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

\rightleftharpoons

S-adenosyl-L-homocysteine + 2,7-dihydroxy-4'-methoxyisoflavanone

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. (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.
↑ 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.
↑ 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.
↑ 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.

External links

2,7,4'-trihydroxyisoflavanone 4'-O-methyltransferase at the US National Library of Medicine Medical Subject Headings (MeSH)

Transferase: one carbon transferases (EC 2.1)

2.1.1: Methyl-

N-	Histamine N-methyltransferase Phenylethanolamine N-methyltransferase Amine N-methyltransferase Phosphatidylethanolamine N-methyltransferase

O-	5-hydroxyindole-O-methyltransferase/Acetylserotonin O-methyltransferase Catechol-O-methyl transferase

Homocysteine	Betaine-homocysteine methyltransferase Homocysteine methyltransferase Methionine synthase

Other	Phosphatidyl ethanolamine methyltransferase DNMT3B Histone methyltransferase Thymidylate synthase DNA methyltransferase Thiopurine methyltransferase

2.1.2: Hydroxymethyl-,
Formyl- and Related

Hydroxymethyltransferase	Serine hydroxymethyltransferase 3-methyl-2-oxobutanoate hydroxymethyltransferase

Formyltransferase	Phosphoribosylglycinamide formyltransferase Inosine monophosphate synthase

Other	Glutamate formimidoyltransferase Aminomethyltransferase

2.1.3: Carboxy-
and Carbamoyl

Carboxy	methylmalonyl-CoA carboxytransferase

Carbamoyl	Aspartate carbamoyltransferase Ornithine carbamoyltransferase Oxamate carbamoyltransferase Putrescine carbamoyltransferase 3-hydroxymethylcephem carbamoyltransferase Lysine carbamoyltransferase N-acetylornithine carbamoyltransferase

2.1.4: Amidine

Arginine:glycine amidinotransferase

Enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list)

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