Information on EC 1.14.11.9 - flavanone 3-dioxygenase

Word Map on EC 1.14.11.9
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)

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
(2S)-flavan-4-one,2-oxoglutarate:oxygen oxidoreductase (3-hydroxylating)
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
-
-
flavonoid biosynthesis
-
-
Flavonoid biosynthesis
-
-
flavonoid biosynthesis (in equisetum)
-
-
leucodelphinidin biosynthesis
-
-
leucopelargonidin and leucocyanidin biosynthesis
-
-
Metabolic pathways
-
-
pinobanksin biosynthesis
-
-
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
-
UniProt
Manually annotated by BRENDA team
cultivar Oolong No. 17
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
-
-
-
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
-
-
-
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
; gooseberry
-
-
Manually annotated by BRENDA team
cv. Mespi
-
-
Manually annotated by BRENDA team
; raspberry
-
-
Manually annotated by BRENDA team
; blackberry
-
-
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
L. cv. Cabernet Sauvignon
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 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
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 + 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
-
-
?
a flavanone + 2-oxoglutarate + O2
a dihydroflavonol + 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, 37°C
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)
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
-
wild-type enzyme, and second lower optimum at pH 8.0
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
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
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
-
enzyme exists as functional monomeric and oligomeric forms. The monomeric polypeptide comprises the catalytically active flavanone 3beta-hydroxylase
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
stable up to
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
partially stabilized under anaerobic conditions in presence of ascorbate
-
439119
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70°C, in presence of 20 mM ascorbate, stable for more than 6 months
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme
-
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
gene F3H, DNA and amino acid sequence determination and analysis, sequence comparison and phylogenetic tree, quantitative real-time RT-PCR expression analysis
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
gene fht, transcription profiling and quantitative real-time PCR expression analysis
-
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
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
-
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
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
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
D331H
-
no catalytic activity
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
H278Q
-
mutant enzyme has no detectable enzyme activity
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
S290A
-
activity is reduced to 8% of that of the wild-type enzyme
S290T
-
activity is reduced to 20% of that of the wild-type enzyme
S290V
-
activity is reduced to 1% of that of the wild-type enzyme
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
agriculture
additional information
F3H gene may be used as biomarker in tea breeding programs and genetic engineering to improve tea quality
Show AA Sequence (131 entries)
Please use the Sequence Search for a specific query.