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Information on EC 2.1.1.46 - isoflavone 4'-O-methyltransferase
for references in articles please use BRENDA:EC2.1.1.46
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EC Tree 2 Transferases
2.1 Transferring one-carbon groups
2.1.1 Methyltransferases
2.1.1.46 isoflavone 4'-O-methyltransferase
IUBMB Comments
Requires Mg2+ for activity. The enzyme catalyses the methylation of daidzein and genistein. It does not methylate naringenin, apigenin, luteolin or kaempferol.
The enzyme appears in viruses and cellular organisms
Reaction Schemes
showSynonyms
isoflavone-specific 4'-o-methyltransferase, 2,7,4'-trihydroxyisoflavanone 4'-o-methyltransferase/isoflavone 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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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + a 4'-hydroxyisoflavone = S-adenosyl-L-homocysteine + a 4'-methoxyisoflavone
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-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
formononetin biosynthesis, isoflavonoid biosynthesis II
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:4'-hydroxyisoflavone 4'-O-methyltransferase
Requires Mg2+ for activity. The enzyme catalyses the methylation of daidzein and genistein. It does not methylate naringenin, apigenin, luteolin or kaempferol.
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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 + 5,7,4'trihydroxyisoflavone
S-adenosyl-L-homocysteine + 5,7-dihydroxy-4'-O-methylisoflavone
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + 7,4'-dihydroxyisoflavone
S-adenosyl-L-homocysteine + 7-hydroxy-4'-methoxylisoflavone
-
Substrates: i.e. daidzein. The reaction follows an ordered BiBi mechanism with S-adenosylmethionine and S-adenosylhomocysteine as leading reaction partners
Products: -
Products: -
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S-adenosyl-L-methionine + 7,4'-dihydroxyisoflavone
S-adenosyl-L-homocysteine + 7-hydroxy-4'-O-methylisoflavone
S-adenosyl-L-methionine + a 4'-hydroxyisoflavone
S-adenosyl-L-homocysteine + a 4'-methoxyisoflavone
-
Substrates: -
Products: -
Products: -
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S-adenosyl-L-methionine + isoformononetin
S-adenosyl-L-homocysteine + 4',7-dimethoxyisoflavone
Substrates: 5.2% activity compared to genistein
Products: -
Products: -
?
S-adenosyl-L-methionine + prunetin
S-adenosyl-L-homocysteine + 4',7-dimethoxy-5-hydroxyisoflavone
Substrates: 6.2% activity compared to genistein
Products: -
Products: -
?
S-adenosyl-L-methionine + 7,4'-dihydroxyisoflavone
S-adenosyl-L-homocysteine + 7-hydroxy-4'-O-methylisoflavone
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Substrates: i.e. daidzein. Methylation is the last step in the biosynthesis of 4Ā-methoxyisoflavones
Products: -
Products: -
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S-adenosyl-L-methionine + 7,4'-dihydroxyisoflavone
S-adenosyl-L-homocysteine + 7-hydroxy-4'-O-methylisoflavone
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Substrates: i.e. daidzein. Methylation is the last step in the biosynthesis of 4'-methoxyisoflavones
Products: -
Products: -
?
S-adenosyl-L-methionine + daidzein
S-adenosyl-L-homocysteine + formononetin
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + daidzein
S-adenosyl-L-homocysteine + formononetin
Substrates: 48.8% activity compared to genistein
Products: -
Products: -
?
S-adenosyl-L-methionine + genistein
S-adenosyl-L-homocysteine + biochanin A
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + genistein
S-adenosyl-L-homocysteine + biochanin A
Substrates: 100% activity
Products: -
Products: -
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additional information
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Substrates: no methylation of: p-hydroxycinnamic acid, p-hydroxybenzoic acid, 3,4-dihydroxycinnamic acid, naringenin, (5,7,4'-trihydroxyflavanone), apigenin (5,7,4'-trihydroxyflavone), luteolin (5,7,3',4'-tetrahydroxyflavone), kaempferol (3,5,7,4'-tetrahydroxyflavone), wedelolactone (5,3',4'-trihydroxy-7-methoxycoumestone)
Products: -
Products: -
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additional information
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Substrates: the bifunctionally enzyme also catalyzes the formation of a 2,7-dihydroxy-4'-methoxyisoflavanone from a 2,4',7-trihydroxyisoflavanone (reaction of EC 2.1.1.212)
Products: -
Products: -
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additional information
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Substrates: the enzyme is not able to methylate 2,7,4'-trihydroxyisoflavanone, biochanin A, formononetin, apigenin, luteolin, liquirtitigenin, kaempferol, quercetin, isoliquiritigenin, and caffeic acid
Products: -
Products: -
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additional information
?
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Substrates: the enzyme is not able to methylate 2,7,4'-trihydroxyisoflavanone, biochanin A, formononetin, apigenin, luteolin, liquirtitigenin, kaempferol, quercetin, isoliquiritigenin, and caffeic acid
Products: -
Products: -
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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 + 7,4'-dihydroxyisoflavone
S-adenosyl-L-homocysteine + 7-hydroxy-4'-O-methylisoflavone
S-adenosyl-L-methionine + a 4'-hydroxyisoflavone
S-adenosyl-L-homocysteine + a 4'-methoxyisoflavone
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + daidzein
S-adenosyl-L-homocysteine + formononetin
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + genistein
S-adenosyl-L-homocysteine + biochanin A
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + 7,4'-dihydroxyisoflavone
S-adenosyl-L-homocysteine + 7-hydroxy-4'-O-methylisoflavone
-
Substrates: i.e. daidzein. Methylation is the last step in the biosynthesis of 4Ā-methoxyisoflavones
Products: -
Products: -
?
S-adenosyl-L-methionine + 7,4'-dihydroxyisoflavone
S-adenosyl-L-homocysteine + 7-hydroxy-4'-O-methylisoflavone
-
Substrates: i.e. daidzein. Methylation is the last step in the biosynthesis of 4'-methoxyisoflavones
Products: -
Products: -
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.03
S-adenosyl-L-homocysteine
-
pH 8.8, 30Ā°C, versus S-adenosyl-L-methionine
0.3
S-adenosyl-L-homocysteine
-
pH 8.8, 30Ā°C, versus 7,4'-dihydroxyisoflavone
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5 - 10
-
pH 7.5: about 40% of maximal activity (Tris-HCl buffer), pH 10.0: about 25% of maximal activity (glycine-NaOH buffer)
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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
-
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
metabolism
-
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). M3OM1_PEA
360
0
40351
Swiss-Prot
other Location (Reliability: 2)
I4OMT_GLYEC
367
0
40895
Swiss-Prot
other Location (Reliability: 3)
I4OMT_LOTJA
365
0
40690
Swiss-Prot
other Location (Reliability: 2)
I4OMT_MEDTR
364
0
40754
Swiss-Prot
other Location (Reliability: 3)
K9K000_ONOVI
361
0
40433
TrEMBL
Mitochondrion (Reliability: 5)
A0A072UNK8_MEDTR
364
0
40754
TrEMBL
other Location (Reliability: 3)
A0A251V0M9_HELAN
359
0
40498
TrEMBL
other Location (Reliability: 2)
A0A396I467_MEDTR
44
0
5173
TrEMBL
other Location (Reliability: 2)
A0A396I1S6_MEDTR
107
0
12520
TrEMBL
other Location (Reliability: 2)
A0A1L1Z441_PUEML
353
0
39901
TrEMBL
other Location (Reliability: 4)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enzyme expression is increased about 3fold in the presence of methyl jasmonate
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wengenmayer, H.; Ebel, J.; Grisebach, H.
Purification and properties of a S-adenosylmethionine: isoflavone 4-O-methyltransferase from cell suspension cultures of Cicer arietinum L
Eur. J. Biochem.
50
135-143
1974
Cicer arietinum
brenda
Li, J.; Li, C.; Gou, J.; Wang, X.; Fan, R.; Zhang, Y.
An alternative pathway for formononetin biosynthesis in Pueraria lobata
Front. Plant Sci.
7
861
2016
Pueraria montana var. lobata (A0A1L1Z441), Pueraria montana var. lobata
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
EXTERNAL LINKS (specific for EC-Number 2.1.1.46)
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Release 2023.1 (January 2023)
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