1.14.20.6: flavonol synthase
This is an abbreviated version!
For detailed information about flavonol synthase, go to the full flat file.
Word Map on EC 1.14.20.6
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1.14.20.6
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flavonols
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flavanone
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chalcone
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dihydroflavonols
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kaempferol
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anthocyanidins
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4-reductase
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dihydrokaempferol
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3\'-hydroxylase
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leucoanthocyanidin
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r2r3-myb
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dihydroquercetin
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3beta-hydroxylase
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fagopyrum
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tataricum
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2-odds
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2s-naringenin
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dihydroflavonol-4-reductase
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unshius
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analysis
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synthesis
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tartary
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flavonol-specific
- 1.14.20.6
- flavonols
- flavanone
- chalcone
- dihydroflavonols
- kaempferol
- anthocyanidins
-
4-reductase
- dihydrokaempferol
-
3\'-hydroxylase
-
leucoanthocyanidin
-
r2r3-myb
- dihydroquercetin
-
3beta-hydroxylase
- fagopyrum
- tataricum
- 2-odds
- 2s-naringenin
- dihydroflavonol-4-reductase
- unshius
- analysis
- synthesis
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tartary
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flavonol-specific
Reaction
Synonyms
AaFLS1, BnFLS, Cs-COR054, Cs-COR113, EC 1.14.11.23, FKS2, flavonoid 2-oxoglutarate-dependent dioxygenase, flavonol synthase, FLS, FLS1, FLS2, fls3, McFLS, NtFLS1, PhFLS, PpFLS, RrFLS1, SbFLS, VcFLS
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General Information
General Information on EC 1.14.20.6 - flavonol synthase
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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
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
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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
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ZmFLS1 is a key flavonoid biosynthetic enzyme and involved in control of flavonol accumulation in maize
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
part of flavonoid biosynthesis pathway
physiological function
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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
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