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Information on EC 1.14.14.90 - isoflavone 2'-hydroxylase
for references in articles please use BRENDA:EC1.14.14.90
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EC Tree 1 Oxidoreductases
1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
1.14.14 With reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen into the other donor
1.14.14.90 isoflavone 2'-hydroxylase
IUBMB Comments
A cytochrome P-450 (heme-thiolate) protein. Acts on daidzein, formononetin and genistein. EC 1.14.14.89, 4′-methoxyisoflavone 2′-hydroxylase, has the same reaction but is more specific as it requires a 4′-methoxyisoflavone.
The enzyme appears in viruses and cellular organisms
- 1.14.14.90
-
isoflavonoids
-
phytoalexins
- glycyrrhiza
- flavonoid
- echinata
- genistein
-
cinnamic
-
4-hydroxylase
-
phenylpropanoids
- chickpea
- medicarpin
-
cicer
- elicitor
-
legume
- licorice
-
2'-hydroxylated
- arietinum
Reaction Schemes
showSynonyms
isoflavone 2'-hydroxylase, ami2'h, cyp81e1, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CYP Ge-3
CYP81E1
EC 1.14.13.89
-
-
formerly
-
I2'H
isoflavone 2'-monooxygenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
an isoflavone + [reduced NADPH-hemoprotein reductase] + O2 = a 2'-hydroxyisoflavone + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
(-)-glycinol biosynthesis, coumestrol biosynthesis, wighteone and luteone biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
isoflavone,[reduced NADPH-hemoprotein reductase]:oxygen oxidoreductase (2'-hydroxylating)
A cytochrome P-450 (heme-thiolate) protein. Acts on daidzein, formononetin and genistein. EC 1.14.14.89, 4'-methoxyisoflavone 2'-hydroxylase, has the same reaction but is more specific as it requires a 4'-methoxyisoflavone.
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CAS REGISTRY NUMBER
COMMENTARY
110183-49-8
-
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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
3'-hydroxyformononetin + [reduced NADPH-hemoprotein reductase] + O2
2',3'-dihydroxyformononetin + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: 4.7% of the activity with biochanin A
Products: -
Products: -
?
biochanin A + [reduced NADPH-hemoprotein reductase] + O2
2'-hydroxybiochanin A + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: -
Products: -
Products: -
?
daidzein + [reduced NADPH-hemoprotein reductase] + O2
2'-hydroxydaidzein + [oxidized NADPH-hemoprotein reductase] + H2O
formononetin + [reduced NADPH-hemoprotein reductase] + O2
2'-hydroxyformononetin + [oxidized NADPH-hemoprotein reductase] + H2O
genistein + [reduced NADPH-hemoprotein reductase] + O2
2'-hydroxygenistein + [oxidized NADPH-hemoprotein reductase] + H2O
daidzein + [reduced NADPH-hemoprotein reductase] + O2
2'-hydroxydaidzein + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: -
Products: -
Products: -
?
daidzein + [reduced NADPH-hemoprotein reductase] + O2
2'-hydroxydaidzein + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: -
Products: -
Products: -
?
daidzein + [reduced NADPH-hemoprotein reductase] + O2
2'-hydroxydaidzein + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: -
Products: -
Products: -
?
daidzein + [reduced NADPH-hemoprotein reductase] + O2
2'-hydroxydaidzein + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: 18.6% of the activity with biochanin A
Products: + low concentrations of 3'-hydroxydaidzein
Products: + low concentrations of 3'-hydroxydaidzein
?
formononetin + [reduced NADPH-hemoprotein reductase] + O2
2'-hydroxyformononetin + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: -
Products: -
Products: -
?
formononetin + [reduced NADPH-hemoprotein reductase] + O2
2'-hydroxyformononetin + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: -
Products: -
Products: -
?
formononetin + [reduced NADPH-hemoprotein reductase] + O2
2'-hydroxyformononetin + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: 37.2% of the activity with biochanin A
Products: -
Products: -
?
genistein + [reduced NADPH-hemoprotein reductase] + O2
2'-hydroxygenistein + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: -
Products: -
Products: -
?
genistein + [reduced NADPH-hemoprotein reductase] + O2
2'-hydroxygenistein + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: -
Products: -
Products: -
?
genistein + [reduced NADPH-hemoprotein reductase] + O2
2'-hydroxygenistein + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: -
Products: -
Products: -
?
genistein + [reduced NADPH-hemoprotein reductase] + O2
2'-hydroxygenistein + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: 10.2% of the activity with biochanin A
Products: + low concentrations of 3'-hydroxygenistaien
Products: + low concentrations of 3'-hydroxygenistaien
?
additional information
?
-
-
Substrates: no activity with formononetin, cf. EC 1.14.13.53, 4'-methoxyisoflavone 2'-hydroxylase
Products: -
Products: -
?
additional information
?
-
Substrates: no activity with formononetin, cf. EC 1.14.13.53, 4'-methoxyisoflavone 2'-hydroxylase
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme is involved in the biosynthesis of isoflavonoid-derived antimicrobial compounds of legumes
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme is involved in biosynthesis of flavonoids
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is involved in biosynthesis of flavonoids
Products: -
Products: -
?
additional information
?
-
Substrates: no activity with naringenin (5,7,4'-trihydroxyflavanone), liquiritigenin (7,4'-dihydroxyflavanone), trans-cinnamic acid and 4-coumaric acid
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme is involved in biosynthesis of flavonoids
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme is involved in the biosynthesis of isoflavonoid-derived antimicrobial compounds of legumes
Products: -
Products: -
?
additional information
?
-
Substrates: no activity with naringenin (5,7,4'-trihydroxyflavanone), liquiritigenin (7,4'-dihydroxyflavanone), trans-cinnamic acid and 4-coumaric acid
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is essential for isoflavan pterocarpan phytoalexin biosynthesis
Products: -
Products: -
?
additional information
?
-
Substrates: no activity with isoformononetin, prunetin, 6,7,4'-trihydroxyisoflavone, 3',4',7-trihydroxyisoflavone
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with isoformononetin, prunetin, 6,7,4'-trihydroxyisoflavone, 3',4',7-trihydroxyisoflavone
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
daidzein + [reduced NADPH-hemoprotein reductase] + O2
2'-hydroxydaidzein + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: -
Products: -
Products: -
?
genistein + [reduced NADPH-hemoprotein reductase] + O2
2'-hydroxygenistein + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: -
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme is involved in the biosynthesis of isoflavonoid-derived antimicrobial compounds of legumes
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme is involved in biosynthesis of flavonoids
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is involved in biosynthesis of flavonoids
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme is involved in biosynthesis of flavonoids
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme is involved in the biosynthesis of isoflavonoid-derived antimicrobial compounds of legumes
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is essential for isoflavan pterocarpan phytoalexin biosynthesis
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADPH-hemoprotein reductase
A flavoprotein containing both FMN and FAD. This enzyme catalyses the transfer of electrons from NADPH, an obligatory two-electron donor, to microsomal P-450 monooxygenases, EC 1.14.14._
-
NADPH-hemoprotein reductase
A flavoprotein containing both FMN and FAD. This enzyme catalyses the transfer of electrons from NADPH, an obligatory two-electron donor, to microsomal P-450 monooxygenases, EC 1.14.14._
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
protein CPR
is an essential redox partner for functional expression of CYP
-
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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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pH OPTIMUM
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
-
activity increases 10 h after elicitation with reduced glutathione. Only a low level of transcription is observed in untreated seedlings
brenda
additional information
suspension, induction with yeast extract
brenda
-
suspension, induction with yeast extract
-
brenda
additional information
AmI2'H is expressed throughout the entire plant
brenda
additional information
-
AmI2'H is expressed throughout the entire plant
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
metabolism
the enzyme is involved in isoflavonoid biosynthesis
physiological function
the enzyme promotes the accumulation of medicarpin malonyl glucoside
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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.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
modification of the gene sequence to facilitate protein expression and increase protein solubility, removal of the N-terminal membrane binding motif to enhance protein solubility
additional information
-
modification of the gene sequence to facilitate protein expression and increase protein solubility, removal of the N-terminal membrane binding motif to enhance protein solubility
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant truncated enzyme, lacking the N-terminal membrane binding motif, from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
dual plasmid method development for functional expression of plant CYPs in Escherichia coli, method and culture conditions optimization, overview. Gene CYP81E11, DNA and amino acid sequence determination and analysis, recombinant expression of the transmembrane-domain truncated CYP enzyme in Escherichia coli strain C41(DE3) and coexpression with CPR from Lotus japonicus as a discrete polypeptide. The optimal temperature is 25°C, addition of the heme precursor 5-aminolevulinic acid is essential for functional expression of CYP81E11
dual plasmid method development for functional expression of plant CYPs in Escherichia coli, method and culture conditions optimiztaion, overview. Gene CYP81E12, DNA and amino acid sequence determination and analysis, recombinant expression of the transmembrane-domain truncated CYP enzyme in Escherichia coli strain C41(DE3) and coexpression with CPR from Lotus japonicus as a discrete polypeptide. The optimal temperature is 25°C, addition of the heme precursor 5-aminolevulinic acid is essential for functional expression of CYP81E12
dual plasmid method development for functional expression of plant CYPs in Escherichia coli, method and culture conditions optimiztaion, overview. Gene CYP81E13, DNA and amino acid sequence determination and analysis, recombinant expression of the transmembrane-domain truncated CYP enzyme in Escherichia coli strain C41(DE3) and coexpression with CPR from Lotus japonicus as a discrete polypeptide. The optimal temperature is 25°C, addition of the heme precursor 5-aminolevulinic acid is essential for functional expression of CYP81E13
gene AmI2'H or CYP81E42, DNA and amino acid sequence determination and analysis, recombinant expression of truncated enzyme, lacking the N-terminal membrane binding motif, in Escherichia coli strain BL21(DE3). Expression of the enzyme without removal of the transmembrane domain or insertion of the hydrophilic peptide AKKTSSKGKL is unsuccessful
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the gene is upregulated during infection by Candidatus Leiberibacter asiaticus
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Akashi, T.; Aoki, T.; Ayabe, S.I.
CYP81E1, a cytochrome P450 cDNA of licorice (Glycyrrhiza echinata L.), encodes isoflavone 2'-hydroxylase
Biochem. Biophys. Res. Commun.
251
67-70
1998
Glycyrrhiza echinata (P93147), Glycyrrhiza echinata L. (P93147)
brenda
Shimada, N.; Akashi, T.; Aoki, T.; Ayabe, S.i.
Induction of isoflavonoid pathway in the model legume Lotus japonicus: molecular characterization of enzymes involved in phytoalexin biosynthesis
Plant Sci.
160
37-47
2000
Lotus japonicus
brenda
Nakamura, K.; Akashi, T.; Aoki, T.; Kawaguchi, K.; Ayabe, S.
Induction of isoflavonoid and retrochalcone branches of the flavonoid pathway in cultured Glycyrrhiza echinata cells treated with yeast extract
Biosci. Biotechnol. Biochem.
63
1618-1620
1999
Glycyrrhiza echinata (P93147), Glycyrrhiza echinata, Glycyrrhiza echinata AK-1 (P93147)
brenda
Liu, C.J.; Huhman, D.; Sumner, L.W.; Dixon, R.A.
Regiospecific hydroxylation of isoflavones by cytochrome p450 81E enzymes from Medicago truncatula
Plant J.
36
471-484
2003
Medicago truncatula (Q6WNR0), Medicago truncatula
brenda
Gholampour, H.; Ghayeb Zamharir, M.; Karimi, J.; Farrokhi, N.; Alizadeh, A.; Taheri, P.
Identification of genes expressed differentially in grapefruit infected with Candidatus liberibacter asiaticus in the late stage of disease
J. Phytopathol.
162
811-819
2014
Citrus x paradisi
-
brenda
Uchida, K.; Akashi, T.; Aoki, T.
Functional expression of cytochrome P450 in Escherichia coli An approach to functional analysis of uncharacterized enzymes for flavonoid biosynthesis
Plant Biotechnol.
32
205-213
2015
Glycine max, Glycine max (Q2LAL0)
-
brenda
Chen, J.; Yuan, H.; Zhang, L.; Pan, H.; Xu, R.; Zhong, Y.; Chen, J.; Nan, P.
Cloning, expression and purification of isoflavone-2'-hydroxylase from Astragalus membranaceus Bge. Var. mongolicus (Bge.) Hsiao
Protein Expr. Purif.
107
83-89
2015
Astragalus membranaceus (W5S082), Astragalus membranaceus
brenda
EXTERNAL LINKS (specific for EC-Number 1.14.14.90)
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