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
-
4-reductase
-
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
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r2r3-myb
- eriodictyol
- analysis
-
testa
-
udp-glucose:flavonoid
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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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General Information
General Information on EC 1.14.11.9 - flavanone 3-dioxygenase
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evolution
malfunction
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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
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no significant genetic differentiation is found between cultivated soybean, Glycine max, and its wild relative, Glycine soja, in the target gene, despite of considering bottleneck and founder effect during domestication. The F3H gene might have experienced gene introgressions or diversifying selection events during domestication process, gene F3H2 appears to evolve under positive selection and enjoy a faster evolutionary rate
evolution
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no significant genetic differentiation is found between cultivated soybean, Glycine max, and its wild relative, Glycine soja, in the target gene, despite of considering bottleneck and founder effect during domestication. The F3H gene might have experienced gene introgressions or diversifying selection events during domestication process, gene F3H2 appears to evolve under positive selection and enjoy a faster evolutionary rate
evolution
the F3H isozymes have a unique motif of pfam03171 that is maintained in the superfamily of 2-oxoglutarate and Fe(II)-dependent oxygenases
evolution
the enzyme belongs to the 2-oxoglutarate-dependent dioxygenase (2-ODD) family
evolution
the enzyme belongs to the family of 2-oxoglutarate-dependent dioxygenases
evolution
the enzyme belongs to the Fe(II)- and 2-oxoglutarate-dependent dioxygenase (2-ODD) superfamily, sharing the conserved motif of pfam 03171. F3H has a jelly roll in the enzyme core, a typical structure shared by all 2-oxoglutarate-dependent dioxygenases including F3Hs. Phylogenetic and molecular evolutionary analyses
evolution
the enzyme belongs to the Fe2+/2oxoglutarate-dependent dioxygenase superfamily
metabolism
flavanone 3-hydroxylase converts flavanones to dihydroflavonols for anthocyanin biosynthesis
metabolism
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the enzyme is involved in the flavonoid and phenylpropanoid biosynthesis pathway, overview
metabolism
flavanone 3-hydroxylase is a key enzyme at a diverging point of the flavonoid pathway leading to production of different pigments: phlobaphene, proanthocyanidin, and anthocyanin, flavonoid biosynthetic pathway, overview
metabolism
the enzyme is involved in anthocyanin biosynthesis
metabolism
(2S)-flavanones are converted to flavonols by the activity of the 2-oxoglutarate-dependent dioxygenases flavanone 3-hydroxylase (F3H) and flavonol synthase (FLS)
metabolism
flavanone 3-hydroxylase (F3H) of the flavonoid pathway catalyzes the stereospecific hydroxylation of (2S)-naringenin and (2S)-eriodictyol to form (2R,3R)-dihydrokaempferol and (2R,3R)-dihydroquercetin, respectively. These dihydroflavonols serve as intermediates for the biosynthesis of flavan-3-ols. Enzyme F3H plays a pivotal role in regulation of biosynthesis of flavan-3-ols in Camellia sinensis
metabolism
positive correlation between absisic acid and LcF3H expression level
metabolism
Camellia sinensis UPASI-10
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flavanone 3-hydroxylase (F3H) of the flavonoid pathway catalyzes the stereospecific hydroxylation of (2S)-naringenin and (2S)-eriodictyol to form (2R,3R)-dihydrokaempferol and (2R,3R)-dihydroquercetin, respectively. These dihydroflavonols serve as intermediates for the biosynthesis of flavan-3-ols. Enzyme F3H plays a pivotal role in regulation of biosynthesis of flavan-3-ols in Camellia sinensis
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metabolism
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the enzyme is involved in the flavonoid and phenylpropanoid biosynthesis pathway, overview
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flavanone 3-hydroxylase converts flavanones to dihydroflavonols for anthocyanin biosynthesis, F3H is a key flavonoid structural gene
physiological function
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flavanone 3-hydroxylase is involved in the biosynthesis of flavonoids, which play diverse roles in stress responses
physiological function
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flavanone 3-hydroxylase is involved in the biosynthesis of flavonoids, which play diverse roles in stress responses
physiological function
the enzyme is involved in the red pigmentation of grain tissues, overview
physiological function
F3H is a key regulator for the flavonoid biosynthesis pathway and plays a role in accumulation of anthocyanin pigments in the vacuole
physiological function
F3H is a key regulator for the flavonoid biosynthesis pathway and plays a role in accumulation of anthocyanin pigments in the vacuole
physiological function
flavanone 3-hydroxylase (F3H) is an important regulatory enzyme of the flavonoid pathway which catalyzes the stereospecific hydroxylation of (2S)-naringenin to form (2R,3R)-dihydroflavonol. These dihydroflavonols serve as intermediates for the biosynthesis of anthocyanidins and flavonols
physiological function
flavanone 3-hydroxylase (F3H) is one of the nuclear enzymes acting at the bifurcation of the flavonoid biosynthetic pathway, initiating catalysis of the 3-hydroxylation of (2S)-flavanones, such as naringenin to dihydroflavonols
physiological function
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the enzyme plays a role in plant salt stress resistance. PnF3H transcripts are induced by various stress and may play a positive role in stress tolerance
physiological function
the F3H gene, which encodes flavanone 3-hydroxylase, is a key regulatory gene in the flavonoid biosynthetic pathway for production of flavonoids and anthocyanins. Anthocyanins accumulate mainly in blueberry fruits, while flavonols are mainly found in leaves and stems
physiological function
the F3H gene, which encodes flavanone-3-hydroxylase, is an essential gene in the flavonoid biosynthetic pathway
physiological function
the flavanone 3-hydroxylase (F3H) gene which encodes flavanone 3-hydroxylase, is essential in flavonoids biosynthetic pathway. Lycium chinense (L. chinense) is a deciduous woody perennial halophyte that grows under a large variety of environmental conditions and survives under extreme drought stress, possible relationship between the oxidative damage and the regulation of LcF3H gene expression in Lycium chinense under drought stress
physiological function
the enzyme plays an important role in biosynthesis of flavonoids
physiological function
the enzyme plays an important role in the biosynthesis of spruce phenolic defenses against bark beetles and their fungal associates. The enzyme forms a defensive product, taxifolin, which is also a metabolic precursor of another defensive product, catechin, which in turn synergizes the toxicity of taxifolin to the bark beetle associated fungus
in Sorghum seedlings, expression of the two F3H genes is either absent or strongly suppressed during the accumulation of 3-deoxyanthocyanidins
additional information
the Arg285-X-Ser287 motif (RXS) takes part in 2-oxoglutarate binding
additional information
the 2S-naringenin substrate binding site of RtF3H1 consists of Ser135, Try149, Val214, Arg299, and Val304
additional information
the 2S-naringenin substrate binding site of RtF3H1 consists of Ser135, Try149, Val214, Arg299, and Val304
additional information
the 2S-naringenin substrate binding site of RtF3H2 consists of Ser135, Phe149, Ile214, Arg299, and Ala305
additional information
the 2S-naringenin substrate binding site of RtF3H2 consists of Ser135, Phe149, Ile214, Arg299, and Ala305
additional information
three-dimensional protein structure modeling, overview