Any feedback?
Information on EC 1.14.11.9 - flavanone 3-dioxygenase
for references in articles please use BRENDA:EC1.14.11.9Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
1.14.11.9 flavanone 3-dioxygenaseIUBMB Comments
Requires Fe2+ and ascorbate. This plant enzyme catalyses an early step in the flavonoid biosynthesis pathway, leading to the production of flavanols and anthocyanins. Substrates include (2S)-naringenin, (2S)-eriodictyol, (2S)-dihydrotricetin and (2S)-pinocembrin. Some enzymes are bifuctional and also catalyse EC 1.14.20.6, flavonol synthase.
Specify your search results
Word Map
- 1.14.11.9
- chalcone
- anthocyanins
- dihydroflavonols
- flavonols
- anthocyanidin
-
4-reductase
-
ammonia-lyase
-
3\'-hydroxylase
- petunia
- proanthocyanidins
- dihydrokaempferol
-
leucoanthocyanidin
- 3-o-glucosyltransferase
-
2-oxoglutarate-dependent
-
3',5'-hydroxylase
-
r2r3-myb
- eriodictyol
- analysis
-
testa
-
udp-glucose:flavonoid
-
2s-flavanones
-
4-coumarate-coa
- dihydroflavonol-4-reductase
- dihydroquercetin
- 2s-naringenin
- pelargonidin
- synthesis
- agriculture
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
Synonyms
flavanone 3-hydroxylase, flavanone-3-hydroxylase, flavanone 3beta-hydroxylase, csf3h, lcf3h, aaf3h, ctf3h, naringenin 3-dioxygenase, acf3h, (2s)-flavanone 3-hydroxylase, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(2S)-flavanone 3-hydroxylase
-
-
-
-
AcF3H
CsF3H
F3H
FHT
FHTPH
-
-
-
-
flavanone 3-dioxygenase
flavanone 3-hydroxylase
flavanone 3beta-hydroxylase
flavanone synthase I
-
-
-
-
flavanone-3-hydroxylase
FS I
-
-
-
-
naringenin 3-dioxygenase
-
-
-
-
naringenin,2-oxoglutarate:oxygen oxidoreductase (3-hydroxylating)
-
-
-
-
oxygenase, flavanone 3-di-
-
-
-
-
F3H
-
-
-
-
flavanone 3-hydroxylase
-
-
-
-
flavanone 3beta-hydroxylase
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a (2S)-flavan-4-one + 2-oxoglutarate + O2 = a (2R,3R)-dihydroflavonol + succinate + CO2
enzyme catalyzes double-bond formation by direct abstraction of vicinal hydrogen atoms at C-2 and C-3 of the substrate
-
a (2S)-flavan-4-one + 2-oxoglutarate + O2 = a (2R,3R)-dihydroflavonol + succinate + CO2
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
(2S)-flavan-4-one,2-oxoglutarate:oxygen oxidoreductase (3-hydroxylating)
Requires Fe2+ and ascorbate. This plant enzyme catalyses an early step in the flavonoid biosynthesis pathway, leading to the production of flavanols and anthocyanins. Substrates include (2S)-naringenin, (2S)-eriodictyol, (2S)-dihydrotricetin and (2S)-pinocembrin. Some enzymes are bifuctional and also catalyse EC 1.14.20.6, flavonol synthase.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
75991-43-4
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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)-flavanone + 2-oxoglutarate + O2
(2R/3R)-dihydroflavonol + succinate + CO2
-
key step towards biosynthesis of flavonols, anthocyanins and catechins
-
-
?
(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
-
-
-
?
eriodyctiol + 2-oxoglutarate + O2
dihydroquercetin + succinate + CO2
-
-
-
-
?
naringenin + 2-oxoadipate + O2
dihydrokaempferol + pentanedioate + CO2
-
-
-
?
naringenin + 2-oxoglutarate + O2
dihydrokaempferol + succinate + O2 + 2 H2O
-
-
-
-
?
pinocembrin + 2-oxoglutarate + O2
?
-
38% of the activity with naringenin
-
-
?
(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
Camellia sinensis UPASI-10
-
-
-
?
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
x Ascocenda NK-2012
-
-
-
?
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
Camellia sinensis UPASI-10
-
-
-
?
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
Camellia sinensis UPASI-10
-
-
-
?
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
-
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.
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)-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
-
-
-
?
eriodyctiol + 2-oxoglutarate + O2
dihydroquercetin + 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
Camellia sinensis UPASI-10
-
-
-
?
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
x Ascocenda NK-2012
-
-
-
?
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
Camellia sinensis UPASI-10
-
-
-
?
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
Camellia sinensis UPASI-10
-
-
-
?
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
Iron
Fe2+
the flavanone 3beta-hydroxylase activity of OcFLS1 and OcFLS2 does not absolutely require iron. However, the presence of sufficient Fe2+ is conducive to successive catalysis of flavanones to flavonols
Fe2+
dependent on, required for catalysis, the ferrous iron binding site HxDxnH is formed by His78, His121, His211, Asp213, His221, Asp 223, His265, His267, and His279
Fe2+
required, amino acid residues His76, His218, Asp220 and His275 are involved in binding of the ferrous iron
Fe2+
required, two histidines and one aspartic acid of the pfam03171 motif are sites for putative iron binding
Iron
-
non-heme iron protein. His220, His278 and Asp222 constitute three of the possible ligands for iron binding in the active site of the enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
sodium 4,6-dioxo-2,2-dimethyl-5-(1-alloxyamino-butylidene)-cyclohexane-1-carboxylic acid methyl ester
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
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
diethyldicarbonate
-
0.5 mM, 10% inhibition; 2 mM, complete inhibition; slight
EDTA
0.2 M, complete loss of activity; 0.2 M, complete loss of activity; 0.2 M, complete loss of activity
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
sodium 4,6-dioxo-2,2-dimethyl-5-(1-alloxyamino-butylidene)-cyclohexane-1-carboxylic acid methyl ester
additional information
sugars induce anthocyanin accumulation and flavanone 3-hydroxylase expression in grape berries. Glucosamine and mannoheptulose, the specific inhibitors of hexokinase, block the activation induced by sugar on both anthocyanin accumulation and F3H expression
-
pyridine-2,3-dicarboxylic acid
-
1 mM 205% relative activity, 0.1 mM 120% relative activity
pyridine-2,3-dicarboxylic acid
-
1 mM 205% relative activity, 0.1 mM 120% relative activity
pyridine-2,6-dicarboxylic acid
-
1 mM 220% relative activity, 0.1 mM 186% relative activity
pyridine-2,6-dicarboxylic acid
-
1 mM 220% relative activity, 0.1 mM 186% relative activity
pyridine-2,6-dicarboxylic acid chloride
-
1 mM, 196% relative activity, 0.1 mM 194% relative activity
pyridine-2,6-dicarboxylic acid chloride
-
1 mM, 196% relative activity, 0.1 mM 194% relative activity
sodium 4,6-dioxo-2,2-dimethyl-5-(1-alloxyamino-butylidene)-cyclohexane-1-carboxylic acid methyl ester
-
0.1 mM 115% relative activity
sodium 4,6-dioxo-2,2-dimethyl-5-(1-alloxyamino-butylidene)-cyclohexane-1-carboxylic acid methyl ester
-
0.1 mM 115% relative activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Infections
Overexpression of a tea flavanone 3-hydroxylase gene confers tolerance to salt stress and Alternaria solani in transgenic tobacco.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
Km-values of mutant enzymes
-
additional information
additional information
-
varying Km-values, depending on the purification procedure
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0000026
-
unripe fruit: 43 nkat/kg total protein (enzyme extraction protocol 2)
0.0000079
-
ripe fruit: 131 nkat/kg total protein (enzyme extraction protocol 2), no activity with enzyme extraction protocol 1
0.000012
0.000015
-
unripe fruit: 242 nkat/kg total protein (enzyme extraction protocol 1)
0.000019
-
leaves: 316 nkat/kg total protein (enzyme extraction protocol 1), no activity with enzyme extraction protocol 2
0.000023
-
ripe fruit: 388 nkat/kg total protein (enzyme extraction protocol 1)
0.000026
-
unripe fruit: 440 nkat/kg total protein (enzyme extraction protocol 2), no activity with enzyme extraction protocol 1
0.000027
-
ripe fruit: 443 nkat/kg total protein (enzyme extraction protocol 2)
0.000029
-
ripe fruit: 484 nkat/kg total protein (enzyme extraction protocol 2)
0.000041
0.00005
-
unripe fruit: 833 nkat/kg total protein (enzyme extraction protocol 2), no activity with enzyme extraction protocol 1
0.000062
-
unripe fruit: 1039 nkat/kg total protein (enzyme extraction protocol 2)
0.000066
-
leaves: 1105 nkat/kg total protein (enzyme extraction protocol 2), no activity with enzyme extraction protocol 1
0.000092
-
ripe fruit: 1537 nkat/kg total protein (enzyme extraction protocol 2), no activity with enzyme extraction protocol 1
0.00012
-
leaves: 1933 nkat/kg total protein (enzyme extraction protocol 2), no activity with enzyme extraction protocol 1
0.00026
-
unripe fruit: 4400 nkat/kg total protein (enzyme extraction protocol 2), no activity with enzyme extraction protocol 1
0.0009
-
ripe fruit: 15072 nkat/kg total protein (enzyme extraction protocol 1)
0.00094
-
ripe fruit: 15652 nkat/kg total protein (enzyme extraction protocol 2)
additional information
0.000012
-
unripe fruit: 196 nkat/kg total protein (enzyme extraction protocol 1)
0.000041
-
leaves: 690 nkat/kg total protein (enzyme extraction protocol 1), no activity with enzyme extraction protocol 2
0.000041
-
ripe fruit: 688 nkat/kg total protein (enzyme extraction protocol 1)
additional information
-
no activity in leaves, whether with enzyme extraction protocol 1 or 2
additional information
-
no activity in ripe fruit, whether with enzyme extraction protocol 1 or 2
additional information
-
no activity in unripe fruit, whether with enzyme extraction protocol 1 or 2
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.25
7.3
8.5
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 8
pH 5.0: about 75% of maximal activity, pH 8.0: about 40% of maximal activity
5 - 9
pH 5.0: about 40% of maximal activity, pH 9.0: about 50% of maximal activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
35
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0 - 43
0°C: about 80% of maximal activity, 45°C: about 75% of maximal activity
5 - 50
5°C: about 90% of maximal activity, 50°C: about 50% of maximal activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.6
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Camellia sinensis UPASI-10
from the tea garden at the CSIR-Institute of Himalayan Bioresource Technology, Palampur
UniProt
brenda
a quinochalcone-type safflower line with orange-yellow flowers and a flavonol-type safflower line with white flowers, i.e. ZHH0119 line and XHH007 line, respectively
UniProt
brenda
enzyme is present in cyanic strain, absent in acyanic strain
-
-
brenda
cv. Buntharik (white petal lotus) and cv. Satabankacha (pink petal lotus)
UniProt
brenda
no activity in Actinidia deliciosa
ten year old healthy tree growing in the botanical garden of Panjab University, Chandigarh, India under natural conditions
UniProt
brenda
collected from the Eastern Alxa-Western Ordos area in Inner Mongolia, China
UniProt
brenda
Streptocarpus hybrida
enzyme is present in cyanic strain, absent in acyanic strain
-
-
brenda
from the tea garden at the CSIR-Institute of Himalayan Bioresource Technology, Palampur
UniProt
brenda
cv. Wye, 33 Chinese soybean accessions including 16 Glycine soja and 17 Glycine max
UniProt
brenda
33 Chinese soybean accessions including 16 Glycine soja and 17 Glycine max
-
-
brenda
no activity in Actinidia deliciosa
kiwi fruit, cultivar Hayward, ripe fruit and leaves
-
-
brenda
gene F3H-B1; diverse wheat lines, F3H gene F3H-B1, and a fourth gene F3H-B2, a nonhomologous duplication of F3H-B1
UniProt
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
the transcriptome expression of CtF3H shows a diametrically opposed expression pattern in a quinochalcone-type safflower line (with orange-yellow flowers) and a flavonol-type safflower line (with white flowers) under external stimulation by methyl jasmonate (MeJA), which has been identified as an elicitor of flavonoid metabolites. High expression of CtF3H in quinochalcone-type safflower line
brenda
enzyme expression analysis of AcF3H at different developmental stages and in different parts of the flower, overview. The highest enzyme expression occurs when the petals turned pale-orange
brenda
x Ascocenda NK-2012
-
enzyme expression analysis of AcF3H at different developmental stages and in different parts of the flower, overview. The highest enzyme expression occurs when the petals turned pale-orange
-
brenda
increase in transcript level of PgF3H with respect to the growth of the fruits
brenda
positive correlation between the concentration of catechins and the expression of flavonol 3-hydroxylase in different developmental stages. Expression is down-regulated in response to drought and gibberellic acid treatment, but up-regulated in response to wounding
brenda
positive correlation between the concentration of catechins and F3H expression in leaves of different developmental stages
brenda
-
high level of expression in primary leaves of 32 day old seedlings
brenda
primordial leaf, young leaf (highest level), and mature leaf
brenda
high transcript levels of gene RtF3H2 in roots and stems
brenda
-
enzyme shows a drastic increase in activity after illumination and reaches a maximum at the time of rapid anthocyanin accumulation
brenda
high transcript levels of gene RtF3H1 in stems, high transcript levels of gene RtF3H2 in roots and stems
brenda
additional information
-
the AaF3H transcripts are accumulated in the cultivar with higher level of flavonoids than that with lower level of flavonoids
brenda
additional information
tissue pattern of enzyme expression, overview
brenda
additional information
-
tissue pattern of enzyme expression, overview
brenda
additional information
expression of F3H is specifically regulated in petals and stamens. The F3H expression is slightly diminished in petals of cultivar Satabankacha at the fully-opening stage, whereas it is detected in the cultivar Buntharik only when white petals are tinted with pink.
brenda
additional information
-
protein content of the enzyme in the different plants and tissue preparations obtained with two different protocols
brenda
additional information
-
no activity in leaves, protein content of the enzyme in the different plants and tissue preparations obtained with two different protocols
brenda
additional information
-
protein content of the enzyme in the different plants and tissue preparations obtained with two different protocols
brenda
additional information
-
protein content of the enzyme in the different plants and tissue preparations obtained with two different protocols
brenda
additional information
-
protein content of the enzyme in the different plants and tissue preparations obtained with two different protocols
brenda
additional information
-
protein content of the enzyme in the different plants and tissue preparations obtained with two different protocols
brenda
additional information
-
protein content of the enzyme in the different plants and tissue preparations obtained with two different protocols
brenda
additional information
the F3H gene is highly activated in the red grains and coleoptiles, no expression in white grains
brenda
additional information
the F3H gene is highly activated in the red grains and coleoptiles, no expression in white grains
brenda
additional information
the F3H gene is highly activated in the red grains and coleoptiles, no expression in white grains
brenda
additional information
-
the F3H gene is highly activated in the red grains and coleoptiles, no expression in white grains
brenda
additional information
the F3H gene is highly activated in the red grains and coleoptiles, only slight expression in white grains
brenda
additional information
the F3H gene is highly activated in the red grains and coleoptiles, only slight expression in white grains
brenda
additional information
the F3H gene is highly activated in the red grains and coleoptiles, only slight expression in white grains
brenda
additional information
-
the F3H gene is highly activated in the red grains and coleoptiles, only slight expression in white grains
brenda
additional information
tissue enzyme expression pattern analysis, the enzyme is ubiquitously expressed
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
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
metabolism
physiological function
additional information
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 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
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
Camellia sinensis UPASI-10
-
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
Show AA Sequence and Transmembrane Helices (247 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
42700
68000
-
x * 42700, calculated, x * 68000, SDS-PAGE of fusion protein with glutathione S-transferase
42700
-
x * 42700, calculated, x * 68000, SDS-PAGE of fusion protein with glutathione S-transferase
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
?
x * 40720, sequence calculation, x * 40000, recombinant detagged enzyme, SDS-PAGE
?
-
x * 42700, calculated, x * 68000, SDS-PAGE of fusion protein with glutathione S-transferase
?
x * 41220, sequence calculation, x * 41500, recombinant enzyme, SDS-PAGE
additional information
-
enzyme exists as functional monomeric and oligomeric forms. The monomeric polypeptide comprises the catalytically active flavanone 3beta-hydroxylase
additional information
three-dimensional protein structure modeling, overview. F3H has a jelly roll in the enzyme core, a typical structure shared by all 2-oxoglutarate-dependent dioxygenases including F3Hs. Position between 194 and 295 amino acids represent the 2-oxoglutarate-ferrous(II) oxygenase superfamily domain which plays key role in catalyzing a redox reaction
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotecnology
-
AaF3H is a potential target for regulation of flavonoids biosynthesis in Artemisia annua through metabolic engineering
D195E
-
mutant constructed to confer flavone synthase activity to flavanone 3beta-hydroxylase. Substrate naringenin is completely converted to flavanone 3beta-hydroxylase product dihydrokaempferol
D195E/L215V/K216R
-
mutant constructed to confer flavone synthase activity to flavanone 3beta-hydroxylase. Substrate naringenin is completely converted to flavanone 3beta-hydroxylase product dihydrokaempferol
I115T
-
mutant constructed to confer flavone synthase activity to flavanone 3beta-hydroxylase. Substrate naringenin is completely converted to flavanone 3beta-hydroxylase product dihydrokaempferol
I115T/V116I
-
mutant constructed to confer flavone synthase activity to flavanone 3beta-hydroxylase. Substrate naringenin is completely converted to flavanone 3beta-hydroxylase product dihydrokaempferol
I115T/V116I/I131F/D195E
-
mutant constructed to confer flavone synthase activity to flavanone 3beta-hydroxylase. Substrate naringenin is converted to 76% flavanone 3beta-hydroxylase product dihydrokaempferol and to 24% flavone synthase product apigenin
I131F
-
mutant constructed to confer flavone synthase activity to flavanone 3beta-hydroxylase. Substrate naringenin is completely converted to flavanone 3beta-hydroxylase product dihydrokaempferol
I131F/D195E
-
mutant constructed to confer flavone synthase activity to flavanone 3beta-hydroxylase. Substrate naringenin is completely converted to flavanone 3beta-hydroxylase product dihydrokaempferol
I131F/D195E/L215V/K216R
-
mutant constructed to confer flavone synthase activity to flavanone 3beta-hydroxylase. Substrate naringenin is converted to 69% flavanone 3beta-hydroxylase product dihydrokaempferol and to 31% flavone synthase product apigenin
I131F/L215V/K216R
-
mutant constructed to confer flavone synthase activity to flavanone 3beta-hydroxylase. Substrate naringenin is converted to 78% flavanone 3beta-hydroxylase product dihydrokaempferol and to 22% flavone synthase product apigenin
L215V/K216R
-
mutant constructed to confer flavone synthase activity to flavanone 3beta-hydroxylase. Substrate naringenin is completely converted to flavanone 3beta-hydroxylase product dihydrokaempferol
M106T
-
mutant constructed to confer flavone synthase activity to flavanone 3beta-hydroxylase. Substrate naringenin is completely converted to flavanone 3beta-hydroxylase product dihydrokaempferol
M106T/I115T/V116I/I131F/D195E
-
mutant constructed to confer flavone synthase activity to flavanone 3beta-hydroxylase. Substrate naringenin is converted to 66% flavanone 3beta-hydroxylase product dihydrokaempferol and to 34% flavone synthase product apigenin
M106T/I115T/V116I/I131F/D195E/L215V/K216R
-
mutant constructed to confer flavone synthase activity to flavanone 3beta-hydroxylase. Substrate naringenin is converted to 18% flavanone 3beta-hydroxylase product dihydrokaempferol and to 82% flavone synthase product apigenin
M106T/I131F/D195E
-
mutant constructed to confer flavone synthase activity to flavanone 3beta-hydroxylase. Substrate naringenin is converted to 85% flavanone 3beta-hydroxylase product dihydrokaempferol and to 15% flavone synthase product apigenin
H220Q
-
catalytic activity is reduced to about 0.15% of that of the wild-type enzyme. Slightly increased Km-value with respect to iron binding, as compared to the wild-type enzyme
N222N
-
catalytic activity is reduced to about 0.15% of that of the wild-type enzyme. Slightly increased Km-value with respect to iron binding, as compared to the wild-type enzyme
R288K
-
decrease in catalytic activity and a 5fold increase in Km-value for 2-oxoglutarate
R288Q
-
decrease in catalytic activity and a 160fold increase in Km-value for 2-oxoglutarate
additional information
additional information
-
in mutants lacking flavanone 3beta-hydroxylase, the enzymes flavonol synthase EC 1.14.11.23, and anthocyanidin synthase, EC 1.14.11.19, can partially compensate for its activity in vivo
additional information
-
F3H silencing by fht antisense transgenic apple clones construction, diverse transgenic lines, phenotypes, overview
additional information
method evaluation for RNAi-mediated silencing downregulation of F3H expression, vector pJA8F3H is efficient and can be used as a transformation vector to transiently suppress F3H expression in waterlily or lotus
additional information
method evaluation for RNAi-mediated silencing downregulation of F3H expression, introduction of RNAi gene-silencing vector, pJA8F3H, encoding a hairpin F3H RNA, to waterlily petals using the Agrobacterium tumefaciens strain GV3101 infiltration method, F3H expression is analysed at 1 and 3 days post infiltration semi-quantitative RT-PCR, showing that F3H expression is downregulated at 3 dpi in flowers tested of the red petal variety and purplish blue petal variety compared to controls. Vector pJA8F3H is efficient and can be used as a transformation vector to transiently suppress F3H expression in waterlily or lotus
additional information
-
domain swapping experiments joining the N-terminus of flavanone 3beta-hydroxylase with the C-terminus of flavone synthase I and vice versa. Active site residues of flavanone 3beta-hydroxylase are M106, I115, V116, I131, D195, V200, L215, and K216
additional information
-
four C-terminally truncated enzyme forms are generated by deletion of five, 11, 24 or 29 amino acids. The recombinant enzymes preserve their substrate electrivity, but the specific activity decreases gradually with the extent of truncation. An enzyme chimera is constructed by domain swapping replacing the C-terminal 52 amino acids of the Petunia enzyme by equivalent region of flavonol synthase from Citrus unshiu
additional information
the enzyme is ngineered for synthesizing polyphenol core structuressuch as the stilbene resveratrol and the (2S)-flavanone naringenin
additional information
the enzyme is ngineered for synthesizing polyphenol core structuressuch as the stilbene resveratrol and the (2S)-flavanone naringenin
additional information
-
construction of transgenic Arabidospis thaliana plants expressing the enzyme from Pohlia nutans, the Agrobacterium tumefaciens-mediated transformation of gene PnF3H confers tolerance to salt stress and abscisic acid treatment in transgenic Arabidopsis, naringenin-feeding experiments and flavonoid metabolism profiling by HPLC analysis, phenotype, overview
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 50
recombinant enzyme, stable at 20-45°C, loss of activity above 45°C, inactivation at 60°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
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
-
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloned into the pGEM T-easy plasmid vector and transformed into DH5alpha Escherichia coli competent cells
expressed in yeast strain InvSc1
expression in a reticulocyte system
expression in Escherichia coli
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
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
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.
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
downregulation of flavanone 4-reductase leads to upregulation of other flavanoid pathway genes, inclunding the flavanone 3-hydroxylase, feedback regulation of flavonoid gene expression, overview
-
expression is down-regulated in response to drought, abscisic acid and gibberellic acid treatment
flavanone 3-hydroxylase expression increases in response to N depletion, in agreement with a corresponding increase in flavonoid and caffeoyl content in tomato leaves, and/or to lower temperatures, overview. The effects of N depletion are apparently mediated through the overall regulators of the pathway the MYB transcription factor ANT1, ANTHOCYANIN 1, and SlJAF13, a bHLH transcription factor orthologue of petunia JAF13 and maize RED genes
increase in transcript level of PgF3H with respect to the growth of the fruits
PnF3H expression levels increase by 2.49fold at 1 h and then slightly decrease to 1.47fold at 24 h with cold treatment. For the simulated drought stress (i.e. 20% PEG 6000), the PnF3H expression levels enhance by 2.39fold at 3 h and the transcript abundance remains high up to 12 h. In the UV-B radiation, the PnF3H expression levels increase and reach the maximum level of 4.57fold at 3 h. After exogenous abscisic acid treatment, the PnF3H expression levels increase quickly and reach the maximum level of 2.57fold at 0.5 h
-
positive correlation between absisic acid and LcF3H expression level
rapid increase in gene expression of RsF3H under stress, both UV-B radiation and drought stress induce an increase in RsF3H enzyme activity and the accumulation of the products in the flavonoid biosynthetic pathway (total flavonoid and anthocyanin), overview
the enzyme flavanone 3-hydroxylase is induced by methyl jasmonate. Further metabolite analysis shows the increasing tendency of quinochalcones and flavonols, such as hydroxysafflor yellow A, kaempferol-3-O-beta-D-glucoside, kaempferol-3-O-beta-rutinoside, rutin, carthamin, and luteolin, in the quinochalcone-type safflower line. Also, the accumulation of kaempferol-3-O-beta-rutinoside and kaempferol-3-O-beta-D-glucoside in flavonols-typed safflower line shows enhanced accumulation pattern after methyl jasmonate treatment. Other flavonols, such as kaempferol, dihydrokaempferol and quercetin-3-O-beta-D-glucoside, in flavonols-typed safflower line present downregulation in respons to the methyl jasmonate stimulus
the enzyme is significantly up-regulated in the roots of hydroponic Boehmeria nivea, and higher total flavonoids content in the hydroponic ramie roots is also observed
the transcript levels of LcF3H shows significant decrease when plants are treated by exogenous nordihydroguaiaretic acid (100 mM) application together with drought stress treatment comparing to that treated with drought stress alone, the decrease in LcF3H expression under drought stress is less in overexpressing lines compared to the control plants
transcript levels of the two F3H genes, RtF3H1 and RtF3H2, are increased in Reaumuria trigyna not only under salt stress but also under drought and cold stresses, and by abscisic acid
flavanone 3-hydroxylase expression increases in response to N depletion, in agreement with a corresponding increase in flavonoid and caffeoyl content in tomato leaves, and/or to lower temperatures, overview. The effects of N depletion are apparently mediated through the overall regulators of the pathway the MYB transcription factor ANT1, ANTHOCYANIN 1, and SlJAF13, a bHLH transcription factor orthologue of petunia JAF13 and maize RED genes
-
flavanone 3-hydroxylase expression increases in response to N depletion, in agreement with a corresponding increase in flavonoid and caffeoyl content in tomato leaves, and/or to lower temperatures, overview. The effects of N depletion are apparently mediated through the overall regulators of the pathway the MYB transcription factor ANT1, ANTHOCYANIN 1, and SlJAF13, a bHLH transcription factor orthologue of petunia JAF13 and maize RED genes
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
analysis
synthesis
additional information
F3H gene may be used as biomarker in tea breeding programs and genetic engineering to improve tea quality
agriculture
basis for further research on the control of berry skin color and wine quality
agriculture
-
the aim is to identify the soybean mosaic virus resistance associated single nucleotide polymorphism in the IFS1, IFS2 and F3H gene by association mapping in order to develop valuable genetic markers for future soybean mosaic virus resistance breeding efforts in soybean
agriculture
the aim is to identify the soybean mosaic virus resistance associated single nucleotide polymorphism in the IFS1, IFS2 and F3H gene by association mapping in order to develop valuable genetic markers for future soybean mosaic virus resistance breeding efforts in soybean
analysis
-
an HPLC method for the determination of phenylalanine ammonia-lyase, flavanone 3-hydroxylase and flavonol synthase enzyme activity is proposed. This method is based on the determination of the compounds produced and consumed on the enzymatic reaction in just one chromatographic analysis. Optimisation of the method consideres kinetic studies to establish the incubation time to perform the assay. The method is an approach to measure the activities of the three enzymes simultaneously increasing the rapidity, selectivity and sensitivity over other exiting methods
analysis
-
an HPLC method for the determination of phenylalanine ammonia-lyase, flavanone 3-hydroxylase and flavonol synthase enzyme activity is proposed. This method is based on the determination of the compounds produced and consumed on the enzymatic reaction in just one chromatographic analysis. Optimisation of the method consideres kinetic studies to establish the incubation time to perform the assay. The method is an approach to measure the activities of the three enzymes simultaneously increasing the rapidity, selectivity and sensitivity over other exiting methods
analysis
an HPLC method for the determination of phenylalanine ammonia-lyase, flavanone 3-hydroxylase and flavonol synthase enzyme activity is proposed. This method is based on the determination of the compounds produced and consumed on the enzymatic reaction in just one chromatographic analysis. Optimisation of the method consideres kinetic studies to establish the incubation time to perform the assay. The method is an approach to measure the activities of the three enzymes simultaneously increasing the rapidity, selectivity and sensitivity over other exiting methods
analysis
an HPLC method for the determination of phenylalanine ammonia-lyase, flavanone 3-hydroxylase and flavonol synthase enzyme activity is proposed. This method is based on the determination of the compounds produced and consumed on the enzymatic reaction in just one chromatographic analysis. Optimisation of the method consideres kinetic studies to establish the incubation time to perform the assay. The method is an approach to measure the activities of the three enzymes simultaneously increasing the rapidity, selectivity and sensitivity over other exiting methods
analysis
an HPLC method for the determination of phenylalanine ammonia-lyase, flavanone 3-hydroxylase and flavonol synthase enzyme activity is proposed. This method is based on the determination of the compounds produced and consumed on the enzymatic reaction in just one chromatographic analysis. Optimisation of the method consideres kinetic studies to establish the incubation time to perform the assay. The method is an approach to measure the activities of the three enzymes simultaneously increasing the rapidity, selectivity and sensitivity over other exiting methods
synthesis
functional expression of plant-derived O-methyltransferase, flavanone 3-hydroxylase, and flavonol synthase in Corynebacterium glutamicum for production of pterostilbene, kaempferol, and quercetin
synthesis
expression of heterologous dioxygenase genes in (2S)-flavanone-producing Corynebacterium glutamicum strains enables the production of flavanonols and flavonols, e.g kaempferol and quercetin, starting from thephenylpropanoids p-coumaric acid and caffeic acid
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Select items on the left to see more content.
EXTERNAL LINKS (specific for EC-Number 1.14.11.9)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
