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(+)-trans-dihydrokaempferol + 2-oxoglutarate + O2
kaempferol + succinate + CO2 + H2O
-
-
-
-
?
(2R)-naringenin + 2-oxoglutarate + O2
(-)-trans-dihydrokaempferol + succinate + CO2 + H2O
-
-
-
-
?
(2R)-naringenin + 2-oxoglutarate + O2
(2S,3R)-dihydrokaempferol + succinate + CO2 + H2O
-
transhydroxylation
-
-
?
(2R)-naringenin + 2-oxoglutarate + O2
(2S,3S)-dihydrokaempferol + succinate + CO2 + H2O
-
-
+ low amounts of kaempferol
-
?
(2R)-naringenin + 2-oxoglutarate + O2
? + succinate + CO2 + H2O
-
-
-
-
?
(2R,3R)-trans-dihydroquercetin + 2-oxoglutarate + O2
quercetin + succinate + CO2 + H2O
-
-
-
-
?
(2R,3S,4R)-trans-leucocyanidin + 2-oxoglutarate + O2
? + succinate + CO2 + H2O
-
-
-
-
?
(2R/3R)-dihydrokaempferol + 2-oxoglutarate + O2
kaempferol + succinate + CO2 + H2O
(2R/3R)-dihydroquercetin + 2-oxoglutarate + O2
quercetin + succinate + CO2 + H2O
(2S)-naringenin + 2-oxoglutarate + O2
(2R,3S)-cis-dihydrokaempferol + (2R,3R)-trans-dihydrokaempferol + apigenin + kaempferol + succinate + CO2 + H2O
(2S)-naringenin + 2-oxoglutarate + O2
(2R,3S)-dihydrokaempferol + (2S,3S)-dihydrokaempferol + kaempferol + succinate + CO2 + H2O
-
-
-
-
?
(2S)-naringenin + 2-oxoglutarate + O2
? + succinate + CO2 + H2O
-
-
-
-
?
(2S)-naringenin + 2-oxoglutarate + O2
dihydrokaempferol + kaempferol + succinate + CO2 + H2O
poor substrate
-
-
?
(2S)-naringenin + 2-oxoglutarate + O2
kaempferol + succinate + CO2 + H2O
-
-
-
-
?
3'-O-methyltaxifolin + 2-oxoglutarate + O2
isorhamnetin + succinate + CO2 + H2O
-
-
-
?
a dihydroflavonol + 2-oxoglutarate + O2
a flavonol + succinate + CO2 + H2O
-
-
-
?
cis-dihydrokaempferol + 2-oxoglutarate + O2
kaempferol + succinate + CO2 + H2O
weak reaction, only traces of kaempferol produced
-
-
?
dihydrokaempferol + 2-oxoglutarate + O2
kaempferol + succinate + CO2 + H2O
dihydromyricetin + 2-oxoglutarate + O2
myricetin + succinate + CO2 + H2O
dihydroquercetin + 2-oxoglutarate + O2
quercetin + succinate + CO2 + H2O
naringenin + 2-oxoglutarate + O2
kaempferol + succinate + CO2 + H2O
pinobanksin + 2-oxoglutarate + O2
galangin + succinate + CO2 + H2O
-
-
-
?
trans-dihydrokaempferol + 2-oxoglutarate + O2
kaempferol + succinate + CO2 + H2O
-
-
-
?
additional information
?
-
(2R/3R)-dihydrokaempferol + 2-oxoglutarate + O2
kaempferol + succinate + CO2 + H2O
-
-
-
?
(2R/3R)-dihydrokaempferol + 2-oxoglutarate + O2
kaempferol + succinate + CO2 + H2O
-
-
-
?
(2R/3R)-dihydrokaempferol + 2-oxoglutarate + O2
kaempferol + succinate + CO2 + H2O
-
-
-
?
(2R/3R)-dihydrokaempferol + 2-oxoglutarate + O2
kaempferol + succinate + CO2 + H2O
-
-
-
-
?
(2R/3R)-dihydrokaempferol + 2-oxoglutarate + O2
kaempferol + succinate + CO2 + H2O
-
-
-
-
?
(2R/3R)-dihydroquercetin + 2-oxoglutarate + O2
quercetin + succinate + CO2 + H2O
-
-
-
?
(2R/3R)-dihydroquercetin + 2-oxoglutarate + O2
quercetin + succinate + CO2 + H2O
-
-
-
?
(2R/3R)-dihydroquercetin + 2-oxoglutarate + O2
quercetin + succinate + CO2 + H2O
-
-
-
?
(2R/3R)-dihydroquercetin + 2-oxoglutarate + O2
quercetin + succinate + CO2 + H2O
-
-
-
?
(2R/3R)-dihydroquercetin + 2-oxoglutarate + O2
quercetin + succinate + CO2 + H2O
-
-
-
-
?
(2R/3R)-dihydroquercetin + 2-oxoglutarate + O2
quercetin + succinate + CO2 + H2O
-
-
-
-
?
(2S)-naringenin + 2-oxoglutarate + O2
(2R,3S)-cis-dihydrokaempferol + (2R,3R)-trans-dihydrokaempferol + apigenin + kaempferol + succinate + CO2 + H2O
-
-
-
-
?
(2S)-naringenin + 2-oxoglutarate + O2
(2R,3S)-cis-dihydrokaempferol + (2R,3R)-trans-dihydrokaempferol + apigenin + kaempferol + succinate + CO2 + H2O
-
-
(2R,3S)-dihydrokaempferol is the predominant two-electron oxidation product
-
?
dihydrokaempferol + 2-oxoglutarate + O2
kaempferol + succinate + CO2 + H2O
-
-
-
?
dihydrokaempferol + 2-oxoglutarate + O2
kaempferol + succinate + CO2 + H2O
-
-
-
-
?
dihydrokaempferol + 2-oxoglutarate + O2
kaempferol + succinate + CO2 + H2O
good substrate
-
-
?
dihydrokaempferol + 2-oxoglutarate + O2
kaempferol + succinate + CO2 + H2O
-
-
-
-
?
dihydrokaempferol + 2-oxoglutarate + O2
kaempferol + succinate + CO2 + H2O
-
-
-
?, r
dihydrokaempferol + 2-oxoglutarate + O2
kaempferol + succinate + CO2 + H2O
-
-
-
-
r
dihydrokaempferol + 2-oxoglutarate + O2
kaempferol + succinate + CO2 + H2O
-
-
-
-
?
dihydrokaempferol + 2-oxoglutarate + O2
kaempferol + succinate + CO2 + H2O
-
-
-
?
dihydrokaempferol + 2-oxoglutarate + O2
kaempferol + succinate + CO2 + H2O
-
-
-
-
ir
dihydrokaempferol + 2-oxoglutarate + O2
kaempferol + succinate + CO2 + H2O
the mutated enzymes L311F, Y240P, F146I, A120M and L311F-A120M are all able to oxidize dihydrokaempferol to kaempferol, with respective catalytic activities relative to the wild type level of 355%, 104%, 86%, 162% and 175%. L311F substitution increases the flavonol synthase activity
-
-
?
dihydrokaempferol + 2-oxoglutarate + O2
kaempferol + succinate + CO2 + H2O
-
-
-
-
ir
dihydrokaempferol + 2-oxoglutarate + O2
kaempferol + succinate + CO2 + H2O
-
-
-
-
?
dihydrokaempferol + 2-oxoglutarate + O2
kaempferol + succinate + CO2 + H2O
-
-
-
-
?
dihydrokaempferol + 2-oxoglutarate + O2
kaempferol + succinate + CO2 + H2O
-
-
-
-
?
dihydrokaempferol + 2-oxoglutarate + O2
kaempferol + succinate + CO2 + H2O
-
-
-
-
?
dihydrokaempferol + 2-oxoglutarate + O2
kaempferol + succinate + CO2 + H2O
-
-
-
-
?
dihydrokaempferol + 2-oxoglutarate + O2
kaempferol + succinate + CO2 + H2O
-
-
-
-
?
dihydromyricetin + 2-oxoglutarate + O2
myricetin + succinate + CO2 + H2O
-
-
-
?
dihydromyricetin + 2-oxoglutarate + O2
myricetin + succinate + CO2 + H2O
-
-
-
-
?
dihydromyricetin + 2-oxoglutarate + O2
myricetin + succinate + CO2 + H2O
-
-
-
?
dihydromyricetin + 2-oxoglutarate + O2
myricetin + succinate + CO2 + H2O
-
-
-
-
ir
dihydromyricetin + 2-oxoglutarate + O2
myricetin + succinate + CO2 + H2O
-
-
-
-
ir
dihydromyricetin + 2-oxoglutarate + O2
myricetin + succinate + CO2 + H2O
-
-
-
-
?
dihydroquercetin + 2-oxoglutarate + O2
quercetin + succinate + CO2 + H2O
-
-
-
?
dihydroquercetin + 2-oxoglutarate + O2
quercetin + succinate + CO2 + H2O
-
-
-
-
?
dihydroquercetin + 2-oxoglutarate + O2
quercetin + succinate + CO2 + H2O
-
-
-
?
dihydroquercetin + 2-oxoglutarate + O2
quercetin + succinate + CO2 + H2O
poor substrate
-
-
?
dihydroquercetin + 2-oxoglutarate + O2
quercetin + succinate + CO2 + H2O
-
-
-
?
dihydroquercetin + 2-oxoglutarate + O2
quercetin + succinate + CO2 + H2O
-
-
-
?, r
dihydroquercetin + 2-oxoglutarate + O2
quercetin + succinate + CO2 + H2O
-
-
-
-
r
dihydroquercetin + 2-oxoglutarate + O2
quercetin + succinate + CO2 + H2O
-
-
-
-
?
dihydroquercetin + 2-oxoglutarate + O2
quercetin + succinate + CO2 + H2O
-
-
-
-
ir
dihydroquercetin + 2-oxoglutarate + O2
quercetin + succinate + CO2 + H2O
-
-
-
-
ir
dihydroquercetin + 2-oxoglutarate + O2
quercetin + succinate + CO2 + H2O
-
-
-
-
?
dihydroquercetin + 2-oxoglutarate + O2
quercetin + succinate + CO2 + H2O
-
-
-
-
?
naringenin + 2-oxoglutarate + O2
kaempferol + succinate + CO2 + H2O
-
-
-
?
naringenin + 2-oxoglutarate + O2
kaempferol + succinate + CO2 + H2O
-
-
-
-
?
naringenin + 2-oxoglutarate + O2
kaempferol + succinate + CO2 + H2O
-
-
-
?
naringenin + 2-oxoglutarate + O2
kaempferol + succinate + CO2 + H2O
-
-
in a second reaction step with kaempferol 3-O-methyltransferase kaempferol is converted into 3-O-methylkaempferol
-
?
additional information
?
-
substrates are bound with similar affinity
-
-
?
additional information
?
-
-
the enzyme is involved in the biosynthesis of flavonoids
-
-
?
additional information
?
-
flavonol synthase and flavanone 3beta-hydroxylase are key enzymes in the biosynthesis of the UV-B protectant, kaempferol
-
-
?
additional information
?
-
-
flavonol synthase and flavanone 3beta-hydroxylase are key enzymes in the biosynthesis of the UV-B protectant, kaempferol
-
-
?
additional information
?
-
-
FLS1 is capable of converting the dihydrokaempferol and dihydroquercetin dihydroflavonols to the corresponding flavonols, kaempferol and quercetin
-
-
?
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2,2'-dipyridyl
-
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
-
2 mM, 16% inhibition
diethyldithiocarbamate
-
2 mM, 80% inhibition
EDTA
-
5 mM, 94% inhibition
KCN
-
5 mM, 63% inhibition
p-hydroxymercuribenzoate
-
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
3-hydroxy-5-oxo-4-butyryl-cyclohex-3-ene-1-carboxylic acid ethyl ester
-
1 mM 48% activity, 0.1 mM 88% activity
3-hydroxy-5-oxo-4-butyryl-cyclohex-3-ene-1-carboxylic acid ethyl ester
-
1 mM 48% activity, 0.1 mM 88% activity
3-hydroxy-5-oxo-4-cyclopropanecarbonyl-cyclohex-3-ene-1-carboxylic acid ethyl ester
-
1 mM 50% activity, 0.1 mM 77% activity
3-hydroxy-5-oxo-4-cyclopropanecarbonyl-cyclohex-3-ene-1-carboxylic acid ethyl ester
-
1 mM 50% activity, 0.1 mM 77% activity
3-hydroxy-5-oxo-4-propionyl-cyclohex-3-ene-1-(2-dimethylamino)-thiazole
-
1 mM 44% activity, 0.1 mM 73% activity
3-hydroxy-5-oxo-4-propionyl-cyclohex-3-ene-1-(2-dimethylamino)-thiazole
-
1 mM 44% activity, 0.1 mM 73% activity
3-hydroxy-5-oxo-4-propionyl-cyclohex-3-ene-1-carbaldehyde
-
1 mM 56% activity, 0.1 mM 82% activity
3-hydroxy-5-oxo-4-propionyl-cyclohex-3-ene-1-carbaldehyde
-
1 mM 56% activity, 0.1 mM 82% activity
3-hydroxy-5-oxo-4-propionyl-cyclohex-3-ene-1-carbothioic acid S-ethyl ester
-
1 mM 33% activity, 0.1 mM 90% activity
3-hydroxy-5-oxo-4-propionyl-cyclohex-3-ene-1-carbothioic acid S-ethyl ester
-
1 mM 33% activity, 0.1 mM 90% activity
3-hydroxy-5-oxo-4-propionyl-cyclohex-3-ene-1-pentanoic acid
-
1 mM 23% activity, 0.1 mM 64% activity
3-hydroxy-5-oxo-4-propionyl-cyclohex-3-ene-1-pentanoic acid
-
1 mM 23% activity, 0.1 mM 64% activity
benzene-1,2,4,5-tetracarboxylic acid
-
1 mM 95% activity
benzene-1,2,4,5-tetracarboxylic acid
-
1 mM 95% activity
calcium 3-hydroxy-5-oxo-4-propionyl-cyclohex-3-ene-1-carboxylate
-
1 mM 11% activity, 0.1 mM 29% relative activity
calcium 3-hydroxy-5-oxo-4-propionyl-cyclohex-3-ene-1-carboxylate
-
1 mM 11% activity, 0.1 mM 29% activity
pyrazole-3,5-dicarboxylic acid
-
1 mM 22% activity, 0.1 mM 79% activity
pyrazole-3,5-dicarboxylic acid
-
1 mM 22% activity, 0.1 mM 79% activity
pyridine-2,4-dicarboxylic acid diethyl ester
-
1 mM 3% activity, 0.1 mM 13% activity
pyridine-2,4-dicarboxylic acid diethyl ester
-
1 mM 3% activity, 0.1 mM 13% activity
pyridine-2,5-dicarboxylic acid
-
1 mM 3% activity, 0.1 mM 11% activity
pyridine-2,5-dicarboxylic acid
-
1 mM 3% activity, 0.1 mM 11% activity
pyridine-3,4-dicarboxylic acid
-
1 mM 86% activity, 0.1 mM 85% activity
pyridine-3,4-dicarboxylic acid
-
1 mM 86% activity, 0.1 mM 85% activity
sodium 4,6-dioxo-2,2-dimethyl-5-(1-alloxyamino-butylidene)-cyclohexane-1-carboxylic acid methyl ester
-
1 mM 78% activity, 0.1 mM 84% activity
sodium 4,6-dioxo-2,2-dimethyl-5-(1-alloxyamino-butylidene)-cyclohexane-1-carboxylic acid methyl ester
-
1 mM 78% activity, 0.1 mM 84% activity
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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
evolution
the enzyme belongs to the 2-oxoglutarate iron-dependent oxygenase family
evolution
the enzyme belongs to the 2-oxoglutarate-dependent dioxygenase family
evolution
the enzyme belongs to the the 2-oxoglutarate-Fe(II) dioxygenase superfamily
malfunction
-
second functional flavonol synthase fls3 in case of fls1 mutant lines, lacking the active flavonol synthase
malfunction
gene FLS silencing reduces the flavonol content by 17-53%, while it increases catechin and epicatechin content 51-93% and 18-27%, respectively. The silenced lines show a significant increase in expression of genes for dihydroflavonol reductase and anthocyanidin synthase, a downstream gene towards epicatechin production, with no significant change in expression of other genes of the flavonoid pathway, phenotypes, overview
malfunction
gene FLS1 silencing reduces the flavonol content by 17-53%, while it increases catechin and epicatechin content 51-93% and 18-27%, respectively. The silenced lines show a significant increase in expression of genes for dihydroflavonol reductase and anthocyanidin synthase, a downstream gene towards epicatechin production, with no significant change in expression of other genes of the flavonoid pathway, phenotypes, overview
malfunction
post-transcriptional silencing of flavonol synthase mRNA in tobacco leads to fruits with arrested seed set, FLS silenced lines show 20-80% reduction in FLS encoding gene expression and 25-93% reduction in quercetin content, as well as a reduction in anthocyanidins content. Content of flavan-3-ols, i.e. catechin, epi-catechin and epigallocatechin, is increased in the transgenic lines, phenotypes, overview
malfunction
post-transcriptional silencing of flavonol synthase mRNA in tobacco leads to fruits with arrested seed set, FLS1 silenced lines show 20-80% reduction in FLS1 encoding gene expression and 25-93% reduction in quercetin content, as well as a reduction in anthocyanidins content. Content of flavan-3-ols, i.e. catechin, epi-catechin and epigallocatechin, is increased in the transgenic lines, phenotypes, overview
malfunction
the anthocyanin level of fls1-3 knock-out mutants is about two-fold higher than that of wild-type seedlings
metabolism
part of flavonoid biosynthetic pathway
metabolism
-
ZmFLS1 is a key flavonoid biosynthetic enzyme and involved in control of flavonol accumulation in maize
metabolism
-
key enzyme in the biosynthesis of flavonols, pathway overview
metabolism
the FLS enzyme competes with dihydroflavonol 4-reductase for the common substrate dihydroflavonols
metabolism
flavonol synthase is key enzyme in the flavonol biosynthetic pathway
metabolism
the enzyme is involved in flavonoid pathway. Flavonol synthase and dihydroflavonol-4-reductase compete for common substrates in order to direct the biosynthesis of flavonols and anthocyanins, respectively, thereby determining white vs. red coloration of flowers
metabolism
the enzyme is involved in flavonoid pathway. Flavonol synthase and dihydroflavonol-4-reductase compete for common substrates in order to direct the biosynthesis of flavonols and anthocyanins, respectively, thereby determining white vs. red coloration of flowers
metabolism
the enzyme is involved in flavonoid pathway. Flavonol synthase and dihydroflavonol-4-reductase compete for common substrates in order to direct the biosynthesis of flavonols and anthocyanins, respectively, thereby determining white vs. red coloration of flowers
metabolism
the enzyme is involved in flavonoid pathway. Flavonol synthase and dihydroflavonol-4-reductase compete for common substrates in order to direct the biosynthesis of flavonols and anthocyanins, respectively, thereby determining white vs. red coloration of flowers
physiological function
part of flavonoid biosynthesis pathway
physiological function
-
key enzyme in the biosynthesis of flavonols, which have defense-related and antioxidant functions in plants
physiological function
the enzyme controls a key step in flavonol biosynthesis and might play a key role in rutin biosynthesis
physiological function
flavonol synthase is involved in the plant defense response
physiological function
involved in flavonoid pathway
physiological function
the concentrations of anthocyanins and flavonols correlates with leaf color and it is proposed that the expression of dihydroflavonol 4-reductase and flavonol synthase influences their accumulation. Overexpression of dihydroflavonol 4-reductase, or silencing of flavonol synthase, increases anthocyanin production, resulting in red-leaf and red fruit peel phenotypes. Conversely, elevated flavonol production and green phenotypes in crabapple leaves and apple peel are observed when dihydroflavonol 4-reductase is overexpressed or dihydroflavonol 4-reductase is silenced. These results suggest that the relative activities of dihydroflavonol 4-reductase and flavonol synthase are important determinants of the red color of crabapple leaves, via the regulation of the metabolic fate of substrates that these enzymes have in common
physiological function
the enzyme is involved in flavonoid pathway. Flavonol synthase and dihydroflavonol-4-reductase compete for common substrates in order to direct the biosynthesis of flavonols and anthocyanins, respectively, thereby determining white vs. red coloration of flowers
physiological function
the enzyme is involved in flavonoid pathway. Flavonol synthase and dihydroflavonol-4-reductase compete for common substrates in order to direct the biosynthesis of flavonols and anthocyanins, respectively, thereby determining white vs. red coloration of flowers
physiological function
the enzyme is involved in flavonoid pathway. Flavonol synthase and dihydroflavonol-4-reductase compete for common substrates in order to direct the biosynthesis of flavonols and anthocyanins, respectively, thereby determining white vs. red coloration of flowers
physiological function
the enzyme is involved in flavonoid pathway. Flavonol synthase and dihydroflavonol-4-reductase compete for common substrates in order to direct the biosynthesis of flavonols and anthocyanins, respectively, thereby determining white vs. red coloration of flowers
physiological function
expression of FLS1 complements an Arabidopsis thaliana FLS1 mutant
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D223E
no catalytic activity
E295L
7% of wild-type activity
E295Q
48% of wild-type activity
F134A
15% of wild-type activity
F134L
54% of wild-type activity
F293A
8% of wild-type activity
F293L
9% of wild-type activity
H132F
124% of wild-type activity
H132Y
83% of wild-type activity
H221W
no catalytic activity
H277F
no catalytic activity
K202M
24% of wild-type activity
K202R
12% of wild-type activity
R287K
no catalytic activity
S289T
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
A120M
the mutant enzyme is able to oxidize dihydrokaempferol to kaempferol with 162% of the catalytic activity relative to wild-type enzyme
F146I
the mutant enzyme is able to oxidize dihydrokaempferol to kaempferol with 86% of the catalytic activity relative to wild-type enzyme
L311F
the mutant enzyme is able to oxidize dihydrokaempferol to kaempferol with 355% of the catalytic activity relative to wild-type enzyme
Y240P
the mutant enzyme is able to oxidize dihydrokaempferol to kaempferol with 104% of the catalytic activity relative to wild-type enzyme
Y240P/A120M
the mutant enzyme is able to oxidize dihydrokaempferol to kaempferol with 175% of the catalytic activity relative to wild-type enzyme
H132F
-
site-directed mutagenesis, the mutant shows similar kinetics with dihydrokaempferol compared to the wild-type enzyme
additional information
-
wild-type, fls1-2 single mutant and ldox/fls1-2 double mutant, lacking acitve form of flavonol synthase and leucoanthocyanidin dioxygenase, EC 1.14.11.19
additional information
a single base deletion in the flavonol synthase gene is responsible for the magenta flower mutant Harosoy due to a truncated polypeptide that lacks the dioxygenase domains A and B
additional information
-
a single base deletion in the flavonol synthase gene is responsible for the magenta flower mutant Harosoy due to a truncated polypeptide that lacks the dioxygenase domains A and B
additional information
silencing of FLS gene by RNAi, in lines G12, A2, B1 and E13, the quercetin content is increased by 351%, 49%, 157% and 258%, the silenced lines show arrest in pollen tube germination, and the pollen tubes grows only to about nine-tenths of the way down the style, and tube tips are swollen, contents of anthocyanins, epigallocatechin, and epicatechin are altered and content in indole acetic acid is reduced compared to the wild-type, overview
additional information
silencing of FLS gene by RNAi, in lines G12, A2, B1 and E13, the quercetin content is increased by 351%, 49%, 157% and 258%, the silenced lines show arrest in pollen tube germination, and the pollen tubes grows only to about nine-tenths of the way down the style, and tube tips are swollen, contents of anthocyanins, epigallocatechin, and epicatechin are altered and content in indole acetic acid is reduced compared to the wild-type, overview
additional information
-
silencing of FLS gene by RNAi, in lines G12, A2, B1 and E13, the quercetin content is increased by 351%, 49%, 157% and 258%, the silenced lines show arrest in pollen tube germination, and the pollen tubes grows only to about nine-tenths of the way down the style, and tube tips are swollen, contents of anthocyanins, epigallocatechin, and epicatechin are altered and content in indole acetic acid is reduced compared to the wild-type, overview
additional information
silencing of FLS gene using an ihpRNA construct from gene sequences of FLS and FLS1 and transferred to Agrobacterium tumefaciens strain LBA4404 through tri-parental mating, Agrobacterium tumefaciens-mediated transfection, phenotype, overview
additional information
silencing of FLS gene using an ihpRNA construct from gene sequences of FLS and FLS1 and transferred to Agrobacterium tumefaciens strain LBA4404 through tri-parental mating, Agrobacterium tumefaciens-mediated transfection, phenotype, overview
additional information
-
silencing of FLS gene using an ihpRNA construct from gene sequences of FLS and FLS1 and transferred to Agrobacterium tumefaciens strain LBA4404 through tri-parental mating, Agrobacterium tumefaciens-mediated transfection, phenotype, overview
additional information
silencing of FLS1 gene by RNAi, in lines G12, A2, B1 and E13, the quercetin content is increased by 351%, 49%, 157% and 258%, the silenced lines show arrest in pollen tube germination, and the pollen tubes grows only to about nine-tenths of the way down the style, and tube tips are swollen, contents of anthocyanins, epigallocatechin, and epicatechin are altered and content in indole acetic acid is reduced compared to the wild-type, overview
additional information
silencing of FLS1 gene by RNAi, in lines G12, A2, B1 and E13, the quercetin content is increased by 351%, 49%, 157% and 258%, the silenced lines show arrest in pollen tube germination, and the pollen tubes grows only to about nine-tenths of the way down the style, and tube tips are swollen, contents of anthocyanins, epigallocatechin, and epicatechin are altered and content in indole acetic acid is reduced compared to the wild-type, overview
additional information
-
silencing of FLS1 gene by RNAi, in lines G12, A2, B1 and E13, the quercetin content is increased by 351%, 49%, 157% and 258%, the silenced lines show arrest in pollen tube germination, and the pollen tubes grows only to about nine-tenths of the way down the style, and tube tips are swollen, contents of anthocyanins, epigallocatechin, and epicatechin are altered and content in indole acetic acid is reduced compared to the wild-type, overview
additional information
-
ZmFLS1 partially complements the flavonol deficiency of the Arabidopsis thaliana fls1 mutant, and restores anthocyanin accumulation to normal levels. ZmFLS1 is an immediate direct target of the P1 and C1/R regulatory complexes
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