Information on EC 1.14.11.9 - flavanone 3-dioxygenase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.14.11.9
-
RECOMMENDED NAME
GeneOntology No.
flavanone 3-dioxygenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
a (2S)-flavan-4-one + 2-oxoglutarate + O2 = a (2R,3R)-dihydroflavonol + succinate + CO2
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
flavonoid biosynthesis
-
-
flavonoid biosynthesis (in equisetum)
-
-
leucodelphinidin biosynthesis
-
-
leucopelargonidin and leucocyanidin biosynthesis
-
-
pinobanksin biosynthesis
-
-
Flavonoid biosynthesis
-
-
Metabolic pathways
-
-
Biosynthesis of secondary metabolites
-
-
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 1.14.11.23, flavonol synthase.
CAS REGISTRY NUMBER
COMMENTARY hide
75991-43-4
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
from the tea garden at the CSIR-Institute of Himalayan Bioresource Technology, Palampur
UniProt
Manually annotated by BRENDA team
cultivar Oolong No. 17
UniProt
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
-
TrEMBL
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
enzyme is present in cyanic strain, absent in acyanic strain
-
-
Manually annotated by BRENDA team
enzyme is present in cyanic strain, absent in acyanic strain
-
-
Manually annotated by BRENDA team
gene F3H
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
cv. Buntharik (white petal lotus) and cv. Satabankacha (pink petal lotus)
UniProt
Manually annotated by BRENDA team
no activity in Actinidia deliciosa
green-fleshed cultivar Hayward; kiwi fruit, cultivar Hayward, ripe fruit and leaves
-
-
Manually annotated by BRENDA team
var. St. Louis Gold
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
ten year old healthy tree growing in the botanical garden of Panjab University, Chandigarh, India under natural conditions
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
cultivar Augustkirsche, cherry; cv. Augustkirsche
-
-
Manually annotated by BRENDA team
cultivar Pandy 114, sour cherry; cv. Pandy 114
-
-
Manually annotated by BRENDA team
; plum
-
-
Manually annotated by BRENDA team
cultivars Pyrodwarf and Conference
-
-
Manually annotated by BRENDA team
collected from the Eastern Alxa-Western Ordos area in Inner Mongolia, China
UniProt
Manually annotated by BRENDA team
; gooseberry
-
-
Manually annotated by BRENDA team
cv. Mespi
-
-
Manually annotated by BRENDA team
; elder
-
-
Manually annotated by BRENDA team
fragment; rye Imperial and Monstrous
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
structural gene F3H
-
-
Manually annotated by BRENDA team
two structural genes SbF3H1 and SbF3H2
UniProt
Manually annotated by BRENDA team
Streptocarpus hybrida
enzyme is present in cyanic strain, absent in acyanic strain
-
-
Manually annotated by BRENDA team
c.v. Apeldoorn
-
-
Manually annotated by BRENDA team
Mengdie
UniProt
Manually annotated by BRENDA team
L. cv. Cabernet Sauvignon
UniProt
Manually annotated by BRENDA team
xAscocenda
var. Subun
UniProt
Manually annotated by BRENDA team
xAscocenda NK-2012
var. Subun
UniProt
Manually annotated by BRENDA team
enzyme is present in cyanic strain, absent in acyanic strain
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
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
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(2S)-flavanone + 2-oxoglutarate + O2
(2R/3R)-dihydroflavonol + succinate + CO2
show the reaction diagram
-
key step towards biosynthesis of flavonols, anthocyanins and catechins
-
-
?
(2S)-naringenin + 2-oxoglutarate + O2
(2R,3R)-dihydrokaempferol + succinate + CO2
show the reaction diagram
(S)-eriodictyol + 2-oxoglutarate + O2
(2R,3R)-dihydroquercetin + succinate + CO2
show the reaction diagram
-
-
-
?
3'-methoxy eriodictyol + 2-oxoglutarate + O2
? + succinate + CO2
show the reaction diagram
4'-methoxy eriodictyol + 2-oxoglutarate + O2
? + succinate + CO2
show the reaction diagram
a (2S)-flavan-4-one + 2-oxoglutarate + O2
a (2R,3R)-dihydroflavonol + succinate + CO2
show the reaction diagram
a flavanone + 2-oxoglutarate + O2
a dihydroflavonol + succinate + CO2
show the reaction diagram
eriodictyol + 2-oxoglutarate + O2
(2R,3R)-dihydroquercetin + succinate + CO2
show the reaction diagram
eriodictyol + 2-oxoglutarate + O2
dihydroquercetin + succinate + CO2
show the reaction diagram
eriodyctiol + 2-oxoglutarate + O2
dihydroquercetin + succinate + CO2
show the reaction diagram
-
-
-
-
?
naringenin + 2-oxoadipate + O2
dihydrokaempferol + pentanedioate + CO2
show the reaction diagram
-
-
-
?
naringenin + 2-oxoglutarate + O2
(2R,3R)-dihydrokaempferol + succinate + CO2
show the reaction diagram
naringenin + 2-oxoglutarate + O2
dihydrokaempferol + succinate + CO2
show the reaction diagram
naringenin + 2-oxoglutarate + O2
dihydroquercetin + succinate + CO2
show the reaction diagram
-
-
-
?
naringenin + O2 + 2-oxoglutarate
dihydrokaempferol + succinate + CO2
show the reaction diagram
pinocembrin + 2-oxoglutarate + O2
?
show the reaction diagram
-
38% of the activity with naringenin
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(2S)-flavanone + 2-oxoglutarate + O2
(2R/3R)-dihydroflavonol + succinate + CO2
show the reaction diagram
-
key step towards biosynthesis of flavonols, anthocyanins and catechins
-
-
?
(2S)-naringenin + 2-oxoglutarate + O2
(2R,3R)-dihydrokaempferol + succinate + CO2
show the reaction diagram
-
-
-
-
-
a (2S)-flavan-4-one + 2-oxoglutarate + O2
a (2R,3R)-dihydroflavonol + succinate + CO2
show the reaction diagram
a flavanone + 2-oxoglutarate + O2
a dihydroflavonol + succinate + CO2
show the reaction diagram
eriodictyol + 2-oxoglutarate + O2
dihydroquercetin + succinate + CO2
show the reaction diagram
eriodyctiol + 2-oxoglutarate + O2
dihydroquercetin + succinate + CO2
show the reaction diagram
-
-
-
-
?
naringenin + 2-oxoglutarate + O2
(2R,3R)-dihydrokaempferol + succinate + CO2
show the reaction diagram
naringenin + 2-oxoglutarate + O2
dihydrokaempferol + succinate + CO2
show the reaction diagram
naringenin + O2 + 2-oxoglutarate
dihydrokaempferol + succinate + CO2
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-oxoglutarate
ascorbate
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
-
can partially replace Fe2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(+)-dihydrokaempferol
-
product inhibition
3-Bromo-2-oxoglutarate
-
1 mM 92% inhibition
3-hydroxy-5-oxo-4-butyryl-cyclohex-3-ene-1-carboxylic acid ethyl ester
3-hydroxy-5-oxo-4-cyclopropanecarbonyl-cyclohex-3-ene-1-carboxylic acid ethyl ester
3-hydroxy-5-oxo-4-propionyl-cyclohex-3-ene-1-(2-dimethylamino)-thiazole
3-hydroxy-5-oxo-4-propionyl-cyclohex-3-ene-1-carbaldehyde
3-hydroxy-5-oxo-4-propionyl-cyclohex-3-ene-1-carbothioic acid S-ethyl ester
3-hydroxy-5-oxo-4-propionyl-cyclohex-3-ene-1-pentanoic acid
benzene-1,2,4,5-tetracarboxylic acid
calcium 3-hydroxy-5-oxo-4-propionyl-cyclohex-3-ene-1-carboxylate
diethyldicarbonate
diethyldithiocarbamate
Fe3+
-
1 mM, 56% inhibition
p-chloromercuribenzoate
prohexadione-Ca
-
an enzyme inhibitor for 2-oxoglutarate dependent dioxygenases, used as a growth retardant and for control of secondary fire blight, Erwinia amylovora, of apple leaves
Pyridine-2,4-dicarboxylate
pyridine-2,4-dicarboxylic acid diethyl ester
Pyridine-2,5-dicarboxylate
-
0.01 mM, 40% inhibition
pyridine-2,5-dicarboxylic acid
sodium 4,6-dioxo-2,2-dimethyl-5-(1-alloxyamino-butylidene)-cyclohexane-1-carboxylic acid methyl ester
Zn2+
-
in presence of 0.01 mM Fe2+
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ascorbate
catalase
-
stimulates
-
piperazine-1,4-bis-(2-ethane sulfonic acid)
-
1 mM, 96% relative activity
piperazine-1,4-bis-(2-ethane sulphonic acid)
-
1 mM, 96% relative activity
pyridine-2,3-dicarboxylic acid
pyridine-2,6-dicarboxylic acid
pyridine-2,6-dicarboxylic acid chloride
pyrrole-3,4-dicarboxylic acid diethyl ester
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
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.008 - 0.012
(2S)-eriodictyol
0.005 - 0.024
(2S)-naringenin
0.0057 - 0.0578
(S)-eriodictyol
1.4
2-oxoadipate
-
-
0.0019 - 0.1896
2-oxoglutarate
0.087
eriodictyol
-
pH 8.0, 37C
0.207 - 0.218
naringenin
additional information
additional information
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0012 - 0.0018
Pyridine 2,4-dicarboxylate
0.04
Pyridine 2,5-dicarboxylate
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0000026
-
unripe fruit: 43 nkat/kg total protein (enzyme extraction protocol 2)
0.0000038
-
flower: 64 nkat/kg total protein (enzyme extraction protocol 1)
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
0.000021
-
ripe fruit: 357 nkat/kg total protein (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)
0.000028
-
flower: 46 nkat/kg total protein (enzyme extraction protocol 2)
0.000029
-
ripe fruit: 484 nkat/kg total protein (enzyme extraction protocol 2)
0.000036
-
leaves: 606 nkat/kg total protein (enzyme extraction protocol 2)
0.000041
-
leaves: 690 nkat/kg total protein (enzyme extraction protocol 1), no activity with enzyme extraction protocol 2; ripe fruit: 688 nkat/kg total protein (enzyme extraction protocol 1)
0.000045
-
leaves: 758 nkat/kg total protein (enzyme extraction protocol 1)
0.00005
-
unripe fruit: 833 nkat/kg total protein (enzyme extraction protocol 2), no activity with enzyme extraction protocol 1
0.000056
-
ripe fruit: 932 nkat/kg total protein (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)
32000
-
pH 7.0, 25C
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
-
wild-type enzyme, and second lower optimum at pH 8.0
8
xAscocenda
recombinant enzyme
additional information
-
pH-optima of mutant enzymes
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.01
sequence calculation
5.1
xAscocenda
sequence calculation
5.57
sequence calculation
5.6
-
calculated
5.67
-
sequence calculation
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
tapetum-bound
Manually annotated by BRENDA team
higher accumulation
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35000
-
x * 35000 + x * 37000, two-dimensional SDS-PAGE
36800
x * 36800, calculated
37000
-
x * 35000 + x * 37000, two-dimensional SDS-PAGE
38700
x * 38700, calculated
39200
-
sedimentation equilibrium analysis
40000
-
x * 40000, calculation from nucleotide sequence
41000
SDS-PAGE
41350
x * 41350, sequence calculation
43600
-
x * 43600, calculation from nucleotide sequence
48000
-
gel filtration
68000
-
x * 42700, calculated, x * 68000, SDS-PAGE of fusion protein with glutathione S-transferase
74000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
2 * 24000-25000, SDS-PAGE
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 50
xAscocenda
recombinant enzyme, stable at 20-45C, loss of activity above 45C, inactivation at 60C
30
-
stable up to
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
partially stabilized under anaerobic conditions in presence of ascorbate
-
439119
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70C, in presence of 20 mM ascorbate, stable for more than 6 months
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme
-
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
recombinant MBP-tagged enzyme from Escherichia coli BL21(DE3)pLysS by amylose affinity chromatography
Sephadex G25 column gel filtration
-
shock frozen fruits are ground in a mill, leaves are ground in liquid nitrogen in a mortar, protocol 1: plant material is homogenized in a mortar with quartz sand and Polyclar AT with extraction buffer (0.1 M Tris-HCl, pH 7.5, containing 0.4% sodium ascorbate) and centrifuged, or protocol 2 (optimized for polyphenol-rich tissues): plant material is homogenized with Polyclar AT in a mortar, transferred to a falcon tube containing Dowex in buffer (0.7 M KH2PO4/K2HPO4, pH 8.0, containing 0.4 M sucrose, 0.4 M sodium ascorbate, 1 mM CaCl2, 30 mM EDTA, 50 mM cysteine, 50 mM DIECA, 1.5% PEG 20000, and 0.1% BSA, kept under nitrogen atmosphere after removing oxygen by boiling), homogenate is filtered (glass wool) and centrifuged, supernatants obtained with both protocols are cleared of low molecular compounds by a Sephadex G25 gel chromatography column
shock frozen fruits are ground in a mill, leaves are ground in liquid nitrogen in a mortar, protocol 1: plant material is homogenized in a mortar with quartz sand and Polyclar AT with extraction buffer (0.1 M Tris-HCl, pH 7.5, containing 0.4% sodium ascorbate) and centrifuged, or protocol 2 (optimized for polyphenol-rich tissues): plant material is homogenized with Polyclar AT in a mortar, transferred to a falcon tube containing Dowex in buffer (0.7 M KH2PO4/K2HPO4, pH 8.0, containing 0.4 M sucrose, 0.4 M sodium ascorbate, 1 mM CaCl2, 30mM EDTA, 50 mM cysteine, 50 mM DIECA, 1.5% PEG 20000, and 0.1% BSA, kept under nitrogen atmosphere after removing oxygen by boiling), homogenate is filtered (glass wool) and centrifuged, supernatants obtained with both protocols are cleared of low molecular compounds by a Sephadex G25 gel chromatography column
-
wild-type and mutant enzymes
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cloned into the pGEM T-easy plasmid vector and transformed into DH5alpha Escherichia coli competent cells
enzyme expression analysis by real-time RT-PCR
-
expressed in Escherichia coli BL21Star and Rosetta(DE3) cells
-
expressed in Escherichia coli strain BLR (DE3)
expressed in yeast strain InvSc1
expression as glutathione S-transferase fusion protein; expression as glutathione S-transferase fusion protein; expression as glutathione S-transferase fusion protein
expression in a reticulocyte system
expression in Escherichia coli
expression in Escherichia coli JM109
expression in Saccharomyces cerevisiae
-
expression in wheat-rye hybrids
functional expression of plant-derived O-methyltransferase, flavanone 3-hydroxylase, and flavonol synthase in Corynebacterium glutamicum for production of pterostilbene, kaempferol, and quercetin; gene 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 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
xAscocenda
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 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 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
C0SPH1, C0SPH2, C0SPH3
gene fht, transcription profiling and quantitative real-time PCR expression analysis
-
gene LcF3H, DNA and amino acid sequence determination and analysis, phylogenetic analysis, quantitative PCR enzyme expression analysis, recombinant expression in Escherichia coli strain BL21(DE3), recombinant overexpression in leaves of Nicotiana tabacum cv. Xanthinc via transformation with Agrobacterium tumefaciens strain EHA105, overexpression of heterogenous LcF3H enhances the expression levels of downstream genes but does not cause alteration in the expression of upstream genes including endogenous F3H of Nicotiana tabacum. The enzyme's overexpression does cause a significant increase in the content of three major flavan-3-ols, catechin, epicatechin and epigallocatechin
gene PeF3H, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, semi-quantitative RT-PCR enzyme expression analysis, recombinant expression in Escherichia coli tsrain M15 pREP-4
gene PnF3H, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis and tree, quantitative real-time PCR enzyme expression analysis, functional recombinant expression in Arabidopsis thaliana ecotype Col-0 via Agrobacterium tumefaciens-mediated transformation conferring tolerance to salt stress and abscisic acid treatment in transgenic Arabidopsis, recombinant expression of GFP-tagged enzyme in Arabidopsis thaliana
-
gene VcF3H, DNA and amino acid sequence determination and analysis, sequence comparisons, quantitative RT-PCR enzyme expression analysis, recombinant expression in Arabidopsis thaliana increasing the anthocyanin content in leaves without increasing the flavonol content
-
genes SbF3H1 and SbF3H2, semi-quantitative RT-PCR expression analysis of flavonoid structural genes in sorghum seedlings, overview. Complementation of Arabidopsis thaliana flavonoid mutants by genes SbF3H1 and SbF3H2, complementation analysis, overview
overexpression of the Camellia sinensis flavanone 3-hydroxylase gene in leaves of transgenic Nicotiana tabacum cv. Xanthi confers tolerance to salt stress and pathogenic fungus Alternaria solani, transformation via Agrobacterium tumefaciens strain LBA4404 containing pCAMBIA-F3H. A decrease in pectin methyl esterase (PME) activity and increase in pectin methyl esterification is also observed in CsF3H transgenic tobacco plants. Transcript expression analysis, and analysis of trangenic PME activity in flavonoid (epigallocatechin)-exposed and -unexposed seedlings, and in seedlings exposed to salt
wild-type and mutant enzymes, expression in Escherichia coli
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
decrease at stage of flowering
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
-
expression is up-regulated in response to wounding
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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
no induction of the SbF3H1 and SbF3H2 genes by methyljasmonate
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
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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 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; 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
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
biotecnology
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AaF3H is a potential target for regulation of flavonoids biosynthesis in Artemisia annua through metabolic engineering
D195E
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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
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mutant constructed to confer flavone synthase activity to flavanone 3beta-hydroxylase. Substrate naringenin is completely converted to flavanone 3beta-hydroxylase product dihydrokaempferol
D331H
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no catalytic activity
I115T
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mutant constructed to confer flavone synthase activity to flavanone 3beta-hydroxylase. Substrate naringenin is completely converted to flavanone 3beta-hydroxylase product dihydrokaempferol
I115T/V116I
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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
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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
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mutant constructed to confer flavone synthase activity to flavanone 3beta-hydroxylase. Substrate naringenin is completely converted to flavanone 3beta-hydroxylase product dihydrokaempferol
I131F/D195E
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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
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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
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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
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mutant constructed to confer flavone synthase activity to flavanone 3beta-hydroxylase. Substrate naringenin is completely converted to flavanone 3beta-hydroxylase product dihydrokaempferol
M106T
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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
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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
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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
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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
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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
H278Q
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mutant enzyme has no detectable enzyme activity
N222N
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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
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decrease in catalytic activity and a 5fold increase in Km-value for 2-oxoglutarate
R288Q
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decrease in catalytic activity and a 160fold increase in Km-value for 2-oxoglutarate
S290A
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activity is reduced to 8% of that of the wild-type enzyme
S290T
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activity is reduced to 20% of that of the wild-type enzyme
S290V
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activity is reduced to 1% of that of the wild-type enzyme
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
agriculture
analysis
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; functional expression of plant-derived O-methyltransferase, flavanone 3-hydroxylase, and flavonol synthase in Corynebacterium glutamicum for production of pterostilbene, kaempferol, and quercetin
additional information
F3H gene may be used as biomarker in tea breeding programs and genetic engineering to improve tea quality
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