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Information on EC 1.14.14.87 - 2-hydroxyisoflavanone synthase
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EC Tree
1.14.14.87 2-hydroxyisoflavanone synthaseIUBMB Comments
A cytochrome P-450 (heme thiolate) protein found in plants. The reaction involves the migration of the 2-phenyl group of the flavanone to the 3-position of the isoflavanone. The 2-hydroxyl group is derived from the oxygen molecule. EC 4.2.1.105, 2-hydroxyisoflavanone dehydratase, acts on the products with loss of water and formation of genistein and daidzein, respectively.
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Word Map
- 1.14.14.87
- soybean
- chalcone
-
isoflavonoids
- genistein
- daidzein
- formononetin
-
soja
- glyceollin
-
non-legume
- medicarpin
-
legume-specific
- synthesis
The enzyme appears in viruses and cellular organisms
Reaction Schemes
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+
=
+
+
+
+
=
+
+
Synonyms
isoflavone synthase, 2-hydroxyisoflavanone synthase, gmifs1, gmifs, 2-his, cyp93c2, cyp93c, cyp93c18, ifs2-12, 2-hydroxyisoflavanone synthase 1, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CYP93C
EC 1.14.13.136
-
-
formerly
-
EC 1.14.13.86
-
-
formerly
-
GmIFS1
IFS
IFS1
IFS2
isoflavone synthase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(2S)-naringenin + O2 + [reduced NADPH-hemoprotein reductase] = 2,4',5,7-tetrahydroxyisoflavanone + H2O + [oxidized NADPH-hemoprotein reductase]
(2)
-
-
-
liquiritigenin + O2 + [reduced NADPH-hemoprotein reductase] = 2,4',7-trihydroxyisoflavanone + H2O + [oxidized NADPH-hemoprotein reductase]
(1)
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
liquiritigenin, [reduced NADPH-hemoprotein reductase]:oxygen oxidoreductase (hydroxylating, aryl migration)
A cytochrome P-450 (heme thiolate) protein found in plants. The reaction involves the migration of the 2-phenyl group of the flavanone to the 3-position of the isoflavanone. The 2-hydroxyl group is derived from the oxygen molecule. EC 4.2.1.105, 2-hydroxyisoflavanone dehydratase, acts on the products with loss of water and formation of genistein and daidzein, respectively.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(2S)-7,4'-dihydroxyflavanone + [reduced NADPH-hemoprotein reductase] + O2
2,7,4'-trihydroxyisoflavanone + [oxidized NADPH-hemoprotein reductase] + H2O
-
i.e. (2S)-liquiritigenin
-
-
?
(2S)-liquiritigenin + [reduced NADPH-hemoprotein reductase] + O2
2,7,4'-trihydroxyisoflavanone + [oxidized NADPH-hemoprotein reductase] + H2O
(2S)-naringenin + O2 + [reduced NADPH-hemoprotein reductase]
2,4',5,7-tetrahydroxyisoflavanone + H2O + [oxidized NADPH-hemoprotein reductase]
(2S)-naringenin + O2 + [reduced NADPH-hemoprotein reductase]
genistein + 2 H2O + [oxidized NADPH-hemoprotein reductase]
-
-
-
-
?
(2S)-naringenin + [reduced NADPH-hemoprotein reductase] + O2
2,5,7,4'-tetrahydroxyisoflavanone + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
7,4'-dihydroxyflavanone + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
2,7,4'-trihydroxyisoflavanone + 3,7,4'-trihydroxyflavanone + 2 [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
i.e. liquirtigenin
3,7,4'-trihydroxyflavanone is the by-product of the reaction (8% yield)
-
?
liquiritigenin + O2 + [reduced NADPH-hemoprotein reductase]
2,4',7-trihydroxyisoflavanone + H2O + [oxidized NADPH-hemoprotein reductase]
liquiritigenin + O2 + [reduced NADPH-hemoprotein reductase]
daidzein + 2 H2O + [oxidized NADPH-hemoprotein reductase]
-
-
-
-
?
liquiritigenin + [reduced NADPH-hemoprotein reductase] + O2
2,4',7-trihydroxyisoflavanone + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
liquiritigenin + [reduced NADPH-hemoprotein reductase] + O2
2,7,4'-trihydroxyisoflavanone + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
major product is 2,7,4'-trihydroxyisoflavanone which further reacts to daidzein
-
?
(2S)-liquiritigenin + [reduced NADPH-hemoprotein reductase] + O2
2,7,4'-trihydroxyisoflavanone + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
(2S)-liquiritigenin + [reduced NADPH-hemoprotein reductase] + O2
2,7,4'-trihydroxyisoflavanone + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
(2S)-naringenin + O2 + [reduced NADPH-hemoprotein reductase]
2,4',5,7-tetrahydroxyisoflavanone + H2O + [oxidized NADPH-hemoprotein reductase]
-
-
-
?
(2S)-naringenin + O2 + [reduced NADPH-hemoprotein reductase]
2,4',5,7-tetrahydroxyisoflavanone + H2O + [oxidized NADPH-hemoprotein reductase]
-
-
-
?
(2S)-naringenin + O2 + [reduced NADPH-hemoprotein reductase]
2,4',5,7-tetrahydroxyisoflavanone + H2O + [oxidized NADPH-hemoprotein reductase]
-
-
-
?
liquiritigenin + O2 + [reduced NADPH-hemoprotein reductase]
2,4',7-trihydroxyisoflavanone + H2O + [oxidized NADPH-hemoprotein reductase]
-
-
-
?
liquiritigenin + O2 + [reduced NADPH-hemoprotein reductase]
2,4',7-trihydroxyisoflavanone + H2O + [oxidized NADPH-hemoprotein reductase]
-
-
-
?
liquiritigenin + O2 + [reduced NADPH-hemoprotein reductase]
2,4',7-trihydroxyisoflavanone + H2O + [oxidized NADPH-hemoprotein reductase]
-
-
-
?
liquiritigenin + O2 + [reduced NADPH-hemoprotein reductase]
2,4',7-trihydroxyisoflavanone + H2O + [oxidized NADPH-hemoprotein reductase]
-
-
-
?
additional information
?
-
enzyme is more active with liquiritigenin than with naringenin
-
-
?
additional information
?
-
-
enzyme is more active with liquiritigenin than with naringenin
-
-
?
additional information
?
-
the amount of conversion of naringenin to genistein is about 50% less than the conversion of liquiritigenin to daidzein for both isoforms IFS1 and IFS2
-
-
?
additional information
?
-
the amount of conversion of naringenin to genistein is about 50% less than the conversion of liquiritigenin to daidzein for both isoforms IFS1 and IFS2
-
-
?
additional information
?
-
-
the amount of conversion of naringenin to genistein is about 50% less than the conversion of liquiritigenin to daidzein for both isoforms IFS1 and IFS2
-
-
?
additional information
?
-
-
the enzyme also produces a spirodienone intermediate from (2S)-liquiritigenin which further reacts to 2,7-dihydroxy-4'-methoxyisoflavanone and formononetin
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(2S)-liquiritigenin + [reduced NADPH-hemoprotein reductase] + O2
2,7,4'-trihydroxyisoflavanone + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
(2S)-naringenin + O2 + [reduced NADPH-hemoprotein reductase]
2,4',5,7-tetrahydroxyisoflavanone + H2O + [oxidized NADPH-hemoprotein reductase]
-
-
-
?
(2S)-naringenin + [reduced NADPH-hemoprotein reductase] + O2
2,5,7,4'-tetrahydroxyisoflavanone + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
liquiritigenin + O2 + [reduced NADPH-hemoprotein reductase]
2,4',7-trihydroxyisoflavanone + H2O + [oxidized NADPH-hemoprotein reductase]
-
-
-
?
liquiritigenin + [reduced NADPH-hemoprotein reductase] + O2
2,4',7-trihydroxyisoflavanone + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
additional information
?
-
enzyme is more active with liquiritigenin than with naringenin
-
-
?
additional information
?
-
-
enzyme is more active with liquiritigenin than with naringenin
-
-
?
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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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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Dehydration
Elicitor-induced association of isoflavone O-methyltransferase with endomembranes prevents the formation and 7-O-methylation of daidzein during isoflavonoid phytoalexin biosynthesis.
Infections
Transcription analyses of GmICHG, a gene coding for a ?-glucosidase that catalyzes the specific hydrolysis of isoflavone conjugates in Glycine max (L.) Merr
Infections
Transcription analyses of GmICHG, a gene coding for a ?-glucosidase that catalyzes the specific hydrolysis of isoflavone conjugates in Glycine max (L.) Merr.
Infections
Virus-induced gene silencing in soybean seeds and the emergence stage of soybean plants with Apple latent spherical virus vectors.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
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
-
and pod, highest expression level of isoform IFS2. Embryos excised from developing soybean seeds also accumulate isoflavonoids from a synthetic medium. Developing soybean embryos have an ability to synthesize isoflavonoids de novo, but transport from maternal tissues may in part contribute to the accumulation of these natural products in the seed
brenda
-
and root, highest expression level of isoform IFS1. Developing soybean embryos have an ability to synthesize isoflavonoids de novo, but transport from maternal tissues may in part contribute to the accumulation of these natural products in the seed
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
overexpression and RNAi-mediated silencing of GmMYB29 in soybean hairy roots resulted in increased and decreased isoflavone content, respectively. 11 Natural GmMYB29 polymorphisms are significantly associated with isoflavone contents, and regulation of GmMYB29 expression partially contributes to the observed phenotypic variation, the detected single nucleotide polymorphism is SNP AX-93910416, detected within the 5'-untranslated region of Glyma20g35180 (GmMYB29)
metabolism
physiological function
metabolism
(2S)-flavanones undergo 2-hydroxylation catalyzed by 2-hydroxyisoflavanone synthase (GmIFS), a microsomal cytochrome P450 enzyme (CYP93C), to produce 2-hydroxyisoflavanones pathway of isoflavone biosynthesis in soybean. Analysis of binary protein-protein interactions of 2-hydroxyisoflavanone synthase 1 (GmIFS1), a P450 (CYP93C), with cytoplasmic enzymes involved in isoflavone biosynthesis in soybean, by split-ubiquitin system. Identification of binary interactions between GmIFS1 and chalcone synthase 1 (GmCHS1), and between GmIFS1 and chalcone isomerases (GmCHIs), the interaction of GmCHS1 and GmCHIs with GmIFS1 takes place on endoplasmic reticulum on which GmIFS1 is located
metabolism
the critical branch point enzymes chalcone synthase (CHS) and isoflavone synthase (IFS) lead substrates to the isoflavone synthesis branch and finally generate isoflavones and their derivatives, isoflavone regulation-related transcription factors, overview. Positive regulatory role of GmMYB29 in isoflavone biosynthesis
physiological function
both transient and stable expression of the IFS2_12 or IFS/alfalfa chalcone isomerase constructs in Nicotiana tabacum result in the production of the isoflavonoid genistein and its conjugates
physiological function
constitutive expression of isoflavone synthase in alfalfa (Medicago sativa) leaves leads to genistein glucoside production (up to 50 nmol/g fresh weight) and to accumulation of glucosides of biochanin A and pratensein. IFS1 is highly expressed in all transgenic organs examined, while genistein accumulation is limited to leaves. IFS1-expressing lines accumulate additional isoflavones, including formononetin and daidzein and the phytoalexin medicarpin, in response to UV-B or Phoma medicaginis. IFS1 expression does not significantly alter global gene expression in the leaves
physiological function
enzyme shows binary interactions with cytoplasmic chalcone synthase 1 and chalcone isomerases CHI, both in recombinant Saccharomyces cerevisiae and in planta
physiological function
expression in Arabidopsis thaliana leads to production of the isoflavone genistein
physiological function
expression in Brassica napus plants via Agrobacterium tumefaciens-mediated transformation direct the synthesis and accumulation of genistein derivatives in leaves up to 0.72 mg/g dry weight. In addition, expression levels for most Brassica napus genes in the phenylpropanoid pathway are altered
physiological function
the expression of the IFS gene in Oryza sativa leads to the production of the isoflavone genistein in rice tissues. The genistein produced in rice cells is present in a glycoside form. The expression of isoflavone synthase confers rice plants with the ability to produce flavonoids that are able to induce nod gene expression, albeit to varied degrees, in different rhizobia
physiological function
upon coexpression of IFS with rice P450 reductase in yeast, the production of genistein from naringein increases about 4.3fold
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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). C93C1_SOYBN
521
0
58869
Swiss-Prot
Mitochondrion (Reliability: 3)
C93C2_GLYEC
523
0
59429
Swiss-Prot
Secretory Pathway (Reliability: 5)
C93C2_GLYUR
523
0
59242
Swiss-Prot
Chloroplast (Reliability: 5)
F8RYF7_ASTMO
525
0
59401
TrEMBL
Mitochondrion (Reliability: 5)
K9JZ57_ONOVI
528
0
59785
TrEMBL
Mitochondrion (Reliability: 5)
A0A072UPL5_MEDTR
522
0
58978
TrEMBL
Mitochondrion (Reliability: 4)
A0A3Q7K757_CICAR
524
0
59368
TrEMBL
Chloroplast (Reliability: 5)
A0A396IHI3_MEDTR
523
0
59198
TrEMBL
Secretory Pathway (Reliability: 5)
I6XNK2_TRIRP
523
0
58984
TrEMBL
Secretory Pathway (Reliability: 5)
Q49BZ0_MEDTR
522
0
59038
TrEMBL
Mitochondrion (Reliability: 5)
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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
K375T
-
the mutant catalyses the aryl migration from liquiritigenin to yield 3,7,4'-trihydroxyflavanone only, its pH optimum is at pH 6.5
L371V/K375T
-
the mutant shows 3-5% activity levels compared to the wild type. The mutant produces a mixture of 95% 3beta-hydroxyflavanone and 5% flavone from (2S)-liquiritigenin
S310T
-
the mutant also catalyses the aryl migration from liquiritigenin to yield 2,7,4'-trihydroxyisoflavanone, but the ratio of the by-product (3,7,4'-trihydroxyflavanone) formation is increased from 8% to 36% (pH 7.5), and a small amount (7%) of a new product, 7,4'-dihydroxyflavone, is detected compared to the wild type
S310T/K375T
-
the P450 level of the mutant is approximately 1.5times that of wild type. The mutant shows 3-5% activity levels compared to the wild type
S310T/L371V/K375T
additional information
S310T/L371V/K375T
-
the mutant produces 100% flavone from (2S)-liquiritigenin
S310T/L371V/K375T
-
the mutant shows 4times higher P450 level than the wild type
additional information
oestrogen-deficient (ovariectomized, Ovx) mice fed with leaf extract from transgenic plant co-expressing AtMYB12 and GmIFS1 but not wild-type extract exhibit significant conservation of trabecular microarchitecture, reduced osteoclast number and expression of osteoclastogenic genes, higher total serum antioxidant levels, and increased uterine oestrogenicity compared with Ovx mice treated with vehicle (control). The simultaneous coexpression of AtMYB12 and GmIFS1 in tobacco leads to the accumulation of substantial amount of genistein in addition to flavonols
additional information
-
oestrogen-deficient (ovariectomized, Ovx) mice fed with leaf extract from transgenic plant co-expressing AtMYB12 and GmIFS1 but not wild-type extract exhibit significant conservation of trabecular microarchitecture, reduced osteoclast number and expression of osteoclastogenic genes, higher total serum antioxidant levels, and increased uterine oestrogenicity compared with Ovx mice treated with vehicle (control). The simultaneous coexpression of AtMYB12 and GmIFS1 in tobacco leads to the accumulation of substantial amount of genistein in addition to flavonols
additional information
deletion of the membrane-spanning domain and insertion of a hydrophilic polypeptide in the N-terminus and a four histidine tag at the C-terminus results dramatically enhanced expression in Escherichia coli and and solubility. The purified enzyme exhibits the same activity as the full length membrane-associated enzyme expressed in yeast
additional information
-
deletion of the membrane-spanning domain and insertion of a hydrophilic polypeptide in the N-terminus and a four histidine tag at the C-terminus results dramatically enhanced expression in Escherichia coli and and solubility. The purified enzyme exhibits the same activity as the full length membrane-associated enzyme expressed in yeast
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Arabidopsis thaliana and in leaves of Nicotiana benthamiana
expression in Saccharomyces cerevisiae
gene ifs1, full-length GmIFS1 cDNA is isolated through RT-PCR of total RNA of soybean seedling, recombinant coexpression of Arabidopsis thaliana transcription factor, AtMYB12, and Glycine max isoflavone synthase, GmIFS1, genes in Nicotiana tabacum cv. Petit Havana via Agrobacterium tumefaciens strain LBA4404 transformation method leading to enhanced biosynthesis of isoflavones and flavonols resulting in osteoprotective activity. real-time PCR and RT-PCR enzyme expression analysis
gene ifs1, protein-protein interaction analysis using the split-ubiquitin system, in planta by BiFC, and the yeast two-hybrid system in Saccharomyces cerevisiae. No appreciable yeast growth is detected with any combinations of proteins under the assay conditions
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
gene ifs1, recombinant coexpression of Arabidopsis thaliana transcription factor, AtMYB12, and Glycine max isoflavone synthase, GmIFS1, genes in Nicotiana benthamiana leads to enhanced biosynthesis of isoflavones and flavonols resulting in osteoprotective activity
the R2R3-type MYB transcription factor GmMYB29 is located in the nucleus and activates the IFS2 (isoflavone synthase 2) gene promoter. Overexpression and RNAi-mediated silencing of GmMYB29 in soybean hairy roots results in increased and decreased isoflavone content, respectively. 11 Natural GmMYB29 polymorphisms are significantly associated with isoflavone contents, and regulation of GmMYB29 expression partially contributes to a phenotypic variation observed after inhibition of GmMYB29
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
construction of an in-frame fusion of IFS and cytochrome P450 reductase from rice after removing the membrane binding domain of both enzymes. Expression of the fusion construct in Escherichia coli leads to conversion of naringenin into genistein. Upon optimization of conditions, 60 microM of genistein can be generated from 80 microM of naringenin
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sawada, Y.; Kinoshita, K.; Akashi, T.; Aoki, T.; Ayabe, S.
Key amino acid residues required for aryl migration catalysed by the cytochrome P450 2-hydroxyisoflavanone synthase
Plant J.
31
555-564
2002
Glycyrrhiza echinata
brenda
Sawada, Y.; Ayabe, S.
Multiple mutagenesis of P450 isoflavonoid synthase reveals a key active-site residue
Biochem. Biophys. Res. Commun.
330
907-913
2005
Glycyrrhiza echinata
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
brenda
Hashim, M.F.; Hakamatsuka, T.; Ebizuka, Y.; Sankawa, U.
Reaction mechanism of oxidative rearrangement of flavanone in isoflavone biosynthesis
FEBS Lett.
271
219-22
1990
Pueraria montana var. lobata
brenda
Lapcik, O.; Honys, D.; Koblovska, R.; Mackova, Z.; Vitkova, M.; Klejdus, B.
Isoflavonoids are present in Arabidopsis thaliana despite the absence of any homologue to known isoflavonoid synthases
Plant Physiol. Biochem.
44
106-114
2006
no activity in Arabidopsis thaliana
brenda
Picmanova, M.; Renak, D.; Fecikova, J.; Ruzika, P.; Miksatkova, P.; Lapcķk, O.; Honys, D.
Functional expression and subcellular localization of pea polymorphic isoflavone synthase CYP93C18
Biol. Plant.
57
635-645
2013
Pisum sativum (Q7XAU5)
-
brenda
Franzmayr, B.K.; Rasmussen, S.; Fraser, K.M.; Jameson, P.E.
Expression and functional characterization of a white clover isoflavone synthase in tobacco
Ann. Bot.
110
1291-1301
2012
Trifolium repens (I6XNK2), Trifolium repens
brenda
Steele, C.L.; Gijzen, M.; Qutob, D.; Dixon, R.A.
Molecular characterization of the enzyme catalyzing the aryl migration reaction of isoflavonoid biosynthesis in soybean
Arch. Biochem. Biophys.
367
146-150
1999
Glycine max (Q9SWR5), Glycine max
brenda
Waki, T.; Yoo, D.; Fujino, N.; Mameda, R.; Denessiouk, K.; Yamashita, S.; Motohashi, R.; Akashi, T.; Aoki, T.; Ayabe, S.; Takahashi, S.; Nakayama, T.
Identification of protein-protein interactions of isoflavonoid biosynthetic enzymes with 2-hydroxyisoflavanone synthase in soybean (Glycine max (L.) Merr.)
Biochem. Biophys. Res. Commun.
469
546-551
2016
Glycine max (Q9M6B9), Glycine max
brenda
Kim, D.H.; Kim, B.G.; Lee, H.J.; Lim, Y.; Hur, H.G.; Ahn, J.H.
Enhancement of isoflavone synthase activity by co-expression of P450 reductase from rice
Biotechnol. Lett.
27
1291-1294
2005
Trifolium pratense (Q84QI4), Trifolium pratense
brenda
Chu, S.; Wang, J.; Cheng, H.; Yang, Q.; Yu, D.
Evolutionary study of the isoflavonoid pathway based on multiple copies analysis in soybean
BMC Genet.
15
76
2014
Glycine max (Q9SWR5)
brenda
Kochs, G.; Grisebach, H.
Enzymic synthesis of isoflavones
Eur. J. Biochem.
155
311-318
1986
Glycine max
brenda
Sreevidya, V.S.; Srinivasa Rao, C.; Sullia, S.B.; Ladha, J.K.; Reddy, P.M.
Metabolic engineering of rice with soybean isoflavone synthase for promoting nodulation gene expression in rhizobia
J. Exp. Bot.
57
1957-1969
2006
Glycine max (O48926), Glycine max
brenda
Kim, D.H.; Kim, B.G.; Jung, N.R.; Ahn, J.H.
Production of genistein from naringenin using Escherichia coli containing isoflavone synthase-cytochrome P450 reductase fusion protein
J. Microbiol. Biotechnol.
19
1612-1616
2009
Trifolium pratense (Q84QI4)
brenda
Jung, W.; Yu, O.; Lau, S.M.; OKeefe, D.P.; Odell, J.; Fader, G.; McGonigle, B.
Identification and expression of isoflavone synthase, the key enzyme for biosynthesis of isoflavones in legumes
Nat. Biotechnol.
18
208-212
2000
Glycine max (O48926), Glycine max (Q9M6B9), Glycine max
brenda
Pandey, A.; Misra, P.; Khan, M.; Swarnkar, G.; Tewari, M.; Bhambhani, S.; Trivedi, R.; Chattopadhyay, N.; Trivedi, P.
Co-expression of Arabidopsis transcription factor, AtMYB12, and soybean isoflavone synthase, GmIFS1, genes in tobacco leads to enhanced biosynthesis of isoflavones and flavonols resulting in osteoprotective activity
Plant Biotechnol. J.
12
69-80
2014
Glycine max (Q9M6D6), Glycine max
brenda
Li, X.; Qin, J.C.; Wang, Q.Y.; Wu, X.; Lang, C.Y.; Pan, H.Y.; Gruber, M.Y.; Gao, M.J.
Metabolic engineering of isoflavone genistein in Brassica napus with soybean isoflavone synthase
Plant Cell Rep.
30
1435-1442
2011
Glycine max (O48926), Glycine max
brenda
Dhaubhadel, S.; McGarvey, B.D.; Williams, R.; Gijzen, M.
Isoflavonoid biosynthesis and accumulation in developing soybean seeds
Plant Mol. Biol.
53
733-743
2003
Glycine max
brenda
Deavours, B.E.; Dixon, R.A.
Metabolic engineering of isoflavonoid biosynthesis in alfalfa
Plant Physiol.
138
2245-2259
2005
Medicago truncatula (Q49BZ0), Medicago truncatula
brenda
Shimada, N.; Akashi, T.; Aoki, T.; Ayabe, S.
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 (A5LGW8), Lotus japonicus
brenda
Chang, Z.; Wang, X.; Wei, R.; Liu, Z.; Shan, H.; Fan, G.; Hu, H.
Functional expression and purification of CYP93C20, a plant membrane-associated cytochrome P450 from Medicago truncatula
Protein Expr. Purif.
150
44-52
2018
Medicago truncatula (Q84Y08), Medicago truncatula
brenda
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