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(2S)-flavanone + 2-oxoglutarate + O2
(2R/3R)-dihydroflavonol + succinate + CO2
-
key step towards biosynthesis of flavonols, anthocyanins and catechins
-
-
?
(2S)-naringenin + 2-oxoglutarate + O2
(2R,3R)-dihydrokaempferol + succinate + CO2
(S)-eriodictyol + 2-oxoglutarate + O2
(2R,3R)-dihydroquercetin + succinate + CO2
-
-
-
?
(S)-eriodictyol + 2-oxoglutarate + O2
dihydroquercetin + succinate + CO2
-
-
-
?
(S)-homoeriodictyol + 2-oxoglutarate + O2
3'-O-methyltaxifolin + succinate + CO2
-
-
-
?
(S)-pinocembrin + 2-oxoglutarate + O2
pinobanksin + succinate + CO2
-
-
-
?
3'-methoxy eriodictyol + 2-oxoglutarate + O2
? + succinate + CO2
4'-methoxy eriodictyol + 2-oxoglutarate + O2
? + succinate + CO2
a (2S)-flavan-4-one + 2-oxoglutarate + O2
a (2R,3R)-dihydroflavonol + succinate + CO2
a flavanone + 2-oxoglutarate + O2
a dihydroflavonol + succinate + CO2
eriodictyol + 2-oxoglutarate + O2
(2R,3R)-dihydroquercetin + succinate + CO2
eriodictyol + 2-oxoglutarate + O2
dihydroquercetin + succinate + CO2
eriodyctiol + 2-oxoglutarate + O2
dihydroquercetin + succinate + CO2
-
-
-
-
?
naringenin + 2-oxoadipate + O2
dihydrokaempferol + pentanedioate + CO2
-
-
-
?
naringenin + 2-oxoglutarate + O2
(2R,3R)-dihydrokaempferol + succinate + CO2
naringenin + 2-oxoglutarate + O2
dihydrokaempferol + succinate + CO2
naringenin + 2-oxoglutarate + O2
dihydrokaempferol + succinate + O2 + 2 H2O
-
-
-
-
?
naringenin + O2 + 2-oxoglutarate
dihydrokaempferol + succinate + CO2
pinocembrin + 2-oxoglutarate + O2
?
-
38% of the activity with naringenin
-
-
?
additional information
?
-
(2S)-naringenin + 2-oxoglutarate + O2
(2R,3R)-dihydrokaempferol + succinate + CO2
-
-
-
?
(2S)-naringenin + 2-oxoglutarate + O2
(2R,3R)-dihydrokaempferol + succinate + CO2
-
enzyme is stereospecific for (S)-naringenin
-
-
?
(2S)-naringenin + 2-oxoglutarate + O2
(2R,3R)-dihydrokaempferol + succinate + CO2
-
-
-
?
(2S)-naringenin + 2-oxoglutarate + O2
(2R,3R)-dihydrokaempferol + succinate + CO2
reaction is stereospecific
-
-
?
(2S)-naringenin + 2-oxoglutarate + O2
(2R,3R)-dihydrokaempferol + succinate + CO2
-
90% of the activity with eriodictyol
-
-
?
(2S)-naringenin + 2-oxoglutarate + O2
(2R,3R)-dihydrokaempferol + succinate + CO2
F3H
-
-
?
(2S)-naringenin + 2-oxoglutarate + O2
(2R,3R)-dihydrokaempferol + succinate + CO2
-
F3H
-
-
?
(2S)-naringenin + 2-oxoglutarate + O2
(2R,3R)-dihydrokaempferol + succinate + CO2
-
-
-
-
ir
(2S)-naringenin + 2-oxoglutarate + O2
(2R,3R)-dihydrokaempferol + succinate + CO2
-
-
-
-
?
(2S)-naringenin + 2-oxoglutarate + O2
(2R,3R)-dihydrokaempferol + succinate + CO2
-
-
-
?
(2S)-naringenin + 2-oxoglutarate + O2
(2R,3R)-dihydrokaempferol + succinate + CO2
-
-
-
-
?
(2S)-naringenin + 2-oxoglutarate + O2
(2R,3R)-dihydrokaempferol + succinate + CO2
-
-
-
?
(2S)-naringenin + 2-oxoglutarate + O2
(2R,3R)-dihydrokaempferol + succinate + CO2
-
His220, His278 and Asp222 are part of the 2-oxoglutarate binding site
-
-
?
(2S)-naringenin + 2-oxoglutarate + O2
(2R,3R)-dihydrokaempferol + succinate + CO2
-
-
-
-
?
3'-methoxy eriodictyol + 2-oxoglutarate + O2
? + succinate + CO2
-
16% of the activity with eriodictyol
-
-
?
3'-methoxy eriodictyol + 2-oxoglutarate + O2
? + succinate + CO2
-
-
-
?
3'-methoxy eriodictyol + 2-oxoglutarate + O2
? + succinate + CO2
68% of the activity with eriodictyol
-
-
?
4'-methoxy eriodictyol + 2-oxoglutarate + O2
? + succinate + CO2
-
56% of the activity with eriodictyol
-
-
?
4'-methoxy eriodictyol + 2-oxoglutarate + O2
? + succinate + CO2
-
-
-
?
4'-methoxy eriodictyol + 2-oxoglutarate + O2
? + succinate + CO2
105% of the activity with eriodictyol
-
-
?
a (2S)-flavan-4-one + 2-oxoglutarate + O2
a (2R,3R)-dihydroflavonol + succinate + CO2
-
-
-
?
a (2S)-flavan-4-one + 2-oxoglutarate + O2
a (2R,3R)-dihydroflavonol + succinate + CO2
-
-
-
?
a (2S)-flavan-4-one + 2-oxoglutarate + O2
a (2R,3R)-dihydroflavonol + succinate + CO2
-
-
-
?
a (2S)-flavan-4-one + 2-oxoglutarate + O2
a (2R,3R)-dihydroflavonol + succinate + CO2
the 2-oxoglutarate binding site RxS is formed by Arg289 and Ser291
-
-
?
a (2S)-flavan-4-one + 2-oxoglutarate + O2
a (2R,3R)-dihydroflavonol + succinate + CO2
-
-
-
?
a (2S)-flavan-4-one + 2-oxoglutarate + O2
a (2R,3R)-dihydroflavonol + succinate + CO2
-
-
-
?
a (2S)-flavan-4-one + 2-oxoglutarate + O2
a (2R,3R)-dihydroflavonol + succinate + CO2
-
-
-
?
a (2S)-flavan-4-one + 2-oxoglutarate + O2
a (2R,3R)-dihydroflavonol + succinate + CO2
-
-
-
?
a (2S)-flavan-4-one + 2-oxoglutarate + O2
a (2R,3R)-dihydroflavonol + succinate + CO2
-
-
-
?
a (2S)-flavan-4-one + 2-oxoglutarate + O2
a (2R,3R)-dihydroflavonol + succinate + CO2
-
-
-
-
?
a (2S)-flavan-4-one + 2-oxoglutarate + O2
a (2R,3R)-dihydroflavonol + succinate + CO2
-
-
-
?
a (2S)-flavan-4-one + 2-oxoglutarate + O2
a (2R,3R)-dihydroflavonol + succinate + CO2
-
-
-
?
a (2S)-flavan-4-one + 2-oxoglutarate + O2
a (2R,3R)-dihydroflavonol + succinate + CO2
-
-
-
?
a flavanone + 2-oxoglutarate + O2
a dihydroflavonol + succinate + CO2
-
-
-
-
?
a flavanone + 2-oxoglutarate + O2
a dihydroflavonol + succinate + CO2
-
-
-
?
a flavanone + 2-oxoglutarate + O2
a dihydroflavonol + succinate + CO2
-
-
-
?
eriodictyol + 2-oxoglutarate + O2
(2R,3R)-dihydroquercetin + succinate + CO2
-
-
-
-
?
eriodictyol + 2-oxoglutarate + O2
(2R,3R)-dihydroquercetin + succinate + CO2
-
-
-
-
?
eriodictyol + 2-oxoglutarate + O2
(2R,3R)-dihydroquercetin + succinate + CO2
-
-
-
-
?
eriodictyol + 2-oxoglutarate + O2
(2R,3R)-dihydroquercetin + succinate + CO2
-
-
-
-
ir
eriodictyol + 2-oxoglutarate + O2
(2R,3R)-dihydroquercetin + succinate + CO2
-
-
-
-
?
eriodictyol + 2-oxoglutarate + O2
(2R,3R)-dihydroquercetin + succinate + CO2
-
-
-
-
?
eriodictyol + 2-oxoglutarate + O2
(2R,3R)-dihydroquercetin + succinate + CO2
-
(2S)-eriodictyol
-
?
eriodictyol + 2-oxoglutarate + O2
(2R,3R)-dihydroquercetin + succinate + CO2
-
95% of the activity with naringenin
-
-
?
eriodictyol + 2-oxoglutarate + O2
(2R,3R)-dihydroquercetin + succinate + CO2
-
-
-
-
?
eriodictyol + 2-oxoglutarate + O2
(2R,3R)-dihydroquercetin + succinate + CO2
-
50% of the activity with naringenin
-
-
?
eriodictyol + 2-oxoglutarate + O2
dihydroquercetin + succinate + CO2
-
-
-
?
eriodictyol + 2-oxoglutarate + O2
dihydroquercetin + succinate + CO2
-
-
-
?
eriodictyol + 2-oxoglutarate + O2
dihydroquercetin + succinate + CO2
-
-
-
?
eriodictyol + 2-oxoglutarate + O2
dihydroquercetin + succinate + CO2
-
-
-
?
eriodictyol + 2-oxoglutarate + O2
dihydroquercetin + succinate + CO2
-
-
-
?
naringenin + 2-oxoglutarate + O2
(2R,3R)-dihydrokaempferol + succinate + CO2
-
the F3H gene is coordinately expressed with chalcone synthase and chalcone isomerase in seedlings. The F3H gene may represent a pivotal point in the regulation of flavonoid biosynthesis
-
-
?
naringenin + 2-oxoglutarate + O2
(2R,3R)-dihydrokaempferol + succinate + CO2
-
-
-
?
naringenin + 2-oxoglutarate + O2
(2R,3R)-dihydrokaempferol + succinate + CO2
-
enzyme is involved in anthocyanin pathway
-
-
?
naringenin + 2-oxoglutarate + O2
(2R,3R)-dihydrokaempferol + succinate + CO2
-
-
-
-
ir
naringenin + 2-oxoglutarate + O2
(2R,3R)-dihydrokaempferol + succinate + CO2
-
enzyme is involved in anthocyanin pathway
-
-
?
naringenin + 2-oxoglutarate + O2
(2R,3R)-dihydrokaempferol + succinate + CO2
-
-
-
-
?
naringenin + 2-oxoglutarate + O2
(2R,3R)-dihydrokaempferol + succinate + CO2
-
enzyme is involved in anthocyanin biosynthesis
-
-
?
naringenin + 2-oxoglutarate + O2
(2R,3R)-dihydrokaempferol + succinate + CO2
-
enzyme is involved in anthocyanin pathway
-
-
?
naringenin + 2-oxoglutarate + O2
(2R,3R)-dihydrokaempferol + succinate + CO2
-
-
-
-
?
naringenin + 2-oxoglutarate + O2
(2R,3R)-dihydrokaempferol + succinate + CO2
-
enzyme is involved in the biosynthesis of flavonoids, catechins, and anthocyanidins
-
-
?
naringenin + 2-oxoglutarate + O2
(2R,3R)-dihydrokaempferol + succinate + CO2
-
-
-
-
?
naringenin + 2-oxoglutarate + O2
(2R,3R)-dihydrokaempferol + succinate + CO2
-
-
-
-
?
naringenin + 2-oxoglutarate + O2
(2R,3R)-dihydrokaempferol + succinate + CO2
-
-
-
-
?
naringenin + 2-oxoglutarate + O2
(2R,3R)-dihydrokaempferol + succinate + CO2
-
-
-
-
?
naringenin + 2-oxoglutarate + O2
(2R,3R)-dihydrokaempferol + succinate + CO2
-
-
-
-
?
naringenin + 2-oxoglutarate + O2
(2R,3R)-dihydrokaempferol + succinate + CO2
-
-
-
-
?
naringenin + 2-oxoglutarate + O2
(2R,3R)-dihydrokaempferol + succinate + CO2
-
-
-
-
?
naringenin + 2-oxoglutarate + O2
(2R,3R)-dihydrokaempferol + succinate + CO2
-
-
-
-
?
naringenin + 2-oxoglutarate + O2
(2R,3R)-dihydrokaempferol + succinate + CO2
-
induction of the enzyme by light
-
-
?
naringenin + 2-oxoglutarate + O2
(2R,3R)-dihydrokaempferol + succinate + CO2
-
enzyme is involved in anthocyanin pathway
-
-
?
naringenin + 2-oxoglutarate + O2
(2R,3R)-dihydrokaempferol + succinate + CO2
Streptocarpus hybrida
-
enzyme is involved in anthocyanin pathway
-
-
?
naringenin + 2-oxoglutarate + O2
(2R,3R)-dihydrokaempferol + succinate + CO2
-
enzyme is involved in anthocyanin pathway
-
-
?
naringenin + 2-oxoglutarate + O2
dihydrokaempferol + succinate + CO2
-
-
-
-
?
naringenin + 2-oxoglutarate + O2
dihydrokaempferol + succinate + CO2
-
-
-
?
naringenin + 2-oxoglutarate + O2
dihydrokaempferol + succinate + CO2
-
-
-
?
naringenin + 2-oxoglutarate + O2
dihydrokaempferol + succinate + CO2
-
-
-
?
naringenin + 2-oxoglutarate + O2
dihydrokaempferol + succinate + CO2
-
-
-
?
naringenin + 2-oxoglutarate + O2
dihydrokaempferol + succinate + CO2
-
-
-
?
naringenin + 2-oxoglutarate + O2
dihydrokaempferol + succinate + CO2
-
-
-
-
?
naringenin + 2-oxoglutarate + O2
dihydrokaempferol + succinate + CO2
-
-
-
?
naringenin + 2-oxoglutarate + O2
dihydrokaempferol + succinate + CO2
-
-
-
?
naringenin + 2-oxoglutarate + O2
dihydrokaempferol + succinate + CO2
-
-
-
-
?
naringenin + 2-oxoglutarate + O2
dihydrokaempferol + succinate + CO2
-
-
-
?
naringenin + 2-oxoglutarate + O2
dihydrokaempferol + succinate + CO2
-
-
-
?
naringenin + 2-oxoglutarate + O2
dihydrokaempferol + succinate + CO2
-
-
-
-
?
naringenin + 2-oxoglutarate + O2
dihydrokaempferol + succinate + CO2
-
-
-
-
?
naringenin + 2-oxoglutarate + O2
dihydrokaempferol + succinate + CO2
-
-
-
-
?
naringenin + 2-oxoglutarate + O2
dihydrokaempferol + succinate + CO2
-
-
-
?
naringenin + 2-oxoglutarate + O2
dihydrokaempferol + succinate + CO2
-
-
-
?
naringenin + 2-oxoglutarate + O2
dihydrokaempferol + succinate + CO2
-
-
-
?
naringenin + O2 + 2-oxoglutarate
dihydrokaempferol + succinate + CO2
-
-
-
?
naringenin + O2 + 2-oxoglutarate
dihydrokaempferol + succinate + CO2
-
0.046 nmol 14C-labeled substrate, 3.48 mM 2-oxoglutarate, 5 mM FeSO4 * 7 H2O, buffer (0.1 M Tris-HCl, pH 7.5, containing 0.4% sodium ascorbate)
-
-
?
naringenin + O2 + 2-oxoglutarate
dihydrokaempferol + succinate + CO2
-
0.046 nmol 14C-labeled substrate, 3.48 mM 2-oxoglutarate, 5 mM FeSO4 * 7 H2O, buffer (0.1 M Tris/HCl, pH 7.5, containing 0.4% sodium ascorbate)
-
-
?
naringenin + O2 + 2-oxoglutarate
dihydrokaempferol + succinate + CO2
-
0.046 nmol 14C-labeled substrate, 3.48 mM 2-oxoglutarate, 5 mM FeSO4 * 7 H2O, buffer (0.1 M Tris/HCl, pH 7.5, containing 0.4% sodium ascorbate)
-
-
?
naringenin + O2 + 2-oxoglutarate
dihydrokaempferol + succinate + CO2
-
-
-
?
naringenin + O2 + 2-oxoglutarate
dihydrokaempferol + succinate + CO2
-
-
-
?
naringenin + O2 + 2-oxoglutarate
dihydrokaempferol + succinate + CO2
-
0.046 nmol 14C-labeled substrate, 3.48 mM 2-oxoglutarate, 5 mM FeSO4 * 7 H2O, buffer (0.1 M Tris/HCl, pH 7.5, containing 0.4% sodium ascorbate)
-
-
?
naringenin + O2 + 2-oxoglutarate
dihydrokaempferol + succinate + CO2
-
-
-
-
?
naringenin + O2 + 2-oxoglutarate
dihydrokaempferol + succinate + CO2
-
0.046 nmol 14C-labeled substrate, 3.48 mM 2-oxoglutarate, 5 mM FeSO4 * 7 H2O, buffer (0.1 M Tris/HCl, pH 7.5, containing 0.4% sodium ascorbate)
-
-
?
naringenin + O2 + 2-oxoglutarate
dihydrokaempferol + succinate + CO2
-
-
-
-
?
naringenin + O2 + 2-oxoglutarate
dihydrokaempferol + succinate + CO2
-
0.046 nmol 14C-labeled substrate, 3.48 mM 2-oxoglutarate, 5 mM FeSO4 * 7 H2O, buffer (0.1 M Tris/HCl, pH 7.5, containing 0.4% sodium ascorbate)
-
-
?
naringenin + O2 + 2-oxoglutarate
dihydrokaempferol + succinate + CO2
-
0.046 nmol 14C-labeled substrate, 3.48 mM 2-oxoglutarate, 5 mM FeSO4 * 7 H2O, buffer (0.1 M Tris/HCl, pH 7.5, containing 0.4% sodium ascorbate)
-
-
?
additional information
?
-
involved in catechin biosynthesis
-
-
?
additional information
?
-
no activity with kaempferol, dihydrokaempferol, quercetin, and dihydroquercetin
-
-
?
additional information
?
-
-
no activity with kaempferol, dihydrokaempferol, quercetin, and dihydroquercetin
-
-
?
additional information
?
-
development of a reverse phase (C18) HPLC method (with elutant ethylacetate) for the determination of flavanone 3beta-hydroxylase and other enzyme activities based on the determination of the compounds produced and consumed on the enzymatic reaction in just one chromatographic analysis, method optimisation considering kinetic studies to establish the optimal assay incubation time
-
-
?
additional information
?
-
-
no activity with (+)-dihydrokaempferol and (2R)-naringenin
-
-
?
additional information
?
-
-
no activity with (2R)-naringenin and 5,7,3',4',5'-pentahydroxyflavanone
-
-
?
additional information
?
-
-
two different protocols for enzyme preparation from eight fruit species
-
-
?
additional information
?
-
-
two different protocols for enzyme preparation from eight fruit species
-
-
?
additional information
?
-
-
two different protocols for enzyme preparation from eight fruit species
-
-
?
additional information
?
-
-
development of a reverse phase (C18) HPLC method (with elutant ethylacetate) for the determination of flavanone 3beta-hydroxylase and other enzyme activities based on the determination of the compounds produced and consumed on the enzymatic reaction in just one chromatographic analysis, method optimisation considering kinetic studies to establish the optimal assay incubation time
-
-
?
additional information
?
-
development of a reverse phase (C18) HPLC method (with elutant ethylacetate) for the determination of flavanone 3beta-hydroxylase and other enzyme activities based on the determination of the compounds produced and consumed on the enzymatic reaction in just one chromatographic analysis, method optimisation considering kinetic studies to establish the optimal assay incubation time
-
-
?
additional information
?
-
-
development of a reverse phase (C18) HPLC method (with elutant ethylacetate) for the determination of flavanone 3beta-hydroxylase and other enzyme activities based on the determination of the compounds produced and consumed on the enzymatic reaction in just one chromatographic analysis, method optimisation considering kinetic studies to establish the optimal assay incubation time
-
-
?
additional information
?
-
development of a reverse phase (C18) HPLC method (with elutant ethylacetate) for the determination of flavanone 3beta-hydroxylase and other enzyme activities based on the determination of the compounds produced and consumed on the enzymatic reaction in just one chromatographic analysis, method optimisation considering kinetic studies to establish the optimal assay incubation time
-
-
?
additional information
?
-
-
two different protocols for enzyme preparation from eight fruit species
-
-
?
additional information
?
-
-
two different protocols for enzyme preparation from eight fruit species
-
-
?
additional information
?
-
-
development of a reverse phase (C18) HPLC method (with elutant ethylacetate) for the determination of flavanone 3beta-hydroxylase and other enzyme activities based on the determination of the compounds produced and consumed on the enzymatic reaction in just one chromatographic analysis, method optimisation considering kinetic studies to establish the optimal assay incubation time
-
-
?
additional information
?
-
-
two different protocols for enzyme preparation from eight fruit species
-
-
?
additional information
?
-
-
two different protocols for enzyme preparation from eight fruit species
-
-
?
additional information
?
-
development of a reverse phase (C18) HPLC method (with elutant ethylacetate) for the determination of flavanone 3beta-hydroxylase and other enzyme activities based on the determination of the compounds produced and consumed on the enzymatic reaction in just one chromatographic analysis, method optimisation considering kinetic studies to establish the optimal assay incubation time
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(2S)-flavanone + 2-oxoglutarate + O2
(2R/3R)-dihydroflavonol + succinate + CO2
-
key step towards biosynthesis of flavonols, anthocyanins and catechins
-
-
?
(2S)-naringenin + 2-oxoglutarate + O2
(2R,3R)-dihydrokaempferol + succinate + CO2
-
-
-
?
a (2S)-flavan-4-one + 2-oxoglutarate + O2
a (2R,3R)-dihydroflavonol + succinate + CO2
a flavanone + 2-oxoglutarate + O2
a dihydroflavonol + succinate + CO2
eriodictyol + 2-oxoglutarate + O2
dihydroquercetin + succinate + CO2
eriodyctiol + 2-oxoglutarate + O2
dihydroquercetin + succinate + CO2
-
-
-
-
?
naringenin + 2-oxoglutarate + O2
(2R,3R)-dihydrokaempferol + succinate + CO2
naringenin + 2-oxoglutarate + O2
dihydrokaempferol + succinate + CO2
naringenin + O2 + 2-oxoglutarate
dihydrokaempferol + succinate + CO2
additional information
?
-
a (2S)-flavan-4-one + 2-oxoglutarate + O2
a (2R,3R)-dihydroflavonol + succinate + CO2
-
-
-
?
a (2S)-flavan-4-one + 2-oxoglutarate + O2
a (2R,3R)-dihydroflavonol + succinate + CO2
-
-
-
?
a (2S)-flavan-4-one + 2-oxoglutarate + O2
a (2R,3R)-dihydroflavonol + succinate + CO2
-
-
-
?
a (2S)-flavan-4-one + 2-oxoglutarate + O2
a (2R,3R)-dihydroflavonol + succinate + CO2
-
-
-
?
a (2S)-flavan-4-one + 2-oxoglutarate + O2
a (2R,3R)-dihydroflavonol + succinate + CO2
-
-
-
?
a (2S)-flavan-4-one + 2-oxoglutarate + O2
a (2R,3R)-dihydroflavonol + succinate + CO2
-
-
-
?
a (2S)-flavan-4-one + 2-oxoglutarate + O2
a (2R,3R)-dihydroflavonol + succinate + CO2
-
-
-
?
a (2S)-flavan-4-one + 2-oxoglutarate + O2
a (2R,3R)-dihydroflavonol + succinate + CO2
-
-
-
?
a (2S)-flavan-4-one + 2-oxoglutarate + O2
a (2R,3R)-dihydroflavonol + succinate + CO2
-
-
-
-
?
a (2S)-flavan-4-one + 2-oxoglutarate + O2
a (2R,3R)-dihydroflavonol + succinate + CO2
-
-
-
?
a (2S)-flavan-4-one + 2-oxoglutarate + O2
a (2R,3R)-dihydroflavonol + succinate + CO2
-
-
-
?
a (2S)-flavan-4-one + 2-oxoglutarate + O2
a (2R,3R)-dihydroflavonol + succinate + CO2
-
-
-
?
a flavanone + 2-oxoglutarate + O2
a dihydroflavonol + succinate + CO2
-
-
-
-
?
a flavanone + 2-oxoglutarate + O2
a dihydroflavonol + succinate + CO2
-
-
-
?
a flavanone + 2-oxoglutarate + O2
a dihydroflavonol + succinate + CO2
-
-
-
?
eriodictyol + 2-oxoglutarate + O2
dihydroquercetin + succinate + CO2
-
-
-
?
eriodictyol + 2-oxoglutarate + O2
dihydroquercetin + succinate + CO2
-
-
-
?
eriodictyol + 2-oxoglutarate + O2
dihydroquercetin + succinate + CO2
-
-
-
?
naringenin + 2-oxoglutarate + O2
(2R,3R)-dihydrokaempferol + succinate + CO2
-
the F3H gene is coordinately expressed with chalcone synthase and chalcone isomerase in seedlings. The F3H gene may represent a pivotal point in the regulation of flavonoid biosynthesis
-
-
?
naringenin + 2-oxoglutarate + O2
(2R,3R)-dihydrokaempferol + succinate + CO2
-
enzyme is involved in anthocyanin pathway
-
-
?
naringenin + 2-oxoglutarate + O2
(2R,3R)-dihydrokaempferol + succinate + CO2
-
enzyme is involved in anthocyanin pathway
-
-
?
naringenin + 2-oxoglutarate + O2
(2R,3R)-dihydrokaempferol + succinate + CO2
-
enzyme is involved in anthocyanin biosynthesis
-
-
?
naringenin + 2-oxoglutarate + O2
(2R,3R)-dihydrokaempferol + succinate + CO2
-
enzyme is involved in anthocyanin pathway
-
-
?
naringenin + 2-oxoglutarate + O2
(2R,3R)-dihydrokaempferol + succinate + CO2
-
enzyme is involved in the biosynthesis of flavonoids, catechins, and anthocyanidins
-
-
?
naringenin + 2-oxoglutarate + O2
(2R,3R)-dihydrokaempferol + succinate + CO2
-
induction of the enzyme by light
-
-
?
naringenin + 2-oxoglutarate + O2
(2R,3R)-dihydrokaempferol + succinate + CO2
-
enzyme is involved in anthocyanin pathway
-
-
?
naringenin + 2-oxoglutarate + O2
(2R,3R)-dihydrokaempferol + succinate + CO2
Streptocarpus hybrida
-
enzyme is involved in anthocyanin pathway
-
-
?
naringenin + 2-oxoglutarate + O2
(2R,3R)-dihydrokaempferol + succinate + CO2
-
enzyme is involved in anthocyanin pathway
-
-
?
naringenin + 2-oxoglutarate + O2
dihydrokaempferol + succinate + CO2
-
-
-
-
?
naringenin + 2-oxoglutarate + O2
dihydrokaempferol + succinate + CO2
-
-
-
?
naringenin + 2-oxoglutarate + O2
dihydrokaempferol + succinate + CO2
-
-
-
?
naringenin + 2-oxoglutarate + O2
dihydrokaempferol + succinate + CO2
-
-
-
?
naringenin + 2-oxoglutarate + O2
dihydrokaempferol + succinate + CO2
-
-
-
?
naringenin + 2-oxoglutarate + O2
dihydrokaempferol + succinate + CO2
-
-
-
?
naringenin + 2-oxoglutarate + O2
dihydrokaempferol + succinate + CO2
-
-
-
-
?
naringenin + 2-oxoglutarate + O2
dihydrokaempferol + succinate + CO2
-
-
-
?
naringenin + 2-oxoglutarate + O2
dihydrokaempferol + succinate + CO2
-
-
-
?
naringenin + 2-oxoglutarate + O2
dihydrokaempferol + succinate + CO2
-
-
-
-
?
naringenin + 2-oxoglutarate + O2
dihydrokaempferol + succinate + CO2
-
-
-
-
?
naringenin + 2-oxoglutarate + O2
dihydrokaempferol + succinate + CO2
-
-
-
-
?
naringenin + 2-oxoglutarate + O2
dihydrokaempferol + succinate + CO2
-
-
-
?
naringenin + 2-oxoglutarate + O2
dihydrokaempferol + succinate + CO2
-
-
-
?
naringenin + 2-oxoglutarate + O2
dihydrokaempferol + succinate + CO2
-
-
-
?
naringenin + O2 + 2-oxoglutarate
dihydrokaempferol + succinate + CO2
-
0.046 nmol 14C-labeled substrate, 3.48 mM 2-oxoglutarate, 5 mM FeSO4 * 7 H2O, buffer (0.1 M Tris-HCl, pH 7.5, containing 0.4% sodium ascorbate)
-
-
?
naringenin + O2 + 2-oxoglutarate
dihydrokaempferol + succinate + CO2
-
0.046 nmol 14C-labeled substrate, 3.48 mM 2-oxoglutarate, 5 mM FeSO4 * 7 H2O, buffer (0.1 M Tris/HCl, pH 7.5, containing 0.4% sodium ascorbate)
-
-
?
naringenin + O2 + 2-oxoglutarate
dihydrokaempferol + succinate + CO2
-
0.046 nmol 14C-labeled substrate, 3.48 mM 2-oxoglutarate, 5 mM FeSO4 * 7 H2O, buffer (0.1 M Tris/HCl, pH 7.5, containing 0.4% sodium ascorbate)
-
-
?
naringenin + O2 + 2-oxoglutarate
dihydrokaempferol + succinate + CO2
-
0.046 nmol 14C-labeled substrate, 3.48 mM 2-oxoglutarate, 5 mM FeSO4 * 7 H2O, buffer (0.1 M Tris/HCl, pH 7.5, containing 0.4% sodium ascorbate)
-
-
?
naringenin + O2 + 2-oxoglutarate
dihydrokaempferol + succinate + CO2
-
0.046 nmol 14C-labeled substrate, 3.48 mM 2-oxoglutarate, 5 mM FeSO4 * 7 H2O, buffer (0.1 M Tris/HCl, pH 7.5, containing 0.4% sodium ascorbate)
-
-
?
naringenin + O2 + 2-oxoglutarate
dihydrokaempferol + succinate + CO2
-
0.046 nmol 14C-labeled substrate, 3.48 mM 2-oxoglutarate, 5 mM FeSO4 * 7 H2O, buffer (0.1 M Tris/HCl, pH 7.5, containing 0.4% sodium ascorbate)
-
-
?
naringenin + O2 + 2-oxoglutarate
dihydrokaempferol + succinate + CO2
-
0.046 nmol 14C-labeled substrate, 3.48 mM 2-oxoglutarate, 5 mM FeSO4 * 7 H2O, buffer (0.1 M Tris/HCl, pH 7.5, containing 0.4% sodium ascorbate)
-
-
?
additional information
?
-
involved in catechin biosynthesis
-
-
?
additional information
?
-
-
two different protocols for enzyme preparation from eight fruit species
-
-
?
additional information
?
-
-
two different protocols for enzyme preparation from eight fruit species
-
-
?
additional information
?
-
-
two different protocols for enzyme preparation from eight fruit species
-
-
?
additional information
?
-
-
two different protocols for enzyme preparation from eight fruit species
-
-
?
additional information
?
-
-
two different protocols for enzyme preparation from eight fruit species
-
-
?
additional information
?
-
-
two different protocols for enzyme preparation from eight fruit species
-
-
?
additional information
?
-
-
two different protocols for enzyme preparation from eight fruit species
-
-
?
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(+)-dihydrokaempferol
-
product inhibition
3-Bromo-2-oxoglutarate
-
1 mM 92% inhibition
3-hydroxy-5-oxo-4-butyryl-cyclohex-3-ene-1-carboxylic acid ethyl ester
3-hydroxy-5-oxo-4-cyclopropanecarbonyl-cyclohex-3-ene-1-carboxylic acid ethyl ester
3-hydroxy-5-oxo-4-propionyl-cyclohex-3-ene-1-(2-dimethylamino)-thiazole
3-hydroxy-5-oxo-4-propionyl-cyclohex-3-ene-1-carbaldehyde
3-hydroxy-5-oxo-4-propionyl-cyclohex-3-ene-1-carbothioic acid S-ethyl ester
3-hydroxy-5-oxo-4-propionyl-cyclohex-3-ene-1-pentanoic acid
benzene-1,2,4,5-tetracarboxylic acid
calcium 3-hydroxy-5-oxo-4-propionyl-cyclohex-3-ene-1-carboxylate
Fe3+
-
1 mM, 56% inhibition
prohexadione-Ca
-
an enzyme inhibitor for 2-oxoglutarate dependent dioxygenases, used as a growth retardant and for control of secondary fire blight, Erwinia amylovora, of apple leaves
Pyridine-2,4-dicarboxylate
pyridine-2,4-dicarboxylic acid diethyl ester
Pyridine-2,5-dicarboxylate
-
0.01 mM, 40% inhibition
pyridine-2,5-dicarboxylic acid
sodium 4,6-dioxo-2,2-dimethyl-5-(1-alloxyamino-butylidene)-cyclohexane-1-carboxylic acid methyl ester
Zn2+
-
in presence of 0.01 mM Fe2+
3-hydroxy-5-oxo-4-butyryl-cyclohex-3-ene-1-carboxylic acid ethyl ester
-
1 mM 36% relative activity, 0.1 mM 68% relative activity
3-hydroxy-5-oxo-4-butyryl-cyclohex-3-ene-1-carboxylic acid ethyl ester
-
1 mM 36% relative activity, 0.1 mM 68% relative activity
3-hydroxy-5-oxo-4-cyclopropanecarbonyl-cyclohex-3-ene-1-carboxylic acid ethyl ester
-
1 mM 9% relative activity, 0.1 mM 38% relative activity
3-hydroxy-5-oxo-4-cyclopropanecarbonyl-cyclohex-3-ene-1-carboxylic acid ethyl ester
-
1 mM 9% relative activity, 0.1 mM 38% relative activity
3-hydroxy-5-oxo-4-propionyl-cyclohex-3-ene-1-(2-dimethylamino)-thiazole
-
1 mM 25% relative activity, 0.1 mM 56% relative activity
3-hydroxy-5-oxo-4-propionyl-cyclohex-3-ene-1-(2-dimethylamino)-thiazole
-
1 mM 25% relative activity, 0.1 mM 56% relative activity
3-hydroxy-5-oxo-4-propionyl-cyclohex-3-ene-1-carbaldehyde
-
1 mM 33% relative activity, 0.1 mM 75% relative activity
3-hydroxy-5-oxo-4-propionyl-cyclohex-3-ene-1-carbaldehyde
-
1 mM 33% relative activity, 0.1 mM 75% relative activity
3-hydroxy-5-oxo-4-propionyl-cyclohex-3-ene-1-carbothioic acid S-ethyl ester
-
1 mM 15% relative activity, 0.1 mM 40% relative activity
3-hydroxy-5-oxo-4-propionyl-cyclohex-3-ene-1-carbothioic acid S-ethyl ester
-
1 mM 15% relative activity, 0.1 mM 40% relative activity
3-hydroxy-5-oxo-4-propionyl-cyclohex-3-ene-1-pentanoic acid
-
1 mM 13% relative activity, 0.1 mM 75% relative activity
3-hydroxy-5-oxo-4-propionyl-cyclohex-3-ene-1-pentanoic acid
-
1 mM 13% relative activity, 0.1 mM 75% relative activity
benzene-1,2,4,5-tetracarboxylic acid
-
1 mM 95% relative activity
benzene-1,2,4,5-tetracarboxylic acid
-
1 mM 95% relative activity
calcium 3-hydroxy-5-oxo-4-propionyl-cyclohex-3-ene-1-carboxylate
-
1 mM 10% relative activity, 0.1 mM 33% relative activity
calcium 3-hydroxy-5-oxo-4-propionyl-cyclohex-3-ene-1-carboxylate
-
1 mM 10% relative activity, 0.1 mM 33% relative activity
Cu2+
-
in presence of 0.01 mM Fe2+
diethyldicarbonate
-
0.5 mM, 15% inhibition; slight
diethyldicarbonate
-
ascorbate protects against inactivation
diethyldicarbonate
-
0.5 mM, 10% inhibition; 2 mM, complete inhibition; slight
diethyldithiocarbamate
-
-
diethyldithiocarbamate
-
-
diethyldithiocarbamate
-
2 mM, complete inhibition
diethyldithiocarbamate
-
2 mM, 81% inhibition
diethyldithiocarbamate
Streptocarpus hybrida
-
-
diethyldithiocarbamate
-
-
EDTA
-
-
EDTA
-
1 mM, 75% inhibition
EDTA
0.2 M, complete loss of activity; 0.2 M, complete loss of activity; 0.2 M, complete loss of activity
EDTA
-
1 mM, 21% inhibition
EDTA
Streptocarpus hybrida
-
-
EDTA
-
2 mM, complete inhibition
KCN
-
-
KCN
-
5 mM, complete inhibition
KCN
-
1 mM, 11% inhibition
KCN
Streptocarpus hybrida
-
-
KCN
-
5 mM, 72% inhibition
p-chloromercuribenzoate
-
0.1 mM, 5% inhibition
p-chloromercuribenzoate
-
1 mM, 91% inhibition
p-chloromercuribenzoate
-
no inhibition
Pyridine-2,4-dicarboxylate
-
most potent competitive inhibitor
Pyridine-2,4-dicarboxylate
-
0.002 mM, 50% inhibition
pyridine-2,4-dicarboxylic acid diethyl ester
-
1 mM 7% relative activity, 0.1 mM 21% relative activity
pyridine-2,4-dicarboxylic acid diethyl ester
-
1 mM 7% relative activity, 0.1 mM 21% relative activity
pyridine-2,5-dicarboxylic acid
-
1 mM 3% relative activity, 0.1 mM 11% relative activity
pyridine-2,5-dicarboxylic acid
-
1 mM 3% relative activity, 0.1 mM 11% relative activity
sodium 4,6-dioxo-2,2-dimethyl-5-(1-alloxyamino-butylidene)-cyclohexane-1-carboxylic acid methyl ester
-
1 mM 89% relative activity
sodium 4,6-dioxo-2,2-dimethyl-5-(1-alloxyamino-butylidene)-cyclohexane-1-carboxylic acid methyl ester
-
1 mM 89% relative activity
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malfunction
-
silencing of flavanone-3-hydroxylase leads to an accumulation of flavanones in leaves, but in contrast not to the formation of 3-deoxyflavonoids. In prohexadione-Ca treated leaves the 3-deoxyflavonoid luteoforol is formed from accumulating flavanones, acting as an antimicrobial compound against the fire blight pathogen Erwinia amylovora. Inducible resistance to fire blight by prohexadione-Ca is not observed with the antisense flavanone-3-hydroxylase apple plants
evolution
-
no significant genetic differentiation is found between cultivated soybean, Glycine max, and its wild relative, Glycine soja, in the target gene, despite of considering bottleneck and founder effect during domestication. The F3H gene might have experienced gene introgressions or diversifying selection events during domestication process, gene F3H2 appears to evolve under positive selection and enjoy a faster evolutionary rate
evolution
-
no significant genetic differentiation is found between cultivated soybean, Glycine max, and its wild relative, Glycine soja, in the target gene, despite of considering bottleneck and founder effect during domestication. The F3H gene might have experienced gene introgressions or diversifying selection events during domestication process, gene F3H2 appears to evolve under positive selection and enjoy a faster evolutionary rate
evolution
-
the enzyme belongs to the 2-oxoglutarate-dependant dioxygenases
evolution
the F3H isozymes have a unique motif of pfam03171 that is maintained in the superfamily of 2-oxoglutarate and Fe(II)-dependent oxygenases
evolution
the enzyme belongs to the 2-oxoglutarate-dependent dioxygenase (2-ODD) family
evolution
the enzyme belongs to the family of 2-oxoglutarate-dependent dioxygenases
evolution
the enzyme belongs to the Fe(II)- and 2-oxoglutarate-dependent dioxygenase (2-ODD) superfamily, sharing the conserved motif of pfam 03171. F3H has a jelly roll in the enzyme core, a typical structure shared by all 2-oxoglutarate-dependent dioxygenases including F3Hs. Phylogenetic and molecular evolutionary analyses
evolution
the enzyme belongs to the Fe2+/2oxoglutarate-dependent dioxygenase superfamily
metabolism
part of flavonoid biosynthetic pathway
metabolism
flavanone 3-hydroxylase converts flavanones to dihydroflavonols for anthocyanin biosynthesis
metabolism
-
the enzyme is involved in the flavonoid and phenylpropanoid biosynthesis pathway, overview
metabolism
flavanone 3-hydroxylase is a key enzyme at a diverging point of the flavonoid pathway leading to production of different pigments: phlobaphene, proanthocyanidin, and anthocyanin, flavonoid biosynthetic pathway, overview
metabolism
the enzyme is involved in anthocyanin biosynthesis
metabolism
(2S)-flavanones are converted to flavonols by the activity of the 2-oxoglutarate-dependent dioxygenases flavanone 3-hydroxylase (F3H) and flavonol synthase (FLS)
metabolism
flavanone 3-hydroxylase (F3H) of the flavonoid pathway catalyzes the stereospecific hydroxylation of (2S)-naringenin and (2S)-eriodictyol to form (2R,3R)-dihydrokaempferol and (2R,3R)-dihydroquercetin, respectively. These dihydroflavonols serve as intermediates for the biosynthesis of flavan-3-ols. Enzyme F3H plays a pivotal role in regulation of biosynthesis of flavan-3-ols in Camellia sinensis
metabolism
positive correlation between absisic acid and LcF3H expression level
metabolism
-
flavanone 3-hydroxylase (F3H) of the flavonoid pathway catalyzes the stereospecific hydroxylation of (2S)-naringenin and (2S)-eriodictyol to form (2R,3R)-dihydrokaempferol and (2R,3R)-dihydroquercetin, respectively. These dihydroflavonols serve as intermediates for the biosynthesis of flavan-3-ols. Enzyme F3H plays a pivotal role in regulation of biosynthesis of flavan-3-ols in Camellia sinensis
-
metabolism
-
the enzyme is involved in the flavonoid and phenylpropanoid biosynthesis pathway, overview
-
physiological function
flavanone 3-hydroxylase converts flavanones to dihydroflavonols for anthocyanin biosynthesis, F3H is a key flavonoid structural gene
physiological function
-
flavanone 3-hydroxylase is involved in the biosynthesis of flavonoids, which play diverse roles in stress responses
physiological function
-
flavanone 3-hydroxylase is involved in the biosynthesis of flavonoids, which play diverse roles in stress responses
physiological function
the enzyme is involved in the red pigmentation of grain tissues, overview
physiological function
F3H is a key regulator for the flavonoid biosynthesis pathway and plays a role in accumulation of anthocyanin pigments in the vacuole
physiological function
F3H is a key regulator for the flavonoid biosynthesis pathway and plays a role in accumulation of anthocyanin pigments in the vacuole
physiological function
flavanone 3-hydroxylase (F3H) is an important regulatory enzyme of the flavonoid pathway which catalyzes the stereospecific hydroxylation of (2S)-naringenin to form (2R,3R)-dihydroflavonol. These dihydroflavonols serve as intermediates for the biosynthesis of anthocyanidins and flavonols
physiological function
flavanone 3-hydroxylase (F3H) is one of the nuclear enzymes acting at the bifurcation of the flavonoid biosynthetic pathway, initiating catalysis of the 3-hydroxylation of (2S)-flavanones, such as naringenin to dihydroflavonols
physiological function
-
the enzyme plays a role in plant salt stress resistance. PnF3H transcripts are induced by various stress and may play a positive role in stress tolerance
physiological function
the F3H gene, which encodes flavanone 3-hydroxylase, is a key regulatory gene in the flavonoid biosynthetic pathway for production of flavonoids and anthocyanins. Anthocyanins accumulate mainly in blueberry fruits, while flavonols are mainly found in leaves and stems
physiological function
the F3H gene, which encodes flavanone-3-hydroxylase, is an essential gene in the flavonoid biosynthetic pathway
physiological function
the flavanone 3-hydroxylase (F3H) gene which encodes flavanone 3-hydroxylase, is essential in flavonoids biosynthetic pathway. Lycium chinense (L. chinense) is a deciduous woody perennial halophyte that grows under a large variety of environmental conditions and survives under extreme drought stress, possible relationship between the oxidative damage and the regulation of LcF3H gene expression in Lycium chinense under drought stress
physiological function
the enzyme plays an important role in biosynthesis of flavonoids
physiological function
the enzyme plays an important role in the biosynthesis of spruce phenolic defenses against bark beetles and their fungal associates. The enzyme forms a defensive product, taxifolin, which is also a metabolic precursor of another defensive product, catechin, which in turn synergizes the toxicity of taxifolin to the bark beetle associated fungus
additional information
in Sorghum seedlings, expression of the two F3H genes is either absent or strongly suppressed during the accumulation of 3-deoxyanthocyanidins
additional information
the Arg285-X-Ser287 motif (RXS) takes part in 2-oxoglutarate binding
additional information
the 2S-naringenin substrate binding site of RtF3H1 consists of Ser135, Try149, Val214, Arg299, and Val304
additional information
the 2S-naringenin substrate binding site of RtF3H1 consists of Ser135, Try149, Val214, Arg299, and Val304
additional information
the 2S-naringenin substrate binding site of RtF3H2 consists of Ser135, Phe149, Ile214, Arg299, and Ala305
additional information
the 2S-naringenin substrate binding site of RtF3H2 consists of Ser135, Phe149, Ile214, Arg299, and Ala305
additional information
three-dimensional protein structure modeling, overview
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recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
recombinant MBP-tagged enzyme from Escherichia coli BL21(DE3)pLysS by amylose affinity chromatography
Sephadex G25 column gel filtration
-
shock frozen fruits are ground in a mill, leaves are ground in liquid nitrogen in a mortar, protocol 1: plant material is homogenized in a mortar with quartz sand and Polyclar AT with extraction buffer (0.1 M Tris-HCl, pH 7.5, containing 0.4% sodium ascorbate) and centrifuged, or protocol 2 (optimized for polyphenol-rich tissues): plant material is homogenized with Polyclar AT in a mortar, transferred to a falcon tube containing Dowex in buffer (0.7 M KH2PO4/K2HPO4, pH 8.0, containing 0.4 M sucrose, 0.4 M sodium ascorbate, 1 mM CaCl2, 30 mM EDTA, 50 mM cysteine, 50 mM DIECA, 1.5% PEG 20000, and 0.1% BSA, kept under nitrogen atmosphere after removing oxygen by boiling), homogenate is filtered (glass wool) and centrifuged, supernatants obtained with both protocols are cleared of low molecular compounds by a Sephadex G25 gel chromatography column
shock frozen fruits are ground in a mill, leaves are ground in liquid nitrogen in a mortar, protocol 1: plant material is homogenized in a mortar with quartz sand and Polyclar AT with extraction buffer (0.1 M Tris-HCl, pH 7.5, containing 0.4% sodium ascorbate) and centrifuged, or protocol 2 (optimized for polyphenol-rich tissues): plant material is homogenized with Polyclar AT in a mortar, transferred to a falcon tube containing Dowex in buffer (0.7 M KH2PO4/K2HPO4, pH 8.0, containing 0.4 M sucrose, 0.4 M sodium ascorbate, 1 mM CaCl2, 30mM EDTA, 50 mM cysteine, 50 mM DIECA, 1.5% PEG 20000, and 0.1% BSA, kept under nitrogen atmosphere after removing oxygen by boiling), homogenate is filtered (glass wool) and centrifuged, supernatants obtained with both protocols are cleared of low molecular compounds by a Sephadex G25 gel chromatography column
-
wild-type and mutant enzymes
-
-
-
shock frozen fruits are ground in a mill, leaves are ground in liquid nitrogen in a mortar, protocol 1: plant material is homogenized in a mortar with quartz sand and Polyclar AT with extraction buffer (0.1 M Tris-HCl, pH 7.5, containing 0.4% sodium ascorbate) and centrifuged, or protocol 2 (optimized for polyphenol-rich tissues): plant material is homogenized with Polyclar AT in a mortar, transferred to a falcon tube containing Dowex in buffer (0.7 M KH2PO4/K2HPO4, pH 8.0, containing 0.4 M sucrose, 0.4 M sodium ascorbate, 1 mM CaCl2, 30 mM EDTA, 50 mM cysteine, 50 mM DIECA, 1.5% PEG 20000, and 0.1% BSA, kept under nitrogen atmosphere after removing oxygen by boiling), homogenate is filtered (glass wool) and centrifuged, supernatants obtained with both protocols are cleared of low molecular compounds by a Sephadex G25 gel chromatography column
-
shock frozen fruits are ground in a mill, leaves are ground in liquid nitrogen in a mortar, protocol 1: plant material is homogenized in a mortar with quartz sand and Polyclar AT with extraction buffer (0.1 M Tris-HCl, pH 7.5, containing 0.4% sodium ascorbate) and centrifuged, or protocol 2 (optimized for polyphenol-rich tissues): plant material is homogenized with Polyclar AT in a mortar, transferred to a falcon tube containing Dowex in buffer (0.7 M KH2PO4/K2HPO4, pH 8.0, containing 0.4 M sucrose, 0.4 M sodium ascorbate, 1 mM CaCl2, 30 mM EDTA, 50 mM cysteine, 50 mM DIECA, 1.5% PEG 20000, and 0.1% BSA, kept under nitrogen atmosphere after removing oxygen by boiling), homogenate is filtered (glass wool) and centrifuged, supernatants obtained with both protocols are cleared of low molecular compounds by a Sephadex G25 gel chromatography column
-
shock frozen fruits are ground in a mill, leaves are ground in liquid nitrogen in a mortar, protocol 1: plant material is homogenized in a mortar with quartz sand and Polyclar AT with extraction buffer (0.1 M Tris-HCl, pH 7.5, containing 0.4% sodium ascorbate) and centrifuged, or protocol 2 (optimized for polyphenol-rich tissues): plant material is homogenized with Polyclar AT in a mortar, transferred to a falcon tube containing Dowex in buffer (0.7 M KH2PO4/K2HPO4, pH 8.0, containing 0.4 M sucrose, 0.4 M sodium ascorbate, 1 mM CaCl2, 30 mM EDTA, 50 mM cysteine, 50 mM DIECA, 1.5% PEG 20000, and 0.1% BSA, kept under nitrogen atmosphere after removing oxygen by boiling), homogenate is filtered (glass wool) and centrifuged, supernatants obtained with both protocols are cleared of low molecular compounds by a Sephadex G25 gel chromatography column
-
shock frozen fruits are ground in a mill, leaves are ground in liquid nitrogen in a mortar, protocol 1: plant material is homogenized in a mortar with quartz sand and Polyclar AT with extraction buffer (0.1 M Tris-HCl, pH 7.5, containing 0.4% sodium ascorbate) and centrifuged, or protocol 2 (optimized for polyphenol-rich tissues): plant material is homogenized with Polyclar AT in a mortar, transferred to a falcon tube containing Dowex in buffer (0.7 M KH2PO4/K2HPO4, pH 8.0, containing 0.4 M sucrose, 0.4 M sodium ascorbate, 1 mM CaCl2, 30 mM EDTA, 50 mM cysteine, 50 mM DIECA, 1.5% PEG 20000, and 0.1% BSA, kept under nitrogen atmosphere after removing oxygen by boiling), homogenate is filtered (glass wool) and centrifuged, supernatants obtained with both protocols are cleared of low molecular compounds by a Sephadex G25 gel chromatography column
-
shock frozen fruits are ground in a mill, leaves are ground in liquid nitrogen in a mortar, protocol 1: plant material is homogenized in a mortar with quartz sand and Polyclar AT with extraction buffer (0.1 M Tris-HCl, pH 7.5, containing 0.4% sodium ascorbate) and centrifuged, or protocol 2 (optimized for polyphenol-rich tissues): plant material is homogenized with Polyclar AT in a mortar, transferred to a falcon tube containing Dowex in buffer (0.7 M KH2PO4/K2HPO4, pH 8.0, containing 0.4 M sucrose, 0.4 M sodium ascorbate, 1 mM CaCl2, 30 mM EDTA, 50 mM cysteine, 50 mM DIECA, 1.5% PEG 20000, and 0.1% BSA, kept under nitrogen atmosphere after removing oxygen by boiling), homogenate is filtered (glass wool) and centrifuged, supernatants obtained with both protocols are cleared of low molecular compounds by a Sephadex G25 gel chromatography column
-
shock frozen fruits are ground in a mill, leaves are ground in liquid nitrogen in a mortar, protocol 1: plant material is homogenized in a mortar with quartz sand and Polyclar AT with extraction buffer (0.1 M Tris-HCl, pH 7.5, containing 0.4% sodium ascorbate) and centrifuged, or protocol 2 (optimized for polyphenol-rich tissues): plant material is homogenized with Polyclar AT in a mortar, transferred to a falcon tube containing Dowex in buffer (0.7 M KH2PO4/K2HPO4, pH 8.0, containing 0.4 M sucrose, 0.4 M sodium ascorbate, 1 mM CaCl2, 30 mM EDTA, 50 mM cysteine, 50 mM DIECA, 1.5% PEG 20000, and 0.1% BSA, kept under nitrogen atmosphere after removing oxygen by boiling), homogenate is filtered (glass wool) and centrifuged, supernatants obtained with both protocols are cleared of low molecular compounds by a Sephadex G25 gel chromatography column
-
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cloned into the pGEM T-easy plasmid vector and transformed into DH5alpha Escherichia coli competent cells
enzyme expression analysis by real-time RT-PCR
-
expressed in Escherichia coli BL21Star and Rosetta(DE3) cells
-
expressed in Escherichia coli strain BLR (DE3)
expressed in yeast strain InvSc1
expression as glutathione S-transferase fusion protein
expression in a reticulocyte system
expression in Escherichia coli
expression in Escherichia coli JM109
expression in Escherichia coli Transetta (DE3)
expression in Saccharomyces cerevisiae
-
expression in wheat-rye hybrids
functional expression of plant-derived O-methyltransferase, flavanone 3-hydroxylase, and flavonol synthase in Corynebacterium glutamicum for production of pterostilbene, kaempferol, and quercetin
gene CtF3H, DNA and amino acid sequence determination and analysis, phylogenic analysis, quantitative real-time PCR enzyme expression analysis, functional recombinant expression of MBP-tagged enzyme in Escherichia coli BL21(DE3)pLysS from vector pMAL-C5x leading to production of dihydrokaempferol when naringenin is available the substrate. Recombinant expression of GFP-tagged enzyme in onion cells via transfromation of Agrobacterium tumefaciens strain GV3101, where it is localized both in the nucleus and in the cytosol
gene F3H cloned from petals, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis and tree, quantitative RT-PCR enzyme expression analysis, recombinant expression in Escherichia coli strain BL21
gene F3H, DNA and amino acid sequence determination and analysis, phylogenetic tree, semi-quantitative RT-PCR enzyme expression analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
-
gene F3H, DNA and amino acid sequence determination and analysis, sequence comparison and phylogenetic tree, quantitative real-time RT-PCR expression analysis
gene F3H, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, semi-quantitative RT-PCR enzyme expression analysis
gene F3H, functional recombinant expression of codon-optimized enzyme in Corynebacterium glutamicum strain DelAro4, coexpression with gene FLS encoding flavonol synthase from Populus deltoides. Coexpression fo genes F3H and FLS both from Petunia hybrida is not successful
gene F3H-B1 and a fourth gene F3H-B2, a nonhomologous duplication of F3H-B1, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree
gene F3H-D1, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree
gene F3H1, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, semi-quantitative RT-PCR enzyme expression analysis, functional recombinant expression in Escherichia coli, survival rate of the recombinant Escherichia coli strain expressing RtF3H2 is higher than that of the strain expressing RtF3H1 under salt and drought stresses
gene F3H2, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, semi-quantitative RT-PCR enzyme expression analysis, functional recombinant expression in Escherichia coli, survival rate of the recombinant Escherichia coli strain expressing RtF3H2 is higher than that of the strain expressing RtF3H1 under salt and drought stresses
gene F3H2, genotyping in Glycine max cultivars and accessions, phylogenetic analysis
-
gene F3H2, genotyping in Glycine soja cultivars and accessions, phylogenetic analysis
-
gene F3HA1, DNA and amiino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, a recognition site of bZIP-type transcription factor (bZIP911) occurs in the promoter of F3H-A1
gene fht, transcription profiling and quantitative real-time PCR expression analysis
-
gene LcF3H, DNA and amino acid sequence determination and analysis, phylogenetic analysis, quantitative PCR enzyme expression analysis, recombinant expression in Escherichia coli strain BL21(DE3), recombinant overexpression in leaves of Nicotiana tabacum cv. Xanthinc via transformation with Agrobacterium tumefaciens strain EHA105, overexpression of heterogenous LcF3H enhances the expression levels of downstream genes but does not cause alteration in the expression of upstream genes including endogenous F3H of Nicotiana tabacum. The enzyme's overexpression does cause a significant increase in the content of three major flavan-3-ols, catechin, epicatechin and epigallocatechin
gene PeF3H, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, semi-quantitative RT-PCR enzyme expression analysis, recombinant expression in Escherichia coli tsrain M15 pREP-4
gene PnF3H, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis and tree, quantitative real-time PCR enzyme expression analysis, functional recombinant expression in Arabidopsis thaliana ecotype Col-0 via Agrobacterium tumefaciens-mediated transformation conferring tolerance to salt stress and abscisic acid treatment in transgenic Arabidopsis, recombinant expression of GFP-tagged enzyme in Arabidopsis thaliana
-
gene VcF3H, DNA and amino acid sequence determination and analysis, sequence comparisons, quantitative RT-PCR enzyme expression analysis, recombinant expression in Arabidopsis thaliana increasing the anthocyanin content in leaves without increasing the flavonol content
genes SbF3H1 and SbF3H2, semi-quantitative RT-PCR expression analysis of flavonoid structural genes in sorghum seedlings, overview. Complementation of Arabidopsis thaliana flavonoid mutants by genes SbF3H1 and SbF3H2, complementation analysis, overview
overexpression of the Camellia sinensis flavanone 3-hydroxylase gene in leaves of transgenic Nicotiana tabacum cv. Xanthi confers tolerance to salt stress and pathogenic fungus Alternaria solani, transformation via Agrobacterium tumefaciens strain LBA4404 containing pCAMBIA-F3H. A decrease in pectin methyl esterase (PME) activity and increase in pectin methyl esterification is also observed in CsF3H transgenic tobacco plants. Transcript expression analysis, and analysis of trangenic PME activity in flavonoid (epigallocatechin)-exposed and -unexposed seedlings, and in seedlings exposed to salt
wild-type and mutant enzymes, expression in Escherichia coli
-
-
-
cloned into the pGEM T-easy plasmid vector and transformed into DH5alpha Escherichia coli competent cells
-
cloned into the pGEM T-easy plasmid vector and transformed into DH5alpha Escherichia coli competent cells
expressed in yeast strain InvSc1
-
expressed in yeast strain InvSc1
-
expression in a reticulocyte system
-
expression in a reticulocyte system
-
expression in Escherichia coli
-
expression in Escherichia coli
-
expression in Escherichia coli
expression in Escherichia coli
-
gene F3H, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, semi-quantitative RT-PCR enzyme expression analysis
gene F3H, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, semi-quantitative RT-PCR enzyme expression analysis
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Dangelmayr, B.; Stotz, G.; Spribille, R.; Forkmann, G.
Relationship between flower development, anthocyanin accumulation and activity of enzymes involved in flavonoid biosynthesis in Matthiola incana R.Br.
Z. Naturforsch. C
38
551-555
1983
Matthiola incana
-
brenda
Forkmann, G.; Stotz, G.
Genetic control of flavanone 3-hydroxylase activity and flavonoid 3'-hydroxylase activity in Antirrhinum majus (Snapdragon)
Z. Naturforsch. C
36
411-416
1981
Antirrhinum majus
-
brenda
Forkmann, G.; Heller, W.; Grisebach, H.
Anthocyanin biosynthesis in flowers of Matthiola incana flavanone 3- and flavonoid 3'-hydroxylases
Z. Naturforsch. C
35
691-695
1980
Matthiola incana
-
brenda
Britsch, L.
Purification and characterization of flavone synthase I, a 2-oxoglutarate-dependent desaturase
Arch. Biochem. Biophys.
282
152-160
1990
Petroselinum crispum
brenda
Britsch, L.
Purification of flavanone 3 beta-hydroxylase from Petunia hybrida: antibody preparation and characterization of a chemogenetically defined mutant
Arch. Biochem. Biophys.
276
348-354
1990
Petunia x hybrida
brenda
Beerhues, L.; Forkmann, G.; Schoepker, H.; Stotz, G.; Wiermann, R.
Flavanone 3-hydroxylase and dihydroflavonol oxygenase activities in anthers of Tulipa. The significance of the tapetum fraction in flavonoid metabolism
J. Plant Physiol.
133
743-746
1989
Tulipa hybrid cultivar
-
brenda
Takeda, K.; Fischer, D.; Grisebach, H.
Anthocyanin composition of Sinapis alba, light induction of enzymes and biosynthesis
Phytochemistry
27
1351-1353
1988
Sinapis alba
-
brenda
Britsch, L.; Grisebach, H.
Purification and characterization of (2S)-flavanone 3-hydroxylase from Petunia hybrida
Eur. J. Biochem.
156
569-577
1986
Petunia x hybrida
brenda
Forkmann, G.; Stotz, G.
Selection and characterisation of flavanone 3-hydroxylase mutants of Dahlia, Streptocarpus, Verbena and Zinnia
Planta
161
261-265
1984
Dahlia pinnata, Streptocarpus hybrida, Glandularia x hybrida, Zinnia elegans
brenda
Charrier, B.; Coronado, C.; Kondorosi, A.; Ratet, P.
Molecular characterization and expression of alfalfa (Medicago sativa L.) flavanone-3-hydroxylase and dihydroflavonol-4-reductase encoding genes
Plant Mol. Biol.
29
773-786
1995
Medicago sativa
brenda
O'Neill, S.D.; Tong, Y.; Spoerlein, B.; Forkmann, G.; Yoder, J.I.
Molecular genetic analysis of chalcone synthase in Lycopersicon esculentum and an anthocyanin-deficient mutant
Mol. Gen. Genet.
224
279-288
1990
Solanum lycopersicum
brenda
Lukacin, R.; Britsch, L.
Identification of strictly conserved histidine and arginine residues as part of the active site in Petunia hybrida flavanone 3beta-hydroxylase
Eur. J. Biochem.
249
748-757
1997
Petunia x hybrida
brenda
Lukacin, R.; Groning, I.; Pieper, U.; Matern, U.
Site-directed mutagenesis of the active site serine290 in flavanone 3beta-hydroxylase from Petunia hybrida
Eur. J. Biochem.
267
853-860
2000
Petunia x hybrida
brenda
Britsch, L.; Dedio, J.; Saedler, H.; Forkmann, G.
Molecular characterization of flavanone 3 beta-hydroxylases. Consensus sequence, comparison with related enzymes and the role of conserved histidine residues
Eur. J. Biochem.
217
745-754
1993
Antirrhinum majus, Callistephus chinensis, Dianthus caryophyllus, Hordeum vulgare, Matthiola incana, Petunia x hybrida
brenda
Lukacin, R.; Urbanke, C.; Groning, I.; Matern, U.
The monomeric polypeptide comprises the functional flavanone 3beta-hydroxylase from Petunia hybrida
FEBS Lett.
467
353-358
2000
Petunia x hybrida
brenda
Pelletier, M.K.; Shirley, B.W.
Analysis of flavanone 3-hydroxylase in Arabidopsis seedlings. Coordinate regulation with chalcone synthase and chalcone isomerase
Plant Physiol.
111
339-345
1996
Arabidopsis thaliana
brenda
Martens, S.; Forkmann, G.; Britsch, L.; Wellmann, F.; Matern, U.; Lukacin, R.
Divergent evolution of flavonoid 2-oxoglutarate-dependent dioxygenases in parsley
FEBS Lett.
544
93-98
2003
Petroselinum crispum (Q7XZQ7), Petroselinum crispum
brenda
Turnbull, J.J.; Nakajima, J.; Welford, R.W.; Yamazaki, M.; Saito, K.; Schofield, C.J.
Mechanistic studies on three 2-oxoglutarate-dependent oxygenases of flavonoid biosynthesis: anthocyanidin synthase, flavonol synthase, and flavanone 3beta-hydroxylase
J. Biol. Chem.
279
1206-1216
2004
Arabidopsis thaliana
brenda
Wellmann, F.; Matern, U.; Lukacin, R.
Significance of C-terminal sequence elements for Petunia flavanone 3beta-hydroxylase activity
FEBS Lett.
561
149-154
2004
Petunia x hybrida
brenda
Pelt, J.L.; Downes, W.A.; Schoborg, R.V.; McIntosh, C.A.
Flavanone 3-hydroxylase expression in Citrus paradisi and Petunia hybrida seedlings
Phytochemistry
64
435-444
2003
Citrus x paradisi, Petunia sp.
brenda
Miyahisa, I.; Funa, N.; Ohnishi, Y.; Martens, S.; Moriguchi, T.; Horinouchi, S.
Combinatorial biosynthesis of flavones and flavonols in Escherichia coli
Appl. Microbiol. Biotechnol.
71
53-58
2006
Citrus sinensis (Q9ZWR0)
brenda
Halbwirth, H.; Puhl, I.; Haas, U.; Jezik, K.; Treutter, D.; Stich, K.
Two-phase flavonoid formation in developing strawberry (Fragaria x ananassa) fruit
J. Agric. Food Chem.
54
1479-1485
2006
Fragaria x ananassa
brenda
Leonard, E.; Yan, Y.; Koffas, M.A.
Functional expression of a P450 flavonoid hydroxylase for the biosynthesis of plant-specific hydroxylated flavonols in Escherichia coli
Metab. Eng.
8
172-181
2006
Malus domestica
brenda
Halbwirth, H.; Fischer, T.C.; Schlangen, K.; Rademacher, W.; Schleifer, K.; Forkmann, G.; Stich, K.
Screening for inhibitors of 2-oxoglutarate-dependent dioxygenases: Flavanone 3?-hydroxylase and flavonol synthase
Plant Sci.
171
194-205
2006
Malus domestica, Pyrus communis
brenda
Kim, B.G.; Kim, J.H.; Kim, J.; Lee, C.; Ahn, J.H.
Accumulation of flavonols in response to ultraviolet-B irradiation in soybean is related to induction of flavanone 3-beta-hydroxylase and flavonol synthase
Mol. Cells
25
247-252
2008
Glycine max
brenda
Kim, J.H.; Lee, Y.J.; Kim, B.G.; Lim, Y.; Ahn, J.H.
Flavanone 3beta-hydroxylases from rice: key enzymes for favonol and anthocyanin biosynthesis
Mol. Cell
25
312-316
2008
Oryza sativa, Oryza sativa (Q7XR84), Oryza sativa (Q8W2X5)
brenda
Gebhardt, Y.H.; Witte, S.; Steuber, H.; Matern, U.; Martens, S.
Evolution of flavone synthase I from parsley flavanone 3beta-hydroxylase by site-directed mutagenesis
Plant Physiol.
144
1442-1454
2007
Petroselinum crispum
brenda
Owens, D.K.; Crosby, K.C.; Runac, J.; Howard, B.A.; Winkel, B.S.
Biochemical and genetic characterization of Arabidopsis flavanone 3beta-hydroxylase
Plant Physiol. Biochem.
46
833-843
2008
Arabidopsis thaliana
brenda
Singh, K.; Rani, A.; Kumar, S.; Sood, P.; Mahajan, M.; Yadav, S.K.; Singh, B.; Ahuja, P.S.
An early gene of the flavonoid pathway, flavanone 3-hydroxylase, exhibits a positive relationship with the concentration of catechins in tea (Camellia sinensis)
Tree Physiol.
28
1349-1356
2008
Camellia sinensis (Q6DV45), Camellia sinensis
brenda
Halbwirth, H.; Waldner, I.; Miosic, S.; Ibanez, M.; Costa, G.; Stich, K.
Measuring flavonoid enzyme activities in tissues of fruit species
J. Agric. Food Chem.
57
4983-4987
2009
Prunus avium, Prunus domestica, Rubus plicatus, Rubus idaeus, Sambucus nigra, Prunus cerasus, no activity in Actinidia deliciosa, Ribes uva-crispa
brenda
Cheng, H.; Yang, H.; Zhang, D.; Gai, J.; Yu, D.
Polymorphisms of soybean isoflavone synthase and flavanone 3-hydroxylase genes are associated with soybean mosaic virus resistance
Mol. Breed.
25
13-24
2009
Glycine soja, Glycine max (Q53B69)
-
brenda
Khlestkina, E.K.; Tereshchenko, O.Y.; Salina, E.A.
Anthocyanin biosynthesis genes location and expression in wheat-rye hybrids
Mol. Genet. Genomics
282
475-485
2009
Secale cereale (C7S853), Secale cereale
brenda
Hukkanen, A.; Kokko, H.; Buchala, A.; Haeyrinen, J.; Kaerenlampi, S.
Benzothiadiazole affects the leaf proteome in arctic bramble (Rubus arcticus)
Mol. Plant Pathol.
9
799-808
2008
Rubus arcticus
brenda
Zheng, Y.; Tian, L.; Liu, H.; Pan, Q.; Zhan, J.; Huang, W.
Sugars induce anthocyanin accumulation and flavanone 3-hydroxylase expression in grape berries
Plant Growth Regul.
58
251-260
2009
Vitis vinifera (P41090)
-
brenda
Eungwanichayapant, P.D.; Popluechai, S.
Accumulation of catechins in tea in relation to accumulation of mRNA from genes involved in catechin biosynthesis
Plant Physiol. Biochem.
47
94-97
2009
Camellia sinensis var. sinensis (Q6DV45)
brenda
Nakatsuka, A.; Mizuta, D.; Kii, Y.; Miyajima, I.; Kobayashi, N.
Isolation and expression analysis of flavonoid biosynthesis genes in evergreen azalea
Sci. Hortic.
118
314-320
2008
Rhododendron x pulchrum (A9ZMJ3)
-
brenda
Lovdal, T.; Olsen, K.M.; Slimestad, R.; Verheul, M.; Lillo, C.
Synergetic effects of nitrogen depletion, temperature, and light on the content of phenolic compounds and gene expression in leaves of tomato
Phytochemistry
71
605-613
2010
Solanum lycopersicum, Solanum lycopersicum Suzanne
brenda
Liu, H.; Du, Y.; Chu, H.; Shih, C.H.; Wong, Y.W.; Wang, M.; Chu, I.K.; Tao, Y.; Lo, C.
Molecular dissection of the pathogen-inducible 3-deoxyanthocyanidin biosynthesis pathway in sorghum
Plant Cell Physiol.
51
1173-1185
2010
Sorghum bicolor (D2Y4P1)
brenda
Himi, E.; Maekawa, M.; Noda, K.
Differential expression of three flavanone 3-hydroxylase genes in grains and coleoptiles of wheat
Int. J. Plant Genomics
2011
369460
2011
Triticum aestivum (C0SPH1), Triticum aestivum (C0SPH2), Triticum aestivum (C0SPH3), Triticum aestivum
brenda
Flachowsky, H.; Halbwirth, H.; Treutter, D.; Richter, K.; Hanke, M.V.; Szankowski, I.; Gosch, C.; Stich, K.; Fischer, T.C.
Silencing of flavanone-3-hydroxylase in apple (Malus x domestica Borkh.) leads to accumulation of flavanones, but not to reduced fire blight susceptibility
Plant Physiol. Biochem.
51
18-25
2012
Malus domestica
brenda
Liu, M.; Li, X.; Liu, Y.; Cao, B.
Regulation of flavanone 3-hydroxylase gene involved in the flavonoid biosynthesis pathway in response to UV-B radiation and drought stress in the desert plant, Reaumuria soongorica
Plant Physiol. Biochem.
73C
161-167
2013
Reaumuria songarica (H6WAT2)
brenda
Cheng, H.; Wang, J.; Chu, S.; Yan, H.L.; Yu, D.
Diversifying selection on flavanone 3-hydroxylase and isoflavone synthase genes in cultivated soybean and its wild progenitors
PLoS ONE
8
e54154
2013
Glycine max, Glycine soja
brenda
Flores, G.; de la Pena Moreno, F.; Blanch, G.P.; del Castillo, M.L.
Phenylalanine ammonia-lyase, flavanone 3beta-hydroxylase and flavonol synthase enzyme activity by a new in vitro assay method in berry fruits
Food Chem.
153
130-133
2014
Rubus plicatus, Rubus idaeus, Ribes nigrum, Ribes nigrum (A0A0C7DVW3), Ribes rubrum, Ribes rubrum (A0A172MJX5), Fragaria x ananassa (Q66ME9), Vaccinium myrtillus (Q8H249)
brenda
Kallscheuer, N.; Vogt, M.; Bott, M.; Marienhagen, J.
Functional expression of plant-derived O-methyltransferase, flavanone 3-hydroxylase, and flavonol synthase in Corynebacterium glutamicum for production of pterostilbene, kaempferol, and quercetin
J. Biotechnol.
258
190-196
2017
Petunia x hybrida (O22530), Petunia x hybrida (Q07512)
brenda
Li, Q.; Wang, J.; Sun, H.Y.; Shang, X.
Flower color patterning in pansy (Viola x wittrockiana Gams.) is caused by the differential expression of three genes from the anthocyanin pathway in acyanic and cyanic flower areas
Plant Physiol. Biochem.
84
134-141
2014
Viola x wittrockiana (A0A024CDL3)
brenda
Zhang, H.; Zhao, L.; Wang, J.; Zheng, L.; Dang, Z.; Wang, Y.
Cloning and functional analysis of two flavanone-3-hydroxylase genes from Reaumuria trigyna
Acta Physiol. Plant.
36
1221-1229
2014
Reaumuria trigyna (W0S9B2), Reaumuria trigyna (W0SDE6)
-
brenda
Tu, Y.; Liu, F.; Guo, D.; Fan, L.; Zhu, Z.; Xue, Y.; Gao, Y.; Guo, M.
Molecular characterization of flavanone 3-hydroxylase gene and flavonoid accumulation in two chemotyped safflower lines in response to methyl jasmonate stimulation
BMC Plant Biol.
16
132
2016
Carthamus tinctorius (M9MTF3), Carthamus tinctorius
brenda
Chaipanya, C.; Saetiew, K.; Arunyanart, S.; Parinthawong, N.
Isolation and expression analysis of the flavanone 3-hydroxylase genes in lotus (Nelumbo nucifera Gaertn.), waterlily (Nymphaea sp.) and transient silencing in waterlily
Chiang Mai J. Sci.
44
427-437
2017
Nelumbo nucifera (V9P4G8), Nymphaea hybrid cultivar (V9P4H2)
-
brenda
Zhang, C.; Guo, Q.; Liu, Y.; Liu, H.; Wang, F.; Jia, C.
Molecular cloning and functional analysis of a flavanone 3-hydroxylase gene from blueberry
J. Hortic. Sci. Biotechnol.
92
57-64
2017
Vaccinium myrtillus (Q8H249)
-
brenda
Kumar, A.; Singh, B.; Singh, K.
Functional characterization of flavanone 3-hydroxylase gene from Phyllanthus emblica (L.)
J. Plant Biochem. Biotechnol.
24
453-460
2015
Phyllanthus emblica (T1UPN7)
-
brenda
Khumkarjorn, N.; Thanonkeo, S.; Yamada, M.; Thanonkeo, P.
Cloning and expression analysis of a flavanone 3-hydroxylase gene in Ascocenda orchid
J. Plant Biochem. Biotechnol.
26
179-190
2017
x Ascocenda (J9QYL0), x Ascocenda NK-2012 (J9QYL0)
-
brenda
Li, C.; Liu, S.; Yao, X.; Wang, J.; Wang, T.; Zhang, Z.; Zhang, P.; Chen, K.
PnF3H, a flavanone 3-hydroxylase from the Antarctic moss Pohlia nutans, confers tolerance to salt stress and ABA treatment in transgenic Arabidopsis
Plant Growth Regul.
83
489-500
2017
Pohlia nutans
-
brenda
Mahajan, M.; Yadav, S.K.
Overexpression of a tea flavanone 3-hydroxylase gene confers tolerance to salt stress and Alternaria solani in transgenic tobacco
Plant Mol. Biol.
85
551-573
2014
Camellia sinensis (Q6DV45), Camellia sinensis, Camellia sinensis UPASI-10 (Q6DV45)
brenda
Xiong, S.; Tian, N.; Long, J.; Chen, Y.; Qin, Y.; Feng, J.; Xiao, W.; Liu, S.
Molecular cloning and characterization of a flavanone 3-hydroxylase gene from Artemisia annua L.
Plant Physiol. Biochem.
105
29-36
2016
Artemisia annua
brenda
Song, X.; Diao, J.; Ji, J.; Wang, G.; Guan, C.; Jin, C.; Wang, Y.
Molecular cloning and identification of a flavanone 3-hydroxylase gene from Lycium chinense, and its overexpression enhances drought stress in tobacco
Plant Physiol. Biochem.
98
89-100
2016
Lycium chinense (A0A068EM79), Lycium chinense
brenda
Singh, K.; Rani, A.; Kumar, S.; Sood, P.; Mahajan, M.; Yadav, S.K.; Singh, B.; Ahuja, P.S.
An early gene of the flavonoid pathway, flavanone 3-hydroxylase, exhibits a positive relationship with the concentration of catechins in tea (Camellia sinensis)
Tree Physiol.
28
1349-1356
2008
Camellia sinensis (Q6DV45), Camellia sinensis
brenda
Gao, G.; Chen, P.; Chen, J.; Chen, K.; Xiong, H.; Yu, C.; Zhu, A.
Expression profile of genes involved in ramie flavonoids biosynthesis pathway and regulation of flavanone 3-hydroxylase (BnF3H) in response to aquatic environment
Acta Physiol. Plant.
42
60
2020
Boehmeria nivea (A0A411KYJ9)
-
brenda
Sun, Y.J.; He, J.M.; Kong, J.Q.
Characterization of two flavonol synthases with iron-independent flavanone 3-hydroxylase activity from Ornithogalum caudatum Jacq
BMC Plant Biol.
19
195
2019
Albuca bracteata (A0A482LTA5), Albuca bracteata (A0A482LVU5), Albuca bracteata
brenda
Hammerbacher, A.; Kandasamy, D.; Ullah, C.; Schmidt, A.; Wright, L.P.; Gershenzon, J.
Flavanone-3-hydroxylase plays an important role in the biosynthesis of spruce phenolic defenses against bark beetles and their fungal associates
Front. Plant Sci.
10
208
2019
Picea abies (A0A481V8E6), Picea abies
brenda
Kaur, R.; Aslam, L.; Kapoor, N.; Mahajan, R.
Identification and comparative expression analysis of chalcone synthase, flavanone 3-hydroxylase and dihydroflavonol 4-reductase genes in wild pomegranate (Punica granatum L.) organs
Rev. Bras. Bot.
43
883-896
2020
Punica granatum (A0A2U7NZN9)
-
brenda