1.14.11.9: flavanone 3-dioxygenase
This is an abbreviated version!
For detailed information about flavanone 3-dioxygenase, go to the full flat file.
Word Map on EC 1.14.11.9
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1.14.11.9
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chalcone
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anthocyanins
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dihydroflavonols
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flavonols
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anthocyanidin
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4-reductase
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ammonia-lyase
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3\'-hydroxylase
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petunia
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proanthocyanidins
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dihydrokaempferol
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leucoanthocyanidin
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3-o-glucosyltransferase
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2-oxoglutarate-dependent
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3',5'-hydroxylase
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r2r3-myb
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eriodictyol
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analysis
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testa
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udp-glucose:flavonoid
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2s-flavanones
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4-coumarate-coa
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dihydroflavonol-4-reductase
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dihydroquercetin
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2s-naringenin
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pelargonidin
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synthesis
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agriculture
- 1.14.11.9
- chalcone
- anthocyanins
- dihydroflavonols
- flavonols
- anthocyanidin
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4-reductase
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ammonia-lyase
-
3\'-hydroxylase
- petunia
- proanthocyanidins
- dihydrokaempferol
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leucoanthocyanidin
- 3-o-glucosyltransferase
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2-oxoglutarate-dependent
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3',5'-hydroxylase
-
r2r3-myb
- eriodictyol
- analysis
-
testa
-
udp-glucose:flavonoid
-
2s-flavanones
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4-coumarate-coa
- dihydroflavonol-4-reductase
- dihydroquercetin
- 2s-naringenin
- pelargonidin
- synthesis
- agriculture
Reaction
Synonyms
(2S)-flavanone 3-hydroxylase, AaF3H, AcF3H, BnF3H, CsF3H, CtF3H, F3H, F3H protein, F3H1, F3H2, FHT, FHTPH, flavanone 3-dioxygenase, flavanone 3-hydroxylase, flavanone 3beta-hydroxylase, flavanone synthase I, flavanone-3-hydroxylase, FLS1, FLS2, FS I, LcF3H, naringenin 3-dioxygenase, naringenin,2-oxoglutarate:oxygen oxidoreductase (3-hydroxylating), oxygenase, flavanone 3-di-, PeF3H, PgF3H, PnF3H, RtF3H1, RtF3H2, VcF3H
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Engineering
Engineering on EC 1.14.11.9 - flavanone 3-dioxygenase
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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
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
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
additional information
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in mutants lacking flavanone 3beta-hydroxylase, the enzymes flavonol synthase EC 1.14.11.23, and anthocyanidin synthase, EC 1.14.11.19, can partially compensate for its activity in vivo
additional information
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F3H silencing by fht antisense transgenic apple clones construction, diverse transgenic lines, phenotypes, overview
additional information
method evaluation for RNAi-mediated silencing downregulation of F3H expression, vector pJA8F3H is efficient and can be used as a transformation vector to transiently suppress F3H expression in waterlily or lotus
additional information
method evaluation for RNAi-mediated silencing downregulation of F3H expression, introduction of RNAi gene-silencing vector, pJA8F3H, encoding a hairpin F3H RNA, to waterlily petals using the Agrobacterium tumefaciens strain GV3101 infiltration method, F3H expression is analysed at 1 and 3 days post infiltration semi-quantitative RT-PCR, showing that F3H expression is downregulated at 3 dpi in flowers tested of the red petal variety and purplish blue petal variety compared to controls. Vector pJA8F3H is efficient and can be used as a transformation vector to transiently suppress F3H expression in waterlily or lotus
additional information
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domain swapping experiments joining the N-terminus of flavanone 3beta-hydroxylase with the C-terminus of flavone synthase I and vice versa. Active site residues of flavanone 3beta-hydroxylase are M106, I115, V116, I131, D195, V200, L215, and K216
additional information
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four C-terminally truncated enzyme forms are generated by deletion of five, 11, 24 or 29 amino acids. The recombinant enzymes preserve their substrate electrivity, but the specific activity decreases gradually with the extent of truncation. An enzyme chimera is constructed by domain swapping replacing the C-terminal 52 amino acids of the Petunia enzyme by equivalent region of flavonol synthase from Citrus unshiu
additional information
the enzyme is ngineered for synthesizing polyphenol core structuressuch as the stilbene resveratrol and the (2S)-flavanone naringenin
additional information
the enzyme is ngineered for synthesizing polyphenol core structuressuch as the stilbene resveratrol and the (2S)-flavanone naringenin
additional information
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construction of transgenic Arabidospis thaliana plants expressing the enzyme from Pohlia nutans, the Agrobacterium tumefaciens-mediated transformation of gene PnF3H confers tolerance to salt stress and abscisic acid treatment in transgenic Arabidopsis, naringenin-feeding experiments and flavonoid metabolism profiling by HPLC analysis, phenotype, overview