2,7,4'-trihidroksiizoflavanon 4'-O-metiltransferaza.[1][2][3][4] Ovaj enzim katalizuje sledeću hemijsku reakciju

2,7,4'-Trihidroksiizoflavanon 4'-O-metiltransferaza
Identifikatori
EC broj 2.1.1.212
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB RCSB PDB PDBe PDBj PDBsum
S-adenozil-L-metionin + 2,7,4'-trihidroksiizoflavanon S-adenozil-L-homocistein + 2,7-dihidroksi-4'-metoksiizoflavanon

Ovaj enzim specifično metiluje 2,7,4'-trihidroksiizoflavanon u 4'-poziciji. On ne deluje na izoflavone. Enzim učestvuje u biosintezi formononetina .

Reference

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  1. Akashi, T., Sawada, Y., Shimada, N., Sakurai, N., Aoki, T. and 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. PMID 12610212. 
  2. Deavours, B.E., Liu, C.J., Naoumkina, M.A., Tang, Y., Farag, M.A., Sumner, L.W., Noel, J.P. and 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. PMID 17001495. 
  3. Liu, C.J., Deavours, B.E., Richard, S.B., Ferrer, J.L., Blount, J.W., Huhman, D., Dixon, R.A. and 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. PMID 17172354. 
  4. Akashi, T., VanEtten, H.D., Sawada, Y., Wasmann, C.C., Uchiyama, H. and Ayabe, S. (2006). „Catalytic specificity of pea O-methyltransferases suggests gene duplication for (+)-pisatin biosynthesis”. Phytochemistry 67: 2525-2530. 

Literatura

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Spoljašnje veze

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