Information on EC 1.14.11.23 - flavonol synthase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.14.11.23
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RECOMMENDED NAME
GeneOntology No.
flavonol synthase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
a dihydroflavonol + 2-oxoglutarate + O2 = a flavonol + succinate + CO2 + H2O
show the reaction diagram
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-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
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Flavonoid biosynthesis
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flavonoid biosynthesis (in equisetum)
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flavonol biosynthesis
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Metabolic pathways
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rutin biosynthesis
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syringetin biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
dihydroflavonol,2-oxoglutarate:oxygen oxidoreductase
In addition to the desaturation of (2R,3R)-dihydroflavonols to flavonols, the enzyme from the satsuma Citrus unshiu also has a non-specific activity that trans-hydroxylates the flavanones (2S)-naringenin and the unnatural (2R)-naringenin at C-3 to kaempferol and (2R,3R)-dihydrokaempferol, respectively [2]. Requires Fe2+.
CAS REGISTRY NUMBER
COMMENTARY hide
146359-76-4
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene AcFLS
UniProt
Manually annotated by BRENDA team
Marc.
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-
Manually annotated by BRENDA team
gene GbFLS
UniProt
Manually annotated by BRENDA team
cultivars M9 and Weirouge
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Manually annotated by BRENDA team
cv. Italian Giant
SwissProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
cultivars Pyrodwarf and Conference
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
FLS protein structure modeling, overview. The structures of two major flavonols, i.e. melanoxetin or transilitin, found in Acacia confusa heartwood are different from common flavonoids
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(+)-trans-dihydrokaempferol + 2-oxoglutarate + O2
kaempferol + succinate + CO2 + H2O
show the reaction diagram
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-
-
-
?
(2R)-naringenin + 2-oxoglutarate + O2
(-)-trans-dihydrokaempferol + succinate + CO2 + H2O
show the reaction diagram
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-
-
-
?
(2R)-naringenin + 2-oxoglutarate + O2
(2S,3R)-dihydrokaempferol + succinate + CO2 + H2O
show the reaction diagram
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transhydroxylation
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-
?
(2R)-naringenin + 2-oxoglutarate + O2
(2S,3S)-dihydrokaempferol + succinate + CO2 + H2O
show the reaction diagram
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+ low amounts of kaempferol
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?
(2R)-naringenin + 2-oxoglutarate + O2
? + succinate + CO2 + H2O
show the reaction diagram
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-
-
-
?
(2R,3R)-trans-dihydroquercetin + 2-oxoglutarate + O2
quercetin + succinate + CO2 + H2O
show the reaction diagram
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-
-
-
?
(2R,3S,4R)-trans-leucocyanidin + 2-oxoglutarate + O2
? + succinate + CO2 + H2O
show the reaction diagram
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-
-
-
?
(2R/3R)-dihydrokaempferol + 2-oxoglutarate + O2
kaempferol + succinate + CO2 + H2O
show the reaction diagram
(2R/3R)-dihydroquercetin + 2-oxoglutarate + O2
quercetin + succinate + CO2 + H2O
show the reaction diagram
(2S)-naringenin + 2-oxoglutarate + O2
(2R,3S)-cis-dihydrokaempferol + (2R,3R)-trans-dihydrokaempferol + apigenin + kaempferol + succinate + CO2 + H2O
show the reaction diagram
(2S)-naringenin + 2-oxoglutarate + O2
(2R,3S)-dihydrokaempferol + (2S,3S)-dihydrokaempferol + kaempferol + succinate + CO2 + H2O
show the reaction diagram
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-
-
-
?
(2S)-naringenin + 2-oxoglutarate + O2
? + succinate + CO2 + H2O
show the reaction diagram
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-
-
-
?
(2S)-naringenin + 2-oxoglutarate + O2
dihydrokaempferol + kaempferol + succinate + CO2 + H2O
show the reaction diagram
poor substrate
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-
?
(2S)-naringenin + 2-oxoglutarate + O2
kaempferol + succinate + CO2 + H2O
show the reaction diagram
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-
-
-
?
a dihydroflavonol + 2-oxoglutarate + O2
a flavonol + succinate + CO2 + H2O
show the reaction diagram
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-
-
-
?
cis-dihydrokaempferol + 2-oxoglutarate + O2
kaempferol + succinate + CO2 + H2O
show the reaction diagram
weak reaction, only traces of kaempferol produced
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-
?
dihydrokaempferol + 2-oxoglutarate + O2
kaempferol + CO2 + H2O
show the reaction diagram
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-
-
-
?
dihydrokaempferol + 2-oxoglutarate + O2
kaempferol + succinate + CO2 + H2O
show the reaction diagram
dihydromyricetin + 2-oxoglutarate + O2
myricetin + succinate + CO2 + H2O
show the reaction diagram
dihydroquercetin + 2-oxoglutarate + O2
quercetin + CO2 + H2O
show the reaction diagram
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-
-
-
?
dihydroquercetin + 2-oxoglutarate + O2
quercetin + succinate + CO2 + H2O
show the reaction diagram
naringenin + 2-oxoglutarate + O2
3-O-methylkaempferol + kaempferol + CO2 + H2O
show the reaction diagram
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-
-
-
?
naringenin + 2-oxoglutarate + O2
kaempferol + succinate + CO2 + H2O
show the reaction diagram
trans-dihydrokaempferol + 2-oxoglutarate + O2
kaempferol + succinate + CO2 + H2O
show the reaction diagram
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?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(2R/3R)-dihydrokaempferol + 2-oxoglutarate + O2
kaempferol + succinate + CO2 + H2O
show the reaction diagram
(2R/3R)-dihydroquercetin + 2-oxoglutarate + O2
quercetin + succinate + CO2 + H2O
show the reaction diagram
a dihydroflavonol + 2-oxoglutarate + O2
a flavonol + succinate + CO2 + H2O
show the reaction diagram
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-
-
-
?
dihydromyricetin + 2-oxoglutarate + O2
myricetin + succinate + CO2 + H2O
show the reaction diagram
naringenin + 2-oxoglutarate + O2
kaempferol + succinate + CO2 + H2O
show the reaction diagram
H6V8U4
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additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ascorbate
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,2'-dipyridyl
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2 mM, 90% 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
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2 mM, 16% inhibition
diethyldithiocarbamate
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2 mM, 80% inhibition
EDTA
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5 mM, 94% inhibition
KCN
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5 mM, 63% inhibition
p-hydroxymercuribenzoate
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0.1 mM, 89% inhibition
pyrazole-3,5-dicarboxylic acid
pyridine-2,4-dicarboxylic acid diethyl ester
pyridine-2,5-dicarboxylic acid
pyridine-3,4-dicarboxylic acid
sodium 4,6-dioxo-2,2-dimethyl-5-(1-alloxyamino-butylidene)-cyclohexane-1-carboxylic acid methyl ester
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-oxoglutarate
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activity is completely abolished by the omission of 2-oxoglutarate from the reaction mixture
ascorbate
catalase
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without the addition of catalase, the enzyme activity is decreased to approximately 45%
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piperazine-1,4-bis-(2-ethane sulfonic acid)
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1 mM, 115% activity
piperazine-1,4-bis-(2-ethane sulphonic acid)
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1 mM, 115% activity
pyridine-2,3-dicarboxylic acid
pyridine-2,6-dicarboxylic acid
pyridine-2,6-dicarboxylic acid chloride
pyridine-3,5-dicarboxylic acid
pyrrole-3,4-dicarboxylic acid diethyl ester
sorbitol
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.024
(2R/3R)-dihydrokaempferol
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in 10 mM Tris/HCl buffer (pH 8.0), at 37°C
0.031
(2R/3R)-dihydroquercetin
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in 10 mM Tris/HCl buffer (pH 8.0), at 37°C
0.036
2-oxoglutarate
-
0.001 - 0.0584
dihydrokaempferol
0.0012 - 0.32
dihydroquercetin
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
6.6
dihydrokaempferol
Zea mays
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recombinant FLS1, pH not specified in the publication, temperature not specified in the publication
0.015 - 3.9
dihydroquercetin
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
113
dihydrokaempferol
Zea mays
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recombinant FLS1, pH not specified in the publication, temperature not specified in the publication
2555
26
dihydroquercetin
Zea mays
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recombinant FLS1, pH not specified in the publication, temperature not specified in the publication
1502
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0053
purified recombinant enzyme with substrate (2R/3R)-dihydrokaempferol, pH 5.0, 37°C
0.019
purified recombinant enzyme with substrate (2R/3R)-dihydroquercetin, pH 5.0, 37°C
0.15
purified recombinant His-tagged enzyme, substrate dihydroquercetin, pH 6.8, 25°C
0.154
purified recombinant His-tagged enzyme, substrate dihydromyricetin, pH 6.8, 25°C
0.163
purified recombinant His-tagged enzyme, substrate naringenin, pH 6.8, 25°C
26.9
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wild-type, 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.7
sequence calculation
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
of young seedling
Manually annotated by BRENDA team
high expression level
Manually annotated by BRENDA team
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37899
x * 37899, MALDI-TOF mass spectrometry
40000
x * 40000, recombinant enzyme, SDS-PAGE
45000
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about, SDS-PAGE and Western blot
64000
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x * 38000, SDS-PAGE, x * 64000, SDS-PAGE of fusion protein with glutathione S-transferase
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
FLS protein structure modeling, overview
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
identification of putative residues for binding ferrous iron, i.e. H221, D223 and H277, binding 2-oxoglutarate, i.e. R287 and S289, and dihydroquercetin, i.e. H132, F134, K202, F293 and E295 via computational analyses
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, purified enzyme, 2 weeks, no loss of catalytic activity
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
from inclusion bodies of recombiant Escherichia coli, denaturation with 6 M urea. Addition of FeSO4 to purification buffers significantly improves the recovery of active enzyme
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by immunoaffinity chromatography
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant His-tagged FLS protein from Escherichia coli strain BL21-CodonPlus-RIL by nickel affinity chromatography
recombinant His-tagged FLS1 from Escherichia coli to about 80% purity by nickel affinity chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli strain BL21Star
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expressed with a glutathione-S-transferase tagging in Escherichia coli
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expression in Escherichia coli
expression in Escherichia coli as glutathione S-transferase fusion protein
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expression in Escherichia coli as thioredoxin fusion proteins; expression in Escherichia coli as thioredoxin fusion proteins
expression in Escherichia coli JM109
expression in Escherichia coli, His-tag
expression in Saccharomyces cereviseae strain INV Sc1 and in Escherichia coli BL21-A1
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expression in yeast
gene AcFLS, DNA and amino acid sequence determination and analysis, sequence comparison and phylogenetic analysis, recombinant expression of His-tagged FLS protein in Escherichia coli strain BL21-CodonPlus-RIL
gene FtFLS1, DNA and amino acid sequence determination and analysis, phylogenetic tree, functional expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
gene FtFLS1, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, quantitative expression analysis; gene FtFLS2, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree; gene FtFLS2, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, quantitative expression analysis
gene GbFLS, DNA and amino acid sequence determination and analysis, promoter region sequence analysis and putative cis-acting regulatory elements, overview, expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
gene ZmFLS1, ZmFLS1 is under the control of the anthocyanin (C1/PL1 + R/B) and 3-deoxy flavonoid (P1) transcriptional regulators in vivo, recombinant expression as His-tagged protein in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
cold-stress treatment, 4°C for 24 h
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FtFLS1 expression is downregulated by NaCl, salicylic acid, and abscisic acid
GbFLS expression is induced by abiotic stresses: UV-B irradiation, abscisic acid, cold, sucrose, salicylic acid, and ethephon
increase at stage of pigmentation initiation
no effect on FLS2 expression by abscisic acid
the enzyme is UV-B-light-inducible in maize seedlings
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the transcription level of FLS2 is significantlyup-regulated by salicylic acid and NaCl
wounding by cutting leaves induces maximum AcFLS mRNA accumulation 6-12 h after treatment
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D223E
-
no catalytic activity
E295L
-
7% of wild-type activity
E295Q
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48% of wild-type activity
F134A
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15% of wild-type activity
F134L
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54% of wild-type activity
F293A
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8% of wild-type activity
F293L
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9% of wild-type activity
H132F
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124% of wild-type activity
H132Y
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83% of wild-type activity
H221W
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no catalytic activity
H277F
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no catalytic activity
K202M
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24% of wild-type activity
K202R
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12% of wild-type activity
R287K
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no catalytic activity
S289T
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48% of wild-type activity
G261A
mutant enzyme with 10% of wild-type activity
G261P
no immunoreactive FLS polypeptide detected
G68A
mutant enzyme with 6% of wild-type activity
G68P
no immunoreactive FLS polypeptide detected
P207G
no effect on activity
H132F
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site-directed mutagenesis, the mutant shows similar kinetics with dihydrokaempferol compared to the wild-type enzyme
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
production of active flavonol synthase from Camellia sinensis in Escherichia coli, with high specific activity
Show AA Sequence (101 entries)
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