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Information on EC 2.1.1.212 - 2,7,4'-trihydroxyisoflavanone 4'-O-methyltransferase
for references in articles please use BRENDA:EC2.1.1.212
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EC Tree 2 Transferases
2.1 Transferring one-carbon groups
2.1.1 Methyltransferases
2.1.1.212 2,7,4'-trihydroxyisoflavanone 4'-O-methyltransferase
IUBMB Comments
Specifically methylates 2,4′,7-trihydroxyisoflavanone on the 4′-position. No activity with isoflavones . The enzyme is involved in formononetin biosynthesis in legumes . The protein from pea (Pisum sativum) also methylates (+)-6a-hydroxymaackiain at the 3-position (cf. EC 2.1.1.270, (+)-6a-hydroxymaackiain 3-O-methyltransferase) .
The enzyme appears in viruses and cellular organisms
Reaction Schemes
showSynonyms
2-hydroxyisoflavanone 4'-o-methyltransferase, sam 2,7,4'-trihydroxyisoflavanone 4'-o-methyltransferase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2,7,4'-trihydroxyisoflavanone 4'-O-methyltransferase/isoflavone 4'-O-methyltransferase
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HI4'OMT
S-adenosyl-L-methionine: 2-hydroxyisoflavanone 4'-O-methyltransferase
S-adenosyl-L-methionine: 2-hydroxyisoflavanone 4'-O-methyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + 2,4',7-trihydroxyisoflavanone = S-adenosyl-L-homocysteine + 2,7-dihydroxy-4'-methoxyisoflavanone
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
formononetin biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:2,7,4'-trihydroxyisoflavanone 4'-O-methyltransferase
Specifically methylates 2,4',7-trihydroxyisoflavanone on the 4'-position. No activity with isoflavones [2]. The enzyme is involved in formononetin biosynthesis in legumes [1]. The protein from pea (Pisum sativum) also methylates (+)-6a-hydroxymaackiain at the 3-position (cf. EC 2.1.1.270, (+)-6a-hydroxymaackiain 3-O-methyltransferase) [4].
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + 2,4',7-trihydroxyisoflavanone
S-adenosyl-L-homocysteine + 2,7-dihydroxy-4'-methoxyisoflavanone
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Substrates: -
Products: -
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S-adenosyl-L-methionine + 2,7,4'-trihydroxyisoflavanone
S-adenosyl-L-homocysteine + 2,7-dihydroxy-4'-methoxyisoflavanone
S-adenosyl-L-methionine + 2,7,4'-trihydroxyisoflavanone
S-adenosyl-L-homocysteine + 2,7-dihydroxy-4'-methoxyisoflavanone
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Substrates: -
Products: -
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S-adenosyl-L-methionine + 2,7,4'-trihydroxyisoflavanone
S-adenosyl-L-homocysteine + 2,7-dihydroxy-4'-methoxyisoflavanone
Substrates: the enzyme is involved in formononetin biosynthesis in legumes
Products: -
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S-adenosyl-L-methionine + 2,7,4'-trihydroxyisoflavanone
S-adenosyl-L-homocysteine + 2,7-dihydroxy-4'-methoxyisoflavanone
Substrates: -
Products: -
Products: -
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S-adenosyl-L-methionine + 2,7,4'-trihydroxyisoflavanone
S-adenosyl-L-homocysteine + 2,7-dihydroxy-4'-methoxyisoflavanone
Substrates: the enzyme is involved in formononetin biosynthesis
Products: -
Products: -
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S-adenosyl-L-methionine + 2,7,4'-trihydroxyisoflavanone
S-adenosyl-L-homocysteine + 2,7-dihydroxy-4'-methoxyisoflavanone
Substrates: -
Products: -
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S-adenosyl-L-methionine + 2,7,4'-trihydroxyisoflavanone
S-adenosyl-L-homocysteine + 2,7-dihydroxy-4'-methoxyisoflavanone
Substrates: HI4'OMT shows efficiencies (relative Vmax/Km) for the 4'-O-methylation of 2,7,4'-trihydroxyisoflavanone 20 times higher than for the 3-O-methylation of (+)-6a-hydroxymaackiain, respectively
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S-adenosyl-L-methionine + 2,7,4'-trihydroxyisoflavanone
S-adenosyl-L-homocysteine + 2,7-dihydroxy-4'-methoxyisoflavanone
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + 2,7,4'-trihydroxyisoflavanone
S-adenosyl-L-homocysteine + 2,7-dihydroxy-4'-methoxyisoflavanone
Substrates: the enzyme is involved in formononetin biosynthesis
Products: -
Products: -
?
S-adenosyl-L-methionine + 2,7,4'-trihydroxyisoflavanone
S-adenosyl-L-homocysteine + 2,7-dihydroxy-4'-methoxyisoflavanone
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + 2,7,4'-trihydroxyisoflavanone
S-adenosyl-L-homocysteine + 2,7-dihydroxy-4'-methoxyisoflavanone
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Substrates: in pea, HMM1 is the equivalent of the HI4'OMT found in other legumes and is involved in formononetin biosynthesis
Products: -
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S-adenosyl-L-methionine + 2,7,4'-trihydroxyisoflavanone
S-adenosyl-L-homocysteine + 2,7-dihydroxy-4'-methoxyisoflavanone
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Substrates: -
Products: -
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S-adenosyl-L-methionine + 2,7,4'-trihydroxyisoflavanone
S-adenosyl-L-homocysteine + 2,7-dihydroxy-4'-methoxyisoflavanone
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Substrates: HMM1 shows efficiencies (relative Vmax/Km) for the 4'-O-methylation of 2,7,4'-trihydroxyisoflavanone 4 times higher than for the 3-O-methylation of (+)-6a-hydroxymaackiain
Products: -
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S-adenosyl-L-methionine + 2,7,4'-trihydroxyisoflavanone
S-adenosyl-L-homocysteine + 2,7-dihydroxy-4'-methoxyisoflavanone
Substrates: the enzyme is involved in formononetin biosynthesis in legumes
Products: -
Products: -
?
S-adenosyl-L-methionine + 2,7,4'-trihydroxyisoflavanone
S-adenosyl-L-homocysteine + 2,7-dihydroxy-4'-methoxyisoflavanone
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + 2,7,4'-trihydroxyisoflavanone
S-adenosyl-L-homocysteine + 2,7-dihydroxy-4'-methoxyisoflavanone
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + 2,7,4'-trihydroxyisoflavanone
S-adenosyl-L-homocysteine + 2,7-dihydroxy-4'-methoxyisoflavanone
Substrates: the bifunctional enzyme also catalyzes the 3-O-methylation of (+)-6a-hydroxymaackiain, with slightly lower catalytic efficiency
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additional information
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Substrates: no activity with daidzein
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additional information
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Substrates: no activity with daidzein
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additional information
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Substrates: the bifunctionally enzyme typically converts daidzein to formononetin or genistein to biochanin A (reaction of EC 2.1.1.46)
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additional information
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Substrates: low activity with dihydrodaidzein. 4'-Methoxy, 7-methoxy, and 4',7-dimethoxy products are formed in the reaction with dihydrodaidzein. No activity with: 6,7,4'-trihydroxyisoflavone, 6,7'-dihydroxy,4'-methoxyisoflavone, 7,3',4'-trihydroxyisoflavone, daidzein, genistein, glycitein, coumestrol, apigenin, 7,4'-dihydroxyflavone and myricetin
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + 2,4',7-trihydroxyisoflavanone
S-adenosyl-L-homocysteine + 2,7-dihydroxy-4'-methoxyisoflavanone
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Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + 2,7,4'-trihydroxyisoflavanone
S-adenosyl-L-homocysteine + 2,7-dihydroxy-4'-methoxyisoflavanone
S-adenosyl-L-methionine + 2,7,4'-trihydroxyisoflavanone
S-adenosyl-L-homocysteine + 2,7-dihydroxy-4'-methoxyisoflavanone
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + 2,7,4'-trihydroxyisoflavanone
S-adenosyl-L-homocysteine + 2,7-dihydroxy-4'-methoxyisoflavanone
Substrates: the enzyme is involved in formononetin biosynthesis in legumes
Products: -
Products: -
?
S-adenosyl-L-methionine + 2,7,4'-trihydroxyisoflavanone
S-adenosyl-L-homocysteine + 2,7-dihydroxy-4'-methoxyisoflavanone
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + 2,7,4'-trihydroxyisoflavanone
S-adenosyl-L-homocysteine + 2,7-dihydroxy-4'-methoxyisoflavanone
Substrates: the enzyme is involved in formononetin biosynthesis
Products: -
Products: -
?
S-adenosyl-L-methionine + 2,7,4'-trihydroxyisoflavanone
S-adenosyl-L-homocysteine + 2,7-dihydroxy-4'-methoxyisoflavanone
Substrates: the enzyme is involved in formononetin biosynthesis
Products: -
Products: -
?
S-adenosyl-L-methionine + 2,7,4'-trihydroxyisoflavanone
S-adenosyl-L-homocysteine + 2,7-dihydroxy-4'-methoxyisoflavanone
-
Substrates: in pea, HMM1 is the equivalent of the HI4'OMT found in other legumes and is involved in formononetin biosynthesis
Products: -
Products: -
?
S-adenosyl-L-methionine + 2,7,4'-trihydroxyisoflavanone
S-adenosyl-L-homocysteine + 2,7-dihydroxy-4'-methoxyisoflavanone
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + 2,7,4'-trihydroxyisoflavanone
S-adenosyl-L-homocysteine + 2,7-dihydroxy-4'-methoxyisoflavanone
Substrates: the enzyme is involved in formononetin biosynthesis in legumes
Products: -
Products: -
?
S-adenosyl-L-methionine + 2,7,4'-trihydroxyisoflavanone
S-adenosyl-L-homocysteine + 2,7-dihydroxy-4'-methoxyisoflavanone
Substrates: -
Products: -
Products: -
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
var. mongholicus, from Inner Mongolia Seeds Administration Station Inner Mongolia, China, and further cultivated in pots
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-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
Pongamia pinnata seeds contain a significantly higher content of the flavonoid formononetin compared to soybean seeds, by over 2000fold, and lower content of substrate daidzein
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
evolution
-
a synteny block among Cicer arietinum chromosome 6 (inverted), Glycyrrhiza uralensis scaffold 00721 and Medicago truncatula chromosome 4, which includes genes involved in isoflavonoid biosynthesis (7-IOMT, CYP93C and HI4OMT), overview
evolution
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in Pongamia pinnata, five genes encoding 2,7,4'-trihydroxyisoflavanone 4'-O-methyltransferases are found, which expanded through tandem duplication
metabolism
-
2,7-dihydroxy-4'-O-methoxy-isoflavanone is converted to formononetin, calycosin and calycosin-7-O-beta-D-glucoside via a series of reactions in the calycosin-7-O-beta-D-glucoside pathway. The 2,7,4'-trihydroxyisoflavanone is probably more easily caught by 2-hydroxyisoflavanone 4'-O-methyltransferase and hence provides more precursors for formononetin than being converted to daidzein, overview
metabolism
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the enzyme is involved in the isoflavonoid biosynthesis together with 2-hydroxyisoflavanone synthase (CYP93C) and isoflavone-7-O-methyltransferase (7-IOMT), forming a cluster on the scaffold of the liquorice genome. The second gene in the cluster encodes the enzyme 2,7,4'-trihydroxyisoflavanone 4'-O-methyltransferase/isoflavone 4'-O-methyltransferase, i.e. HI4OMT (ECs 2.1.1.212 and 2.1.1.46), which typically converts daidzein to formononetin or genistein to biochanin A
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystallized from a polyethylene glycol precipitant containing 2.5 mM of the reaction product S-adenosyl-L-homocysteine, 2.5 A resolution
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Akashi, T.; Sawada, Y.; Shimada, N.; Sakurai, N.; Aoki, T.; Ayabe, S.
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
2003
Glycyrrhiza echinata (Q84KK6), Glycyrrhiza echinata, Lotus japonicus (Q84KK4), Lotus japonicus
brenda
Akashi, T.; VanEtten, H.D.; Sawada, Y.; Wasmann, C.C.; Uchiyama, H.; Ayabe, S.
Catalytic specificity of pea O-methyltransferases suggests gene duplication for (+)-pisatin biosynthesis
Phytochemistry
67
2525-2530
2006
Glycyrrhiza echinata (Q84KK6), Lathyrus oleraceus
brenda
Deavours, B.E.; Liu, C.J.; Naoumkina, M.A.; Tang, Y.; Farag, M.A.; Sumner, L.W.; Noel, J.P.; Dixon, R.A.
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
2006
Medicago truncatula (Q29U70)
brenda
Kaimoyo, E.; VanEtten, H.
Inactivation of pea genes by RNAi supports the involvement of two similar O-methyltransferases in the biosynthesis of (+)-pisatin and of chiral intermediates with a configuration opposite that found in (+)-pisatin
Phytochemistry
69
76-87
2008
Lathyrus oleraceus
brenda
Akashi, T.; Sawada, Y.; Aoki, T.; Ayabe, S.
New scheme of the biosynthesis of formononetin involving 2,7,4'-trihydroxyisoflavanone but not daidzein as the methyl acceptor
Biosci. Biotechnol. Biochem.
64
2276-2279
2000
Glycyrrhiza echinata (Q84KK6), Glycyrrhiza echinata AK-1 (Q84KK6)
brenda
Liu, C.J.; Deavours, B.E.; Richard, S.B.; Ferrer, J.L.
Blount, J.W.; Huhman, D.; Dixon, R.A.; Noel, J.P.: Structural basis for dual functionality of isoflavonoid O-methyltransferases in the evolution of plant defense responses
Plant Cell
18
3656-3669
2006
Medicago truncatula (Q29U70)
brenda
Xu, R.Y.; Nan, P.; Yang, Y.; Pan, H.; Zhou, T.; Chen, J.
Ultraviolet irradiation induces accumulation of isoflavonoids and transcription of genes of enzymes involved in the calycosin-7-O-?-d-glucoside pathway in Astragalus membranaceus Bge. var. mongholicus (Bge.) Hsiao
Physiol. Plant.
142
265-273
2011
Astragalus membranaceus
brenda
Mochida, K.; Sakurai, T.; Seki, H.; Yoshida, T.; Takahagi, K.; Sawai, S.; Uchiyama, H.; Muranaka, T.; Saito, K.
Draft genome assembly and annotation of Glycyrrhiza uralensis, a medicinal legume
Plant J.
89
181-194
2017
Glycyrrhiza uralensis
brenda
Liu, C.; Huang, R.; Zhao, X.; Xu, R.; Zhang, J.; Li, X.; Liu, G.; Dong, R.; Liu, P.
Comparative analysis of lipid and flavonoid biosynthesis between Pongamia and soybean seeds genomic, transcriptional, and metabolic perspectives
Biotechnol. Biofuels Bioprod.
17
86
2024
Pongamia pinnata
brenda
EXTERNAL LINKS (specific for EC-Number 2.1.1.212)
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