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Information on EC 2.1.1.154 - isoliquiritigenin 2'-O-methyltransferase
for references in articles please use BRENDA:EC2.1.1.154
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EC Tree 2 Transferases
2.1 Transferring one-carbon groups
2.1.1 Methyltransferases
2.1.1.154 isoliquiritigenin 2'-O-methyltransferase
IUBMB Comments
Not identical to EC 2.1.1.65, licodione 2′-O-methyltransferase . While EC 2.1.1.154, isoliquiritigenin 2′-O-methyltransferase can use licodione as a substrate, EC 2.1.1.65 cannot use isoliquiritigenin as a substrate.
The expected taxonomic range for this enzyme is: Medicago
Reaction Schemes
showSynonyms
chalcone omt, s-adenosyl-l-methionine:isoliquiritigenin 2'-o-methyltransferase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
chalcone-O-methyltransferase
chalcone-O-methyltransferase 1
ChOMT1
ChOMT3
MtOMT1
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + isoliquiritigenin = S-adenosyl-L-homocysteine + 2'-O-methylisoliquiritigenin
S-adenosyl-L-methionine + isoliquiritigenin = S-adenosyl-L-homocysteine + 2'-O-methylisoliquiritigenin
sequential Bi Bi mechanism
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S-adenosyl-L-methionine + isoliquiritigenin = S-adenosyl-L-homocysteine + 2'-O-methylisoliquiritigenin
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:isoliquiritigenin 2'-O-methyltransferase
Not identical to EC 2.1.1.65, licodione 2'-O-methyltransferase [2]. While EC 2.1.1.154, isoliquiritigenin 2'-O-methyltransferase can use licodione as a substrate, EC 2.1.1.65 cannot use isoliquiritigenin as a substrate.
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CAS REGISTRY NUMBER
COMMENTARY
139317-14-9
-
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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'-dihydroxy-4-methoxychalcone
S-adenosyl-L-homocysteine + 4'-hydroxy-2',4-dimethoxychalcone
-
Substrates: 77% of the activity with isoliquiritigenin
Products: -
Products: -
?
S-adenosyl-L-methionine + 4',7-dihydroxyflavanone
S-adenosyl-L-homocysteine + ?
-
Substrates: 32% of the activity with isoliquiritigenin
Products: -
Products: -
?
S-adenosyl-L-methionine + isoliquiritigenin
S-adenosyl-L-homocysteine + 2'-O-methylisoliquiritigenin
S-adenosyl-L-methionine + isoliquiritigenin
S-adenosyl-L-homocysteine + 2'-O-methylisoliquiritigenin
-
Substrates: the product of the reaction, 2'-O-methylisoliquiritigenin, is the most potent inducer of nodulation genes of Rhizobium meliloti, the symbiont of Medicago sativa which forms nitrogen-fixing nodules
Products: -
Products: -
?
S-adenosyl-L-methionine + isoliquiritigenin
S-adenosyl-L-homocysteine + 2'-O-methylisoliquiritigenin
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + isoliquiritigenin
S-adenosyl-L-homocysteine + 2'-O-methylisoliquiritigenin
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + isoliquiritigenin
S-adenosyl-L-homocysteine + 2'-O-methylisoliquiritigenin
Medicago truncatula R108
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme specifically involved in the biosynthesis of an inducer of Rhizobium meliloti nodulation genes
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity towards naringenin chalcone, caffeic acid or daidzein
Products: -
Products: -
?
additional information
?
-
-
Substrates: isozymes chalcone-OMT 1 (ChOMT1) and ChOMT3, but not OMT2, 4, and 5 in Medicago truncatula are able to produce 4,4'-dihydroxy-2'-methoxychalcone (DHMC)
Products: -
Products: -
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additional information
?
-
Medicago truncatula R108
-
Substrates: isozymes chalcone-OMT 1 (ChOMT1) and ChOMT3, but not OMT2, 4, and 5 in Medicago truncatula are able to produce 4,4'-dihydroxy-2'-methoxychalcone (DHMC)
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 + isoliquiritigenin
S-adenosyl-L-homocysteine + 2'-O-methylisoliquiritigenin
additional information
?
-
-
Substrates: the enzyme specifically involved in the biosynthesis of an inducer of Rhizobium meliloti nodulation genes
Products: -
Products: -
?
S-adenosyl-L-methionine + isoliquiritigenin
S-adenosyl-L-homocysteine + 2'-O-methylisoliquiritigenin
-
Substrates: the product of the reaction, 2'-O-methylisoliquiritigenin, is the most potent inducer of nodulation genes of Rhizobium meliloti, the symbiont of Medicago sativa which forms nitrogen-fixing nodules
Products: -
Products: -
?
S-adenosyl-L-methionine + isoliquiritigenin
S-adenosyl-L-homocysteine + 2'-O-methylisoliquiritigenin
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + isoliquiritigenin
S-adenosyl-L-homocysteine + 2'-O-methylisoliquiritigenin
Medicago truncatula R108
-
Substrates: -
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
S-adenosyl-L-homocysteine
-
competitive with respect to S-adenosyl-L-methionine
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
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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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
rapid and transient increase in extractable activities after treatment with yeast extract
brenda
-
enzyme activity increases during early stages of seedling development and is predomonantly located in the root
brenda
-
ChOMT1 is specifically expressed in infected root hairs
brenda
-
enzyme activity increases during early stages of seedling development and is predomonantly located in the root
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
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
malfunction
physiological function
additional information
physiological function
-
2'-O-methylisoliquiritigenin strongly induces the nod gene in Medicago truncatula. ChOMT1 is important for nod gene activation in the rhizosphere, and ChOMT1 and 3 promote nodulation
physiological function
Medicago truncatula R108
-
2'-O-methylisoliquiritigenin strongly induces the nod gene in Medicago truncatula. ChOMT1 is important for nod gene activation in the rhizosphere, and ChOMT1 and 3 promote nodulation
-
additional information
-
methylation of isoliquiritigenin by MsChOMT involves the catalytic residues His278, Glu306 and Glu337. Three key substrate binding residues, Met189, Met329 and Thr332, which ensure the A-ring 2'-hydroxy is firmly positioned for deprotonation and methylation, are conserved
additional information
Medicago truncatula R108
-
methylation of isoliquiritigenin by MsChOMT involves the catalytic residues His278, Glu306 and Glu337. Three key substrate binding residues, Met189, Met329 and Thr332, which ensure the A-ring 2'-hydroxy is firmly positioned for deprotonation and methylation, are conserved
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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.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
identification of the homozygous mutant lines NF10582 (chomt1-1, insertion at position 395), NF12032 (chomt1-2, insertion at position 95 bp), and NF16030 (chomt1-3, insertion at position 43 bp). Mutant roots have reduced nod gene-inducing flavonoids in their rhizospheres
additional information
Medicago truncatula R108
-
identification of the homozygous mutant lines NF10582 (chomt1-1, insertion at position 395), NF12032 (chomt1-2, insertion at position 95 bp), and NF16030 (chomt1-3, insertion at position 43 bp). Mutant roots have reduced nod gene-inducing flavonoids in their rhizospheres
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene MtOMT1, quantitative real-time PCR enzyme epression analysis, recombinant expression of His-tagged enzyme in Escherichia coli, recombinant expression in nodulated Medicago truncatula roots using Agrobacterium rhizogenes hairy root transformation
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gene MtOMT3, quantitative real-time PCR enzyme epression analysis, recombinant expression of His-tagged enzyme in Escherichia coli, recombinant expression in nodulated Medicago truncatula roots using Agrobacterium rhizogenes hairy root transformation
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
isoflavone reductase, isoliquiritigenin 2'-O-methyltransferase, chalcone reductase, and chalcone isomerase are upregulated by salt stress under 100 mM in the seedling root
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ichimura, M.; Furuno, T.; Takahashi, T.; Dixon, R.A.; Ayabe, S.
Enzymic O-methylation of isoliquiritigenin and licodione in alfalfa and licorice cultures
Phytochemistry
44
991-995
1997
Medicago sativa, no activity in Glycyrrhiza echinata
brenda
Maxwell, C.A.; Edwards, R.; Dixon, R.A.
Identification, purification, and characterization of S-adenosyl-L-methionine: isoliquiritigenin 2'-O-methyltransferase from alfalfa (Medicago sativa L.)
Arch. Biochem. Biophys.
293
158-166
1992
Medicago sativa
brenda
Maxwell, C.A.; Harrison, M.J.; Dixon, R.A.
Molecular characterization and expression of alfalfa isoliquiritigenin 2'-O-methyltransferase, an enzyme specifically involved in the biosynthesis of an inducer of Rhizobium meliloti nodulation genes
Plant J.
4
971-981
1993
Medicago sativa
brenda
Xiong, J.; Sun, Y.; Yang, Q.; Tian, H.; Zhang, H.; Liu, Y.; Chen, M.
Proteomic analysis of early salt stress responsive proteins in alfalfa roots and shoots
Proteome Sci.
15
19
2017
Medicago sativa (P93324)
brenda
Wu, W.; Zhuang, Y.; Chen, D.; Ruan, Y.; Li, F.; Jackson, K.; Liu, C.W.; East, A.; Wen, J.; Tatsis, E.; Poole, P.S.; Xu, P.; Murray, J.D.
Methylated chalcones are required for rhizobial nod gene induction in the Medicago truncatula rhizosphere
New Phytol.
242
2195-2206
2024
Medicago truncatula, Medicago truncatula R108
brenda
EXTERNAL LINKS (specific for EC-Number 2.1.1.154)
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