Information on EC 1.14.14.87 - 2-hydroxyisoflavanone synthase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.14.14.87
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RECOMMENDED NAME
GeneOntology No.
2-hydroxyisoflavanone synthase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(2S)-naringenin + O2 + [reduced NADPH-hemoprotein reductase] = 2,4',5,7-tetrahydroxyisoflavanone + H2O + [oxidized NADPH-hemoprotein reductase]
show the reaction diagram
(2)
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liquiritigenin + O2 + [reduced NADPH-hemoprotein reductase] = 2,4',7-trihydroxyisoflavanone + H2O + [oxidized NADPH-hemoprotein reductase]
show the reaction diagram
(1)
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
isoflavonoid biosynthesis I
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isoflavonoid biosynthesis II
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Isoflavonoid biosynthesis
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Biosynthesis of secondary metabolites
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SYSTEMATIC NAME
IUBMB Comments
liquiritigenin, [reduced NADPH-hemoprotein reductase]:oxygen oxidoreductase (hydroxylating, aryl migration)
Requires cytochrome P-450. 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.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
no activity in Arabidopsis thaliana
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-
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Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
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Q84QI4
UniProt
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
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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
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(2S)-7,4'-dihydroxyflavanone + [reduced NADPH-hemoprotein reductase] + O2
2,7,4'-trihydroxyisoflavanone + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
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i.e. (2S)-liquiritigenin
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-
?
(2S)-liquiritigenin + [reduced NADPH-hemoprotein reductase] + O2
2,7,4'-trihydroxyisoflavanone + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
(2S)-naringenin + O2 + [reduced NADPH-hemoprotein reductase]
2,4',5,7-tetrahydroxyisoflavanone + H2O + [oxidized NADPH-hemoprotein reductase]
show the reaction diagram
(2S)-naringenin + O2 + [reduced NADPH-hemoprotein reductase]
genistein + 2 H2O + [oxidized NADPH-hemoprotein reductase]
show the reaction diagram
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-
-
-
?
(2S)-naringenin + [reduced NADPH-hemoprotein reductase] + O2
2,5,7,4'-tetrahydroxyisoflavanone + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
-
-
-
?
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
show the reaction diagram
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i.e. liquirtigenin
3,7,4'-trihydroxyflavanone is the by-product of the reaction (8% yield)
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?
liquiritigenin + O2 + [reduced NADPH-hemoprotein reductase]
2,4',7-trihydroxyisoflavanone + H2O + [oxidized NADPH-hemoprotein reductase]
show the reaction diagram
liquiritigenin + O2 + [reduced NADPH-hemoprotein reductase]
daidzein + 2 H2O + [oxidized NADPH-hemoprotein reductase]
show the reaction diagram
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-
-
-
?
liquiritigenin + [reduced NADPH-hemoprotein reductase] + O2
2,4',7-trihydroxyisoflavanone + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
Q9M6D6;
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-
-
?
liquiritigenin + [reduced NADPH-hemoprotein reductase] + O2
2,7,4'-trihydroxyisoflavanone + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
-
-
major product is 2,7,4'-trihydroxyisoflavanone which further reacts to daidzein
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?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(2S)-liquiritigenin + [reduced NADPH-hemoprotein reductase] + O2
2,7,4'-trihydroxyisoflavanone + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
Q7XAU5
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-
-
?
(2S)-naringenin + O2 + [reduced NADPH-hemoprotein reductase]
2,4',5,7-tetrahydroxyisoflavanone + H2O + [oxidized NADPH-hemoprotein reductase]
show the reaction diagram
Q9SWR5
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-
-
?
(2S)-naringenin + [reduced NADPH-hemoprotein reductase] + O2
2,5,7,4'-tetrahydroxyisoflavanone + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
Q7XAU5
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-
-
?
liquiritigenin + O2 + [reduced NADPH-hemoprotein reductase]
2,4',7-trihydroxyisoflavanone + H2O + [oxidized NADPH-hemoprotein reductase]
show the reaction diagram
Q9SWR5
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-
-
?
liquiritigenin + [reduced NADPH-hemoprotein reductase] + O2
2,4',7-trihydroxyisoflavanone + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
Q9M6D6
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?
additional information
?
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Q9SWR5
enzyme is more active with liquiritigenin than with naringenin
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cytochrome P450
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NADPH
additional information
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no cofactors: NADH, FAD, FMN or ascorbate
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Iron
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the (P450) enzyme contains iron
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ancymidol
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complete inhibition at 1 mM
CO2
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52% inhibition in the presence of CO2 gas
Metyrapone
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complete inhibition at 0.1 mM
SKF 525-A
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73% inhibition at 2 mM
uniconazole
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complete inhibition at 0.1 mM
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
O2
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absolutely required
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0087
(2S)-naringenin
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pH 7.5, temperature not specified in the publication
0.006 - 0.011
7,4'-dihydroxyflavanone
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8 - 8.6
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.1
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half-maximal activity
9
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half-maximal activity
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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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
Manually annotated by BRENDA team
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and embryo, highest expression level of isoform IFS2
Manually annotated by BRENDA team
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and seed coat, highest expression level of isoform IFS1
Manually annotated by BRENDA team
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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
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
59400
x * 59400, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Arabidopsis thaliana and in leaves of Nicotiana benthamiana
expressed in Saccharomyces cerevisiae microsomes
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expressed in Saccharomyces cerevisiae strain BJ2168
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expression in insect cells
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expression in Saccharomyces cerevisiae
expression in Saccharomyces cerevisiae; 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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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
Q9M6D6;
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
Q9M6D6;
increased expression upon elicitation
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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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K375T
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the mutant catalyses the aryl migration from liquiritigenin to yield 3,7,4'-trihydroxyflavanone only, its pH optimum is at pH 6.5
L371V
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inactive
L371V/K375T
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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
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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
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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
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the mutant produces 100% flavone from (2S)-liquiritigenin; the mutant shows 4times higher P450 level than the wild type
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
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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