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Enzyme Nomenclature
Information on EC 1.1.1.219 - dihydroflavonol 4-reductase
for references in articles please use BRENDA:EC1.1.1.219
Word Map on EC 1.1.1.219
- 1.1.1.219
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anthocyanins
- flavonoid
- chalcone
- flower
- flavanone
- cultivar
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proanthocyanidins
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phenylpropanoids
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ammonia-lyase
- petunia
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leucoanthocyanidins
- hybrida
- pelargonidins
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3\'-hydroxylase
- majus
- gerbera
- delphinidin
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3',5'-hydroxylase
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r2r3-myb
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3-o-glucosyltransferase
- antirrhinum
- molecular biology
- agriculture
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white-flowered
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3-o-glucosyl
- snapdragon
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udp-glucose:flavonoid
- leucocyanidin
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flavonoid-related
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
1.1.1.219
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RECOMMENDED NAME
GeneOntology No.
dihydroflavonol 4-reductase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a (2R,3S,4S)-leucoanthocyanidin + NADP+ = a (2R,3R)-dihydroflavonol + NADPH + H+
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
redox reaction
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reduction
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oxidation
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
(2R,3S,4S)-leucoanthocyanidin:NADP+ 4-oxidoreductase
This plant enzyme, involved in the biosynthesis of anthocyanidins, is known to act on (+)-dihydrokaempferol, (+)-taxifolin, and (+)-dihydromyricetin, although some enzymes may act only on a subset of these compounds. Each dihydroflavonol is reduced to the corresponding cis-flavan-3,4-diol. NAD+ can act instead of NADP+, but more slowly.
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CAS REGISTRY NUMBER
COMMENTARY
83682-99-9
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98668-58-7
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
var. miniata, an orange flowered variety, and var. citrina, a yellow flowered variety
UniProt
cvs. Palgangbaechu, 8053, and Seoulbaechu
UniProt
Fragaria chiloensis x Fragaria virginiana, cv. Elsanta
UniProt
isozyme MtDFR1; cv. Jemalong, 2 isozymes MtDFR1 and MtDFR2
SwissProt
isozyme MtDFR2; cv. Jemalong, 2 isozymes MtDFR1 and MtDFR2
SwissProt
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
the enzyme belongs to the plant DFR superfamily, phylogenetic analysis
evolution
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DFR gene, which encodes dihyroflavonol 4-reductase, is the candidate gene for the anthocyaninless (ANL) locus in RCBr. DFR shows complete linkage with ANL in genetic crosses with a total of 948 informative chromosomes
evolution
three DFR cDNA clones GbDFRs occur in the gymnosperm Ginkgo biloba. The deduced GbDFR proteins show high identities to other plant DFRs, which form three distinct DFR families. The three GbDFRs each belong to a different DFR family. Phylogenetic tree analysis reveals that the GbDFRs share the same ancestor as other DFRs; three DFR cDNA clones GbDFRs occur in the gymnosperm Ginkgo biloba. The deduced GbDFR proteins show high identities to other plant DFRs, which form three distinct DFR families. The three GbDFRs each belong to a different DFR family. Phylogenetic tree analysis reveals that the GbDFRs share the same ancestor as other DFRs
evolution
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DFR gene, which encodes dihyroflavonol 4-reductase, is the candidate gene for the anthocyaninless (ANL) locus in RCBr. DFR shows complete linkage with ANL in genetic crosses with a total of 948 informative chromosomes
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malfunction
overexpressing the Triticum aestivum dihydroflavonol 4-reductase gene TaDFR increases anthocyanin accumulation in an Arabidopsis thaliana dfr mutant
malfunction
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strain DWRCBr57 with the recessive nonpurple phenotype has a transposon-related insertion in the DFR which is predicted to disrupt gene function. Non-purple strains bear an insertion mutation in exon 4 of the DFR gene. Some purple plants have an insertion mutation in the last intron
malfunction
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downregulation of IbDFR expression in transgenic sweet potato (DFRi) using an RNAi approach dramatically reduces anthocyanin accumulation in young leaves, stems and storage roots. The increase of flavonols quercetin-3-O-hexose-hexoside and quercetin-3-O-glucoside in the leaves and roots of DFRi plants is significant. The metabolic pathway channels greater flavonol influx in the DFRi plants when their anthocyanin and proanthocyanidin accumulation are decreased. These plants also display reduced antioxidant capacity compared to the wild-type. After 24 h of cold treatment and 2 h recovery, the wild-type plants are almost fully restored to the initial phenotype compared to the slower recovery of DFRi plants, in which the levels of electrolyte leakage and hydrogen peroxide accumulation are dramatically increased
malfunction
overexpression of McDFR, or silencing of McFLS, increases anthocyanin production, resulting in red-leaf and red fruit peel phenotypes, while overexpression of McFLS, or silencing of McDFR, increase anthocyanin production, resulting in red-leaf and red fruit peel phenotypes
malfunction
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strain DWRCBr57 with the recessive nonpurple phenotype has a transposon-related insertion in the DFR which is predicted to disrupt gene function. Non-purple strains bear an insertion mutation in exon 4 of the DFR gene. Some purple plants have an insertion mutation in the last intron
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metabolism
the DFR gene is a key gene late in the flavonoid biosynthesis pathway, overview. The enzyme is a key enzyme in the biosynthesis of anthocyanidins, proanthocyanidins, and other flavonoids, and also possesses flavanone 4-reductase activity
metabolism
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dihydroflavonol-4-reductase (DFR) is a key enzyme in the catalysis of the stereospecific reduction of dihydroflavonols to leucoanthocyanidins in anthocyanin biosynthesis
metabolism
dihydroflavonol 4-reductase, McDFR, and flavonol synthase, McFLS, 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. Flavonoid biosynthetic pathway in plant, overview
physiological function
catechins accumulation in tea leaves are regulated by the mRNA accumulation of genes involved in the biosynthesis, which are PAL, CHS, F3H, DFR, and LCR
physiological function
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DFR plays a key role in determining intensity and pigment coloration because its specificity and activities dictate the type and amount of the colorless leucoanthocyanidins
physiological function
DFR plays a key role in determining intensity and pigment coloration because its specificity and activities dictate the type and amount of the colorless leucoanthocyanidins
physiological function
DFR plays a key role in determining intensity and pigment coloration because its specificity and activities dictate the type and amount of the colorless leucoanthocyanidins
physiological function
DFR plays a key role in determining intensity and pigment coloration because its specificity and activities dictate the type and amount of the colorless leucoanthocyanidins
physiological function
DFR plays a key role in determining intensity and pigment coloration because its specificity and activities dictate the type and amount of the colorless leucoanthocyanidins
physiological function
DFR plays a key role in determining intensity and pigment coloration because its specificity and activities dictate the type and amount of the colorless leucoanthocyanidins
physiological function
DFR expression induces and is correlated with anthocyanin accumulation in the petals, induced anthocyanins are primarily cyanidin, along with a small amount of pelargonidin
physiological function
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synthesis of(+)-catechin by leucoanthocyanidin reductase may be tied to regulation of DFR
physiological function
DFR can fully complement the potato locus R, both in terms of tuber color and anthocyanin composition
physiological function
the enzyme is of importance in plant development
physiological function
overexpressing isoform DFR2 in Populus tomentosa Carr improves condensed tannin accumulations; overexpression in Nicotiana tabacum leads to color change in flowers, giving much darker pink flowers. Transgenic plants show a significantly higher accumulation of anthocyanins. Overexpressing isofrm DFR1 in Populus tomentosa Carr results in a higher accumulation of both anthocyanins and condensed tannins
physiological function
transgenic tobacco overexpressing tea cDNA encoding dihydroflavonol 4-reductase and anthocyanidin reductase induces early flowering, and provides biotic stress tolerance, better seed yield, and higher content of flavonoids, e.g. of flavan-3-ols such as catechin, epicatechin and epicatechingallate. The recombinant plants show free increased radical scavenging activity and better resistance to oxidative stress or against infestation by a tobacco leaf cutworm Spodoptera litura
physiological function
BrDFR isozymes are regulated by two transcription factors, BrMYB2-2 and BrTT8, contrasting with anthocyanin accumulation and cold and freezing stress; BrDFR isozymes are regulated by two transcription factors, BrMYB2-2 and BrTT8, contrasting with anthocyanin accumulation and cold and freezing stress; BrDFR isozymes are regulated by two transcription factors, BrMYB2-2 and BrTT8, contrasting with anthocyanin accumulation and cold and freezing stress; BrDFR isozymes are regulated by two transcription factors, BrMYB2-2 and BrTT8, contrasting with anthocyanin accumulation and cold and freezing stress; BrDFR isozymes are regulated by two transcription factors, BrMYB2-2 and BrTT8, contrasting with anthocyanin accumulation and cold and freezing stress; BrDFR isozymes are regulated by two transcription factors, BrMYB2-2 and BrTT8, contrasting with anthocyanin accumulation and cold and freezing stress; BrDFR isozymes are regulated by two transcription factors, BrMYB2-2 and BrTT8, contrasting with anthocyanin accumulation and cold and freezing stress; BrDFR isozymes are regulated by two transcription factors, BrMYB2-2 and BrTT8, contrasting with anthocyanin accumulation and cold and freezing stress; BrDFR isozymes are regulated by two transcription factors, BrMYB2-2 and BrTT8, contrasting with anthocyanin accumulation and cold and freezing stress; BrDFR isozymes are regulated by two transcription factors, BrMYB2-2 and BrTT8, contrasting with anthocyanin accumulation and cold and freezing stress; BrDFR isozymes are regulated by two transcription factors, BrMYB2-2 and BrTT8, contrasting with anthocyanin accumulation and cold and freezing stress; BrDFR isozymes are regulated by two transcription factors, BrMYB2-2 and BrTT8, contrasting with anthocyanin accumulation and cold and freezing stress
physiological function
the enzyme catalyzes the conversion of dihydroflavonol to leucoanthocyanidins during anthocyanin biosynthesis. TaDFR-I complements the function of DFR in Arabidopsis thaliana dfr mutant
physiological function
dihydroflavonol-4-reductase catalyzes a key step late in the biosynthesis of anthocyanins, condensed tannins (proanthocyanidins), and other flavonoids. GbDFR1 appears to be involved in environmental stress response; dihydroflavonol-4-reductase catalyzes a key step late in the biosynthesis of anthocyanins, condensed tannins (proanthocyanidins), and other flavonoids. GbDFR2 is mainly involved in responses to plant hormones, environmental stress and damage; dihydroflavonol-4-reductase catalyzes a key step late in the biosynthesis of anthocyanins, condensed tannins (proanthocyanidins), and other flavonoids. GbDFR3 likely has primary functions in the synthesis of anthocyanins
physiological function
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the enzyme expression is strongly associated with anthocyanin accumulation in leaves, stems and roots. The enzyme plays important roles in flavonoid metabolism, protective function of anthocyanins in enhanced scavenging of reactive oxygen radicals in plants under stressful conditions
physiological function
dihydroflavonol 4-reductase, DFR, is an oxidoreductase which catalyzes the NADPH dependent reduction of the keto group in position 4 of dihydroflavonols to produce flavan 3,4-diols (synonym: leucoanthocyanidins), which are the immediate precursors for the formation of anthocyanidins and flavan 3-ols, the building blocks of condensed tannins. DFR competes with flavonol synthase for dihydroflavonols as common substrates and therefore interferes with flavonol formation. Enzyme DFR has a strong influence on the formation of at least 3 classes of flavonoids, anthocyanin pigments, flavanols (which provide protection against herbivore, pests and pathogens), and flavonols (which act as sunscreens). DFR exhibits selectivity for the B-ring hydroxylation pattern of flavonoid substrates; dihydroflavonol 4-reductase, DFR, is an oxidoreductase which catalyzes the NADPH dependent reduction of the keto group in position 4 of dihydroflavonols to produce flavan 3,4-diols (synonym: leucoanthocyanidins), which are the immediate precursors for the formation of anthocyanidins and flavan 3-ols, the building blocks of condensed tannins. DFR competes with flavonol synthase for dihydroflavonols as common substrates and therefore interferes with flavonol formation. Enzyme DFR has a strong influence on the formation of at least 3 classes of flavonoids, anthocyanin pigments, flavanols (which provide protection against herbivore, pests and pathogens), and flavonols (which act as sunscreens). DFR exhibits selectivity for the B-ring hydroxylation pattern of flavonoid substrates; dihydroflavonol 4-reductase, DFR, is an oxidoreductase which catalyzes the NADPH dependent reduction of the keto group in position 4 of dihydroflavonols to produce flavan 3,4-diols (synonym: leucoanthocyanidins), which are the immediate precursors for the formation of anthocyanidins and flavan 3-ols, the building blocks of condensed tannins. DFR competes with flavonol synthase for dihydroflavonols as common substrates and therefore interferes with flavonol formation. Enzyme DFR has a strong influence on the formation of at least 3 classes of flavonoids, anthocyanin pigments, flavanols (which provide protection against herbivore, pests and pathogens), and flavonols (which act as sunscreens). DFR exhibits selectivity for the B-ring hydroxylation pattern of flavonoid substrates; dihydroflavonol 4-reductase, DFR, is an oxidoreductase which catalyzes the NADPH dependent reduction of the keto group in position 4 of dihydroflavonols to produce flavan 3,4-diols (synonym: leucoanthocyanidins), which are the immediate precursors for the formation of anthocyanidins and flavan 3-ols, the building blocks of condensed tannins. DFR competes with flavonol synthase for dihydroflavonols as common substrates and therefore interferes with flavonol formation. Enzyme DFR has a strong influence onthe formation of at least 3 classes of flavonoids, anthocyanin pigments, flavanols (which provide protection against herbivore, pests and pathogens), and flavonols (which act as sunscreens). DFR exhibits selectivity for the B-ring hydroxylation pattern of flavonoid substrates; dihydroflavonol 4-reductase, DFR, is an oxidoreductase which catalyzes the NADPH dependent reduction of the keto group in position 4 of dihydroflavonols to produce flavan 3,4-diols (synonym: leucoanthocyanidins), which are the immediate precursors for the formation of anthocyanidins and flavan 3-ols, the building blocks of condensed tannins. DFR competes with flavonol synthase for dihydroflavonols as common substrates and therefore interferes with flavonol formation. Enzyme DFR has a strong influence onthe formation of at least 3 classes of flavonoids, anthocyanin pigments, flavanols (which provide protection against herbivore, pests and pathogens), and flavonols (which act as sunscreens). DFR exhibits selectivity for the B-ring hydroxylation pattern of flavonoid substrates; dihydroflavonol 4-reductase, DFR, is an oxidoreductase which catalyzes the NADPH dependent reduction of the keto group in position 4 of dihydroflavonols to produce flavan 3,4-diols (synonym: leucoanthocyanidins), which are the immediate precursors for the formation of anthocyanidins and flavan 3-ols, the building blocks of condensed tannins. DFR competes with flavonol synthase for dihydroflavonols as common substrates and therefore interferes with flavonol formation. Enzyme DFR has a strong influence onthe formation of at least 3 classes of flavonoids, anthocyanin pigments, flavanols (which provide protection against herbivore, pests and pathogens), and flavonols (which act as sunscreens). DFR exhibits selectivity for the B-ring hydroxylation pattern of flavonoid substrates
physiological function
dihydroflavonol 4-reductase, DFR, is an oxidoreductase which catalyzes the NADPH dependent reduction of the keto group in position 4 of dihydroflavonols to produce flavan 3,4-diols (synonym: leucoanthocyanidins), which are the immediate precursors for the formation of anthocyanidins and flavan 3-ols, the building blocks of condensed tannins. DFR competes with flavonol synthase for dihydroflavonols as common substrates and therefore interferes with flavonol formation. Enzyme DFR has a strong influence on the formation of at least 3 classes of flavonoids, anthocyanin pigments, flavanols (which provide protection against herbivore, pests and pathogens), and flavonols (which act as sunscreens). DFR exhibits selectivity for the B-ring hydroxylation pattern of flavonoid substrates; dihydroflavonol 4-reductase, DFR, is an oxidoreductase which catalyzes the NADPH dependent reduction of the keto group in position 4 of dihydroflavonols to produce flavan 3,4-diols (synonym: leucoanthocyanidins), which are the immediate precursors for the formation of anthocyanidins and flavan 3-ols, the building blocks of condensed tannins. DFR competes with flavonol synthase for dihydroflavonols as common substrates and therefore interferes with flavonol formation. Enzyme DFR has a strong influence on the formation of at least 3 classes of flavonoids, anthocyaninpigments, flavanols (which provide protection against herbivore, pests and pathogens), and flavonols (which act as sunscreens). DFR exhibits selectivity for the B-ring hydroxylation pattern of flavonoid substrates; dihydroflavonol 4-reductase, DFR, is an oxidoreductase which catalyzes the NADPH dependent reduction of the keto group in position 4 of dihydroflavonols to produce flavan 3,4-diols (synonym: leucoanthocyanidins), which are the immediate precursors for the formation of anthocyanidins and flavan 3-ols, the building blocks of condensed tannins. DFR competes with flavonol synthase for dihydroflavonols as common substrates and therefore interferes with flavonol formation. Enzyme DFR has a strong influence onthe formation of at least 3 classes of flavonoids, anthocyanin pigments, flavanols (which provide protection against herbivore, pests and pathogens), and flavonols (which act as sunscreens). DFR exhibits selectivity for the B-ring hydroxylation pattern of flavonoid substrates; dihydroflavonol 4-reductase, DFR, is an oxidoreductase which catalyzes the NADPH dependent reduction of the keto group in position 4 of dihydroflavonols to produce flavan 3,4-diols (synonym: leucoanthocyanidins), which are the immediate precursors for the formation of anthocyanidins and flavan 3-ols, the building blocks of condensed tannins. DFR competes with flavonol synthase for dihydroflavonols as common substrates and therefore interferes with flavonol formation. Enzyme DFR has a strong influence onthe formation of at least 3 classes of flavonoids, anthocyanin pigments, flavanols (which provide protection against herbivore, pests and pathogens), and flavonols (which act as sunscreens). DFR exhibits selectivity for the B-ring hydroxylation pattern of flavonoid substrates
physiological function
McDFR expression is associated with red color formation in crabapple leaves. Concentrations of anthocyanins and flavonols correlate with leaf color, the expression of dihydroflavonol 4-reductase, McDFR, and flavonol synthase, McFLS, influences their accumulation. Enzyme McDFR is an important determinant of the red color of crabapple leaves. The relative activities of McDFR and McFLS are important determinants of the red color of crabapple leaves
physiological function
dihydroflavonol 4-reductase, DFR, is a key enzyme responsible for the NADPH-dependent reduction of dihydroflavonols to colourless leucoanthocyanidins
additional information
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the gene encoding dihydroflavonol 4-reductase is a candidate for the anthocyaninless locus of rapid cycling Brassica rapa (fast plants type)
additional information
differences in the fruit colour of the two Fragaria species Fragaria vesca and Fragaria ananassa can be explained by the higher expression of DFR1 in Fragaria ananassa as compared to Fragaria vesca, a higher enzyme efficiency of DFR1 combined with the loss of F3'H activity late in fruit development of Fragaria ananassa; differences in the fruit colour of the two Fragaria species Fragaria vesca and Fragaria ananassa can be explained by the higher expression of DFR1 in Fragaria ananassa as compared to Fragaria vesca, a higher enzyme efficiency of DFR1 combined with the loss of F3'H activity late in fruit development of Fragaria ananassa; differences in the fruit colour of the two Fragaria species Fragaria vesca and Fragaria ananassa can be explained by the higher expression of DFR1 in Fragaria ananassa as compared to Fragaria vesca, a higher enzyme efficiency of DFR1 combined with the loss of F3'H activity late in fruit development of Fragaria ananassa; differences in the fruit colour of the two Fragaria species Fragaria vesca and Fragaria ananassa can be explained by the higher expression of DFR1 in Fragaria ananassa as compared to Fragaria vesca, a higher enzyme efficiency of DFR1 combined with the loss of F3'H activity late in fruit development of Fragaria ananassa; differences in the fruit colour of the two Fragaria species Fragaria vesca and Fragaria ananassa can be explained by the higher expression of DFR1 in Fragaria ananassa as compared to Fragaria vesca, a higher enzyme efficiency of DFR1 combined with the loss of F3'H activity late in fruit development of Fragaria ananassa
additional information
differences in the fruit colour of the two Fragaria species Fragaria vesca and Fragaria ananassa can be explained by the higher expression of DFR1 in Fragaria ananassa as compared to Fragaria vesca, a higher enzyme efficiency of DFR1 combined with the loss of F3'H activity late in fruit development of Fragaria ananassa; differences in the fruit colour of the two Fragaria species Fragaria vesca and Fragaria ananassa can be explained by the higher expression of DFR1 in Fragaria ananassa as compared to Fragaria vesca, a higher enzyme efficiency of DFR1 combined with the loss of F3'H activity late in fruit development of Fragaria ananassa; differences in the fruit colour of the two Fragaria species Fragaria vesca and Fragaria ananassa can be explained by the higher expression of DFR1 in Fragaria ananassa as compared to Fragaria vesca, a higher enzyme efficiency of DFR1 combined with the loss of F3'H activity late in fruit development of Fragaria ananassa; differences in the fruit colour of the two Fragaria species Fragaria vesca and Fragaria ananassa can be explained by the higher expression of DFR1 in Fragaria ananassa as compared to Fragaria vesca, a higher enzyme efficiency of DFR1 combined with the loss of F3'H activity late in fruit development of Fragaria ananassa; differences in the fruit colour of the two Fragaria species Fragaria vesca and Fragaria ananassa can be explained by the higher expression of DFR1 in Fragaria ananassa as compared to Fragaria vesca, a higher enzyme efficiency of DFR1 combined with the loss of F3'H activity late in fruit development of Fragaria ananassa
additional information
differences in the fruit colour of the two Fragaria species Fragaria vesca and Fragaria ananassa can be explained by the higher expression of DFR1 in Fragaria ananassa as compared to Fragaria vesca, a higher enzyme efficiency of DFR1 combined with the loss of F3'H activity late in fruit development of Fragaria ananassa; differences in the fruit colour of the two Fragaria species Fragaria vesca and Fragaria ananassa can be explained by the higher expression of DFR1 in Fragaria ananassa as compared to Fragaria vesca, a higher enzyme efficiency of DFR1 combined with the loss of F3'H activity late in fruit development of Fragaria ananassa; differences in the fruit colour of the two Fragaria species Fragaria vesca and Fragaria ananassa can be explained by the higher expression of DFR1 in Fragaria ananassa as compared to Fragaria vesca, a higher enzyme efficiency of DFR1 combined with the loss of F3'H activity late in fruit development of Fragaria ananassa; differences in the fruit colour of the two Fragaria species Fragaria vesca and Fragaria ananassa can be explained by the higher expression of DFR1 in Fragaria ananassa as compared to Fragaria vesca, a higher enzyme efficiency of DFR1 combined with the loss of F3'H activity late in fruit development of Fragaria ananassa; differences in the fruit colour of the two Fragaria species Fragaria vesca and Fragaria ananassa can be explained by the higher expression of DFR1 in Fragaria ananassa as compared to Fragaria vesca, a higher enzyme efficiency of DFR1 combined with the loss of F3'H activity late in fruit development of Fragaria ananassa
additional information
differences in the fruit colour of the two Fragaria species Fragaria vesca and Fragaria ananassa can be explained by the higher expression of DFR1 in Fragaria ananassa as compared to Fragaria vesca, a higher enzyme efficiency of DFR1 combined with the loss of F3'H activity late in fruit development of Fragaria ananassa; differences in the fruit colour of the two Fragaria species Fragaria vesca and Fragaria ananassa can be explained by the higher expression of DFR1 in Fragaria ananassa as compared to Fragaria vesca, a higher enzyme efficiency of DFR1 combined with the loss of F3'H activity late in fruit development of Fragaria ananassa; differences in the fruit colour of the two Fragaria species Fragaria vesca and Fragaria ananassa can be explained by the higher expression of DFR1 in Fragaria ananassa as compared to Fragaria vesca, a higher enzyme efficiency of DFR1 combined with the loss of F3'H activity late in fruit development of Fragaria ananassa; differences in the fruit colour of the two Fragaria species Fragaria vesca and Fragaria ananassa can be explained by the higher expression of DFR1 in Fragaria ananassa as compared to Fragaria vesca, a higher enzyme efficiency of DFR1 combined with the loss of F3'H activity late in fruit development of Fragaria ananassa; differences in the fruit colour of the two Fragaria species Fragaria vesca and Fragaria ananassa can be explained by the higher expression of DFR1 in Fragaria ananassa as compared to Fragaria vesca, a higher enzyme efficiency of DFR1 combined with the loss of F3'H activity late in fruit development of Fragaria ananassa
additional information
differences in the fruit colour of the two Fragaria species Fragaria vesca and Fragaria ananassa can be explained by the higher expression of DFR1 in Fragaria ananassa as compared to Fragaria vesca, a higher enzyme efficiency of DFR1 combined with the loss of F3'H activity late in fruit development of Fragaria ananassa; differences in the fruit colour of the two Fragaria species Fragaria vesca and Fragaria ananassa can be explained by the higher expression of DFR1 in Fragaria ananassa as compared to Fragaria vesca, a higher enzyme efficiency of DFR1 combined with the loss of F3'H activity late in fruit development of Fragaria ananassa; differences in the fruit colour of the two Fragaria species Fragaria vesca and Fragaria ananassa can be explained by the higher expression of DFR1 in Fragaria ananassa as compared to Fragaria vesca, a higher enzyme efficiency of DFR1 combined with the loss of F3'H activity late in fruit development of Fragaria ananassa; differences in the fruit colour of the two Fragaria species Fragaria vesca and Fragaria ananassa can be explained by the higher expression of DFR1 in Fragaria ananassa as compared to Fragaria vesca, a higher enzyme efficiency of DFR1 combined with the loss of F3'H activity late in fruit development of Fragaria ananassa; differences in the fruit colour of the two Fragaria species Fragaria vesca and Fragaria ananassa can be explained by the higher expression of DFR1 in Fragaria ananassa as compared to Fragaria vesca, a higher enzyme efficiency of DFR1 combined with the loss of F3'H activity late in fruit development of Fragaria ananassa
additional information
differences in the fruit colour of the two Fragaria species Fragaria vesca and Fragaria ananassa can be explained by the higher expression of DFR1 in Fragaria ananassa as compared to Fragaria vesca, a higher enzyme efficiency of DFR1 combined with the loss of F3'H activity late in fruit development of Fragaria ananassa; differences in the fruit colour of the two Fragaria species Fragaria vesca and Fragaria ananassa can be explained by the higher expression of DFR1 in Fragaria ananassa as compared to Fragaria vesca, a higher enzyme efficiency of DFR1 combined with the loss of F3'H activity late in fruit development of Fragaria ananassa; differences in the fruit colour of the two Fragaria species Fragaria vesca and Fragaria ananassa can be explained by the higher expression of DFR1 in Fragaria ananassa as compared to Fragaria vesca, a higher enzyme efficiency of DFR1 combined with the loss of F3'H activity late in fruit development of Fragaria ananassa; differences in the fruit colour of the two Fragaria species Fragaria vesca and Fragaria ananassa can be explained by the higher expression of DFR1 in Fragaria ananassa as compared to Fragaria vesca, a higher enzyme efficiency of DFR1 combined with the loss of F3'H activity late in fruit development of Fragaria ananassa; differences in the fruit colour of the two Fragaria species Fragaria vesca and Fragaria ananassa can be explained by the higher expression of DFR1 in Fragaria ananassa as compared to Fragaria vesca, a higher enzyme efficiency of DFR1 combined with the loss of F3'H activity late in fruit development of Fragaria ananassa
additional information
differences in the fruit colour of the two Fragaria species Fragaria vesca and Fragaria ananassa can be explained by the higher expression of DFR1 in Fragaria ananassa as compared to Fragaria vesca, a higher enzyme efficiency of DFR1 combined with the loss of F3'H activity late in fruit development of Fragaria ananassa; differences in the fruit colour of the two Fragaria species Fragaria vesca and Fragaria ananassa can be explained by the higher expression of DFR1 in Fragaria ananassa as compared to Fragaria vesca, a higher enzyme efficiency of DFR1 combined with the loss of F3'H activity late in fruit development of Fragaria ananassa; differences in the fruit colour of the two Fragaria species Fragaria vesca and Fragaria ananassa can be explained by the higher expression of DFR1 in Fragaria ananassa as compared to Fragaria vesca, a higher enzyme efficiency of DFR1 combined with the loss of F3'H activity late in fruit development of Fragaria ananassa
additional information
differences in the fruit colour of the two Fragaria species Fragaria vesca and Fragaria ananassa can be explained by the higher expression of DFR1 in Fragaria ananassa as compared to Fragaria vesca, a higher enzyme efficiency of DFR1 combined with the loss of F3'H activity late in fruit development of Fragaria ananassa; differences in the fruit colour of the two Fragaria species Fragaria vesca and Fragaria ananassa can be explained by the higher expression of DFR1 in Fragaria ananassa as compared to Fragaria vesca, a higher enzyme efficiency of DFR1 combined with the loss of F3'H activity late in fruit development of Fragaria ananassa; differences in the fruit colour of the two Fragaria species Fragaria vesca and Fragaria ananassa can be explained by the higher expression of DFR1 in Fragaria ananassa as compared to Fragaria vesca, a higher enzyme efficiency of DFR1 combined with the loss of F3'H activity late in fruit development of Fragaria ananassa
additional information
differences in the fruit colour of the two Fragaria species Fragaria vesca and Fragaria ananassa can be explained by the higher expression of DFR1 in Fragaria ananassa as compared to Fragaria vesca, a higher enzyme efficiency of DFR1 combined with the loss of F3'H activity late in fruit development of Fragaria ananassa; differences in the fruit colour of the two Fragaria species Fragaria vesca and Fragaria ananassa can be explained by the higher expression of DFR1 in Fragaria ananassa as compared to Fragaria vesca, a higher enzyme efficiency of DFR1 combined with the loss of F3'H activity late in fruit development of Fragaria ananassa; differences in the fruit colour of the two Fragaria species Fragaria vesca and Fragaria ananassa can be explained by the higher expression of DFR1 in Fragaria ananassa as compared to Fragaria vesca, a higher enzyme efficiency of DFR1 combined with the loss of F3'H activity late in fruit development of Fragaria ananassa
additional information
differences in the fruit colour of the two Fragaria species Fragaria vesca and Fragaria ananassa can be explained by the higher expression of DFR1 in Fragaria ananassa as compared to Fragaria vesca, a higher enzyme efficiency of DFR1 combined with the loss of F3'H activity late in fruit development of Fragaria ananassa; differences in the fruit colour of the two Fragaria species Fragaria vesca and Fragaria ananassa can be explained by the higher expression of DFR1 in Fragaria ananassa as compared to Fragaria vesca, a higher enzyme efficiency of DFR1 combined with the loss of F3'H activity late in fruit development of Fragaria ananassa; differences in the fruit colour of the two Fragaria species Fragaria vesca and Fragaria ananassa can be explained by the higher expression of DFR1 in Fragaria ananassa as compared to Fragaria vesca, a higher enzyme efficiency of DFR1 combined with the loss of F3'H activity late in fruit development of Fragaria ananassa
additional information
-
the gene encoding dihydroflavonol 4-reductase is a candidate for the anthocyaninless locus of rapid cycling Brassica rapa (fast plants type)
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(+)-dihydrokaempferol + NADPH + H+
cis-3,4-leucopelargonidin + NADP+
-
-
-
?
(4S)-5,5,5-trifluoro-4-hydroxy-4-phenylpentan-2-one + NADPH + H+
(2S)-1,1,1-trifluoro-2-phenylpentane-2,4-diol + NADP+
2,3-dihydromyricetin + NADPH
cis-3,4-leucodelphinidin + NADP+
low activity
-
-
?
2,3-dihydroquercetin + NADPH
cis-3,4-leucocyanidin + NADP+
i.e. (+)-taxifolin, stereospecific for (+)-isomer
-
-
?
7-hydroxyflavanone + NADPH + H+
2,4-cis-7-hydroxyflavan-4-ol + 2,4-trans-7-hydroxyflavan-4-ol + NADP+
-
-
-
?
butanal + NADPH
butan-1-ol + NADPH + H+
176% of the activity with benzaldehyde
-
-
?
heptan-2-one + NADPH + H+
(2S)-heptan-2-ol + NADP+
-
99% conversion, 99% enantiomeric excess
-
r
hexan-2-one + NADPH + H+
(2S)-hexan-2-ol + NADP+
-
99% conversion, 99% enantiomeric excess
-
r
hexanal + NADPH
hexan-1-ol + NADPH + H+
74% of the activity with benzaldehyde
-
-
?
(+)-2,3-dihydrokaempferol + NADPH
cis-3,4-leucopelargonidin + NADP+
-
-
-
-
?
(+)-2,3-dihydrokaempferol + NADPH
cis-3,4-leucopelargonidin + NADP+
-
-
-
?
(+)-2,3-dihydrokaempferol + NADPH
cis-3,4-leucopelargonidin + NADP+
low activity
-
-
?
(+)-dihydrokaempferol + NADPH
cis-3,4-leucopelargonidin + NADP+
-
30% as active as dihydroquercetin
-
-
(+)-dihydrokaempferol + NADPH
cis-3,4-leucopelargonidin + NADP+
-
-
-
?
(+)-dihydromyricetin + NADPH
cis-3,4-leucodelphinidin + NADP+
-
i.e. 5'-hydroxy-dihydroquercetin
i.e. 5,7,4'-trihydroxyflavan-3,4-cis-diol
?
(+)-dihydromyricetin + NADPH
cis-3,4-leucodelphinidin + NADP+
-
i.e. 5'-hydroxy-dihydroquercetin
i.e. 5,7,4'-trihydroxyflavan-3,4-cis-diol
-
(+)-dihydromyricetin + NADPH
cis-3,4-leucodelphinidin + NADP+
-
i.e. 5'-hydroxy-dihydroquercetin
i.e. 5,7,4'-trihydroxyflavan-3,4-cis-diol, configuration 2R,3S-trans-3S,4S-cis-leucodelphinidin
-
(+)-dihydromyricetin + NADPH
cis-3,4-leucodelphinidin + NADP+
-
i.e. 5'-hydroxy-dihydroquercetin
i.e. 5,7,4'-trihydroxyflavan-3,4-cis-diol
?
(+)-dihydroquercetin + NADPH
cis-3,4-leucocyanidin + NADP+
-
best substrate
-
-
(+)-dihydroquercetin + NADPH
cis-3,4-leucocyanidin + NADP+
-
-
i.e. 5,7,3',4'-tetrahydroxyflavan-3,4-cis-diol, 2,3-trans-configuration retained
-
(+)-dihydroquercetin + NADPH
cis-3,4-leucocyanidin + NADP+
-
-
-
-
(+)-dihydroquercetin + NADPH
cis-3,4-leucocyanidin + NADP+
-
-
-
?
(+)-dihydroquercetin + NADPH
cis-3,4-leucocyanidin + NADP+
-
-
i.e. 5,7,3',4'-tetrahydroxyflavan-3,4-cis-diol, 2,3-trans-configuration retained
-
(+)-dihydroquercetin + NADPH + H+
cis-3,4-leucocyanidin + NADP+
-
-
-
?
(+)-dihydroquercetin + NADPH + H+
cis-3,4-leucocyanidin + NADP+
-
-
-
?
(+)-dihydroquercetin + NADPH + H+
cis-3,4-leucocyanidin + NADP+
-
-
-
?
(2E)-hex-2-enal + NADPH
(2E)-hex-2-en-1-ol + NADPH + H+
97% of the activity with benzaldehyde
-
-
?
(2E)-hex-2-enal + NADPH
(2E)-hex-2-en-1-ol + NADPH + H+
97% of the activity with benzaldehyde
-
-
?
(2R,3R)-(+)-dihydrokaempferol + NADPH
(2R,3S,4S)-cis-3,4-leucopelargonidin + NADP+
-
-
-
?
(2R,3R)-(+)-dihydrokaempferol + NADPH
(2R,3S,4S)-cis-3,4-leucopelargonidin + NADP+
-
-
-
?
(2R,3R)-(+)-dihydrokaempferol + NADPH
(2R,3S,4S)-cis-3,4-leucopelargonidin + NADP+
-
-
-
?
(2R,3R)-(+)-dihydrokaempferol + NADPH
(2R,3S,4S)-cis-3,4-leucopelargonidin + NADP+
-
-
-
-
?
(2R,3R)-dihydromyricetin + NADPH
(2R,3S,4R)-cis-3,4-leucodelphinidin + NADP+
-
-
-
?
(2R,3R)-dihydromyricetin + NADPH
(2R,3S,4R)-cis-3,4-leucodelphinidin + NADP+
-
-
-
?
(2R,3R)-dihydromyricetin + NADPH
(2R,3S,4R)-cis-3,4-leucodelphinidin + NADP+
-
-
-
?
(2R,3R)-dihydromyricetin + NADPH
(2R,3S,4R)-cis-3,4-leucodelphinidin + NADP+
-
-
-
-
?
(2R,3R)-dihydromyricetin + NADPH
(2R,3S,4R)-cis-3,4-leucodelphinidin + NADP+
-
-
-
?
(2R,3R)-dihydromyricetin + NADPH
(2R,3S,4R)-cis-3,4-leucodelphinidin + NADP+
-
-
-
?
(2R,3R)-dihydromyricetin + NADPH
(2R,3S,4R)-cis-3,4-leucodelphinidin + NADP+
-
-
-
?
(2R,3R)-dihydroquercetin + NADPH
(2R,3S,4R)-leucocyanidin + NADP+
-
-
-
?
(2R,3R)-dihydroquercetin + NADPH
(2R,3S,4R)-leucocyanidin + NADP+
-
-
-
?
(2R,3R)-dihydroquercetin + NADPH
(2R,3S,4R)-leucocyanidin + NADP+
-
-
-
?
(2R,3R)-dihydroquercetin + NADPH
(2R,3S,4R)-leucocyanidin + NADP+
-
-
-
?
(2R,3R)-dihydroquercetin + NADPH
(2R,3S,4R)-leucocyanidin + NADP+
-
-
-
?
(2R,3R)-dihydroquercetin + NADPH
(2R,3S,4R)-leucocyanidin + NADP+
-
-
-
?
(4S)-5,5,5-trifluoro-4-hydroxy-4-phenylpentan-2-one + NADPH + H+
(2S)-1,1,1-trifluoro-2-phenylpentane-2,4-diol + NADP+
enzyme specifically reduces the S-enantiomer
-
-
?
(4S)-5,5,5-trifluoro-4-hydroxy-4-phenylpentan-2-one + NADPH + H+
(2S)-1,1,1-trifluoro-2-phenylpentane-2,4-diol + NADP+
enzyme specifically reduces the S-enantiomer
-
-
?
2-methylpentanal + NADPH
2-methyl-pentan-1-ol + NADPH + H+
249% of the activity with benzaldehyde
-
-
?
2-methylpentanal + NADPH
2-methyl-pentan-1-ol + NADPH + H+
249% of the activity with benzaldehyde
-
-
?
dihydrokaempferol + NADPH + H+
leucopelargonidin + NADP+
-
highest pelargonidin concentration derived from the E-color culture harboring the Anthurium andraeanum DFR
-
?
dihydrokaempferol + NADPH + H+
leucopelargonidin + NADP+
-
-
-
?
dihydrokaempferol + NADPH + H+
leucopelargonidin + NADP+
-
-
-
?
dihydrokaempferol + NADPH + H+
leucopelargonidin + NADP+
-
-
-
?
dihydrokaempferol + NADPH + H+
leucopelargonidin + NADP+
-
-
-
?
dihydrokaempferol + NADPH + H+
leucopelargonidin + NADP+
best substrate
-
-
?
dihydrokaempferol + NADPH + H+
leucopelargonidin + NADP+
-
-
-
?
dihydrokaempferol + NADPH + H+
leucopelargonidin + NADP+
best substrate
-
-
?
dihydrokaempferol + NADPH + H+
leucopelargonidin + NADP+
-
-
-
?
dihydrokaempferol + NADPH + H+
leucopelargonidin + NADP+
-
-
-
?
dihydromyricetin + NADPH + H+
leucodelphinidin + NADP+
-
-
-
?
dihydromyricetin + NADPH + H+
leucodelphinidin + NADP+
-
-
-
?
dihydromyricetin + NADPH + H+
leucodelphinidin + NADP+
-
-
-
?
dihydromyricetin + NADPH + H+
leucodelphinidin + NADP+
14% of the activity with dihydrokaempferol
-
-
?
dihydromyricetin + NADPH + H+
leucodelphinidin + NADP+
-
-
-
?
dihydromyricetin + NADPH + H+
leucodelphinidin + NADP+
23% of the activity with dihydrokaempferol
-
-
?
dihydromyricetin + NADPH + H+
leucodelphinidin + NADP+
-
-
-
?
dihydromyricetin + NADPH + H+
leucodelphinidin + NADP+
-
-
-
?
dihydroquercetin + NADPH + H+
cis-3,4-leucocyanidin + NADP+
-
-
-
?
dihydroquercetin + NADPH + H+
cis-3,4-leucocyanidin + NADP+
-
-
-
?
dihydroquercetin + NADPH + H+
cis-3,4-leucocyanidin + NADP+
-
-
-
?
dihydroquercetin + NADPH + H+
cis-3,4-leucocyanidin + NADP+
14% of the activity with dihydrokaempferol
-
-
?
dihydroquercetin + NADPH + H+
cis-3,4-leucocyanidin + NADP+
-
-
-
?
dihydroquercetin + NADPH + H+
cis-3,4-leucocyanidin + NADP+
11% of the activity with dihydrokaempferol
-
-
?
dihydroquercetin + NADPH + H+
cis-3,4-leucocyanidin + NADP+
-
-
-
?
dihydroquercetin + NADPH + H+
cis-3,4-leucocyanidin + NADP+
-
-
-
?
dihydroquercetin + NADPH + H+
leucocyanidin + NADP+
-
maximum detected levels of extracellular leucocyanidin produced from Escherichia coli strains BL21StarTM (DE3), BLDELTApgi, BLDELTApgiDELTAppc, BLDELTApgiDELTApldADELTAppc and BLDELTApgiDELTApldBDELTAppc expressing DFR
-
-
r
dihydroquercetin + NADPH + H+
leucocyanidin + NADP+
-
-
-
?
additional information
?
-
can not reduce hesperetin or 5,7-dimethoxyflavanone
-
-
-
additional information
?
-
enzyme is involved in production of leucoanthocyanidins, i.e flavan-3,4-diols, and in reduction of flavanones to flavan-4-ols which are important intermediates in the 3-deoxyflavonoid pathway
-
-
-
additional information
?
-
-
no substrates: (+)-dihydromorin, i.e. 3,5,7,2',4'-pentahydroxyflavanone, and pinobanksin, i.e. 3,5,7-trihydroxyflavanone
-
-
-
additional information
?
-
enzyme is involved in production of leucoanthocyanidins, i.e flavan-3,4-diols, and in reduction of flavanones to flavan-4-ols which are important intermediates in the 3-deoxyflavonoid pathway
-
-
-
additional information
?
-
DFR exhibits selectivity for the B-ring hydroxylation pattern of flavonoid substrates
-
-
-
additional information
?
-
DFR exhibits selectivity for the B-ring hydroxylation pattern of flavonoid substrates
-
-
-
additional information
?
-
DFR exhibits selectivity for the B-ring hydroxylation pattern of flavonoid substrates
-
-
-
additional information
?
-
DFR exhibits selectivity for the B-ring hydroxylation pattern of flavonoid substrates
-
-
-
additional information
?
-
DFR exhibits selectivity for the B-ring hydroxylation pattern of flavonoid substrates
-
-
-
additional information
?
-
DFR exhibits selectivity for the B-ring hydroxylation pattern of flavonoid substrates
-
-
-
additional information
?
-
DFR exhibits selectivity for the B-ring hydroxylation pattern of flavonoid substrates
-
-
-
additional information
?
-
DFR exhibits selectivity for the B-ring hydroxylation pattern of flavonoid substrates
-
-
-
additional information
?
-
DFR exhibits selectivity for the B-ring hydroxylation pattern of flavonoid substrates
-
-
-
additional information
?
-
DFR exhibits selectivity for the B-ring hydroxylation pattern of flavonoid substrates
-
-
-
additional information
?
-
enzyme is involved in production of leucoanthocyanidins, i.e flavan-3,4-diols, and in reduction of flavanones to flavan-4-ols which are important intermediates in the 3-deoxyflavonoid pathway
-
-
-
additional information
?
-
linear and branched aliphatic aldehydes are good substrates
-
-
-
additional information
?
-
linear and branched aliphatic aldehydes are good substrates
-
-
-
additional information
?
-
does not catalyze dihydrokaempferol and naringenin
-
-
-
additional information
?
-
-
reaction in anthocyanidin biosynthesis in plants
-
-
-
additional information
?
-
-
enzyme is involved in production of leucoanthocyanidins, i.e flavan-3,4-diols, and in reduction of flavanones to flavan-4-ols which are important intermediates in the 3-deoxyflavonoid pathway
-
-
-
additional information
?
-
-
key enzyme in flux control in biosynthetic branched pathways leading to anthocyanins and condensed tannins
-
-
-
additional information
?
-
key enzyme in flux control in biosynthetic branched pathways leading to anthocyanins and condensed tannins
-
-
-
additional information
?
-
key enzyme in flux control in biosynthetic branched pathways leading to anthocyanins and condensed tannins
-
-
-
additional information
?
-
-
stereospecific enzyme, no activity with substances lacking the the hydroxyl group at the 3-position or with a double bond present between C2 and C3, e.g. quercetin, apigenin, eriodictyol, and kaempferol
-
-
-
additional information
?
-
stereospecific enzyme, no activity with substances lacking the the hydroxyl group at the 3-position or with a double bond present between C2 and C3, e.g. quercetin, apigenin, eriodictyol, and kaempferol
-
-
-
additional information
?
-
stereospecific enzyme, no activity with substances lacking the the hydroxyl group at the 3-position or with a double bond present between C2 and C3, e.g. quercetin, apigenin, eriodictyol, and kaempferol
-
-
-
additional information
?
-
-
biosynthesis of proanthocyanidin polymers (condensed tannins)
-
-
-
additional information
?
-
enzyme is involved in production of leucoanthocyanidins, i.e flavan-3,4-diols, and in reduction of flavanones to flavan-4-ols which are important intermediates in the 3-deoxyflavonoid pathway
-
-
-
additional information
?
-
no activity with (+)-dihydrokaempferol
-
-
-
additional information
?
-
enzyme is involved in production of leucoanthocyanidins, i.e flavan-3,4-diols, and in reduction of flavanones to flavan-4-ols which are important intermediates in the 3-deoxyflavonoid pathway
-
-
-
additional information
?
-
no activity with (+)-dihydrokaempferol
-
-
-
additional information
?
-
the enzyme catalyzes the reduction of dihydroflavonols to leucoanthocyanins. But SmDFR also possesses flavanone 4-reductase (FNR) activity and can catalyze the conversion of eridictyol to luteoforol, EC 1.1.1.234
-
-
-
additional information
?
-
-
the enzyme catalyzes the reduction of dihydroflavonols to leucoanthocyanins. But SmDFR also possesses flavanone 4-reductase (FNR) activity and can catalyze the conversion of eridictyol to luteoforol, EC 1.1.1.234
-
-
-
additional information
?
-
no activity in reduction of dihydromyricetin
-
-
-
additional information
?
-
-
no activity in reduction of dihydromyricetin
-
-
-
additional information
?
-
no substrate: dihydromyricetin. enzyme additionally shows flavanone-4-reductase activity, EC 1.1.1.234
-
-
-
additional information
?
-
-
no substrate: dihydromyricetin. enzyme additionally shows flavanone-4-reductase activity, EC 1.1.1.234
-
-
-
additional information
?
-
enzyme is involved in production of leucoanthocyanidins, i.e flavan-3,4-diols, and in reduction of flavanones to flavan-4-ols which are important intermediates in the 3-deoxyflavonoid pathway
-
-
-
additional information
?
-
no activity with (+)-dihydrokaempferol
-
-
-
additional information
?
-
-
the key enzyme in flavonoid biosynthesis catalyzes a late step in the biosynthesis of anthocyanins and condensed tannins, two flavonoid classes of importance to plant survival and human nutrition, overview
-
-
-
additional information
?
-
-
the specific residue at position 133, Asn or Asp, is involved in controling of the substrate recognition and recognition of the B-ring hydroxylation pattern of dihydroflavonols, structure-function relationship, overview
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
dihydrokaempferol + NADPH + H+
leucopelargonidin + NADP+
M4D235, M4DRB9, M4DU26, M4DU27, M4DU28, M4E380, M4E7I9, M4E7J1, M4E7J2, M4ECU0, M4ES88, M4FB76
-
-
-
?
dihydrokaempferol + NADPH + H+
leucopelargonidin + NADP+
A0A0C6ENR6
-
-
-
?
dihydrokaempferol + NADPH + H+
leucopelargonidin + NADP+
A0A0C6EUC4
-
-
-
?
dihydrokaempferol + NADPH + H+
leucopelargonidin + NADP+
A0A0C6E754
-
-
-
?
dihydrokaempferol + NADPH + H+
leucopelargonidin + NADP+
A0A0A0PTI9, A0A0A0PTJ4, A0A0A0PV90, A0A0A0PVL2, A0A0A0PVL5, A0A0A0PXZ7
-
-
-
?
dihydrokaempferol + NADPH + H+
leucopelargonidin + NADP+
A0A0A0PTJ7, A0A0A0PVL7, O22617, Q5UL14
-
-
-
?
dihydromyricetin + NADPH + H+
leucodelphinidin + NADP+
M4D235, M4DRB9, M4DU26, M4DU27, M4DU28, M4E380, M4E7I9, M4E7J1, M4E7J2, M4ECU0, M4ES88, M4FB76
-
-
-
?
dihydromyricetin + NADPH + H+
leucodelphinidin + NADP+
A0A0C6ENR6
-
-
-
?
dihydromyricetin + NADPH + H+
leucodelphinidin + NADP+
A0A0C6EUC4
-
-
-
?
dihydromyricetin + NADPH + H+
leucodelphinidin + NADP+
A0A0C6E754
-
-
-
?
dihydromyricetin + NADPH + H+
leucodelphinidin + NADP+
A0A0A0PTI9, A0A0A0PTJ4, A0A0A0PV90, A0A0A0PVL2, A0A0A0PVL5, A0A0A0PXZ7
-
-
-
?
dihydromyricetin + NADPH + H+
leucodelphinidin + NADP+
A0A0A0PTJ7, A0A0A0PVL7, O22617, Q5UL14
-
-
-
?
dihydroquercetin + NADPH + H+
cis-3,4-leucocyanidin + NADP+
M4D235, M4DRB9, M4DU26, M4DU27, M4DU28, M4E380, M4E7I9, M4E7J1, M4E7J2, M4ECU0, M4ES88, M4FB76
-
-
-
?
dihydroquercetin + NADPH + H+
cis-3,4-leucocyanidin + NADP+
A0A0C6ENR6
-
-
-
?
dihydroquercetin + NADPH + H+
cis-3,4-leucocyanidin + NADP+
A0A0C6EUC4
-
-
-
?
dihydroquercetin + NADPH + H+
cis-3,4-leucocyanidin + NADP+
A0A0C6E754
-
-
-
?
dihydroquercetin + NADPH + H+
cis-3,4-leucocyanidin + NADP+
A0A0A0PTI9, A0A0A0PTJ4, A0A0A0PV90, A0A0A0PVL2, A0A0A0PVL5, A0A0A0PXZ7
-
-
-
?
dihydroquercetin + NADPH + H+
cis-3,4-leucocyanidin + NADP+
A0A0A0PTJ7, A0A0A0PVL7, O22617, Q5UL14
-
-
-
?
additional information
?
-
P51103
enzyme is involved in production of leucoanthocyanidins, i.e flavan-3,4-diols, and in reduction of flavanones to flavan-4-ols which are important intermediates in the 3-deoxyflavonoid pathway
-
-
-
additional information
?
-
P51104
enzyme is involved in production of leucoanthocyanidins, i.e flavan-3,4-diols, and in reduction of flavanones to flavan-4-ols which are important intermediates in the 3-deoxyflavonoid pathway
-
-
-
additional information
?
-
P51105
enzyme is involved in production of leucoanthocyanidins, i.e flavan-3,4-diols, and in reduction of flavanones to flavan-4-ols which are important intermediates in the 3-deoxyflavonoid pathway
-
-
-
additional information
?
-
-
reaction in anthocyanidin biosynthesis in plants
-
-
-
additional information
?
-
-
enzyme is involved in production of leucoanthocyanidins, i.e flavan-3,4-diols, and in reduction of flavanones to flavan-4-ols which are important intermediates in the 3-deoxyflavonoid pathway
-
-
-
additional information
?
-
-
key enzyme in flux control in biosynthetic branched pathways leading to anthocyanins and condensed tannins
-
-
-
additional information
?
-
Q6TQT0
key enzyme in flux control in biosynthetic branched pathways leading to anthocyanins and condensed tannins
-
-
-
additional information
?
-
Q6TQT1
key enzyme in flux control in biosynthetic branched pathways leading to anthocyanins and condensed tannins
-
-
-
additional information
?
-
-
biosynthesis of proanthocyanidin polymers (condensed tannins)
-
-
-
additional information
?
-
Q41158
enzyme is involved in production of leucoanthocyanidins, i.e flavan-3,4-diols, and in reduction of flavanones to flavan-4-ols which are important intermediates in the 3-deoxyflavonoid pathway
-
-
-
additional information
?
-
Q41158
enzyme is involved in production of leucoanthocyanidins, i.e flavan-3,4-diols, and in reduction of flavanones to flavan-4-ols which are important intermediates in the 3-deoxyflavonoid pathway
-
-
-
additional information
?
-
A5Z0G1
the enzyme catalyzes the reduction of dihydroflavonols to leucoanthocyanins. But SmDFR also possesses flavanone 4-reductase (FNR) activity and can catalyze the conversion of eridictyol to luteoforol, EC 1.1.1.234
-
-
-
additional information
?
-
-
the enzyme catalyzes the reduction of dihydroflavonols to leucoanthocyanins. But SmDFR also possesses flavanone 4-reductase (FNR) activity and can catalyze the conversion of eridictyol to luteoforol, EC 1.1.1.234
-
-
-
additional information
?
-
P51107
enzyme is involved in production of leucoanthocyanidins, i.e flavan-3,4-diols, and in reduction of flavanones to flavan-4-ols which are important intermediates in the 3-deoxyflavonoid pathway
-
-
-
additional information
?
-
-
the key enzyme in flavonoid biosynthesis catalyzes a late step in the biosynthesis of anthocyanins and condensed tannins, two flavonoid classes of importance to plant survival and human nutrition, overview
-
-
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADPH
-
conversion of dihydroquercetin by DFR is likely dependent on the [NADPH]/[NADP+] ratio and less so on the absolute value of NADPH within the cell
NADPH
seuence shows a putative NADPH-binding site; seuence shows a putative NADPH-binding site
NADPH
-
additional information
-
FMN, FAD or 6,7-dimethyl-5,6,7,8-tetrahydropterine cannot replace NADPH
-
additional information
-
ascorbate cannot replace NADPH, the reaction occurs equally well anaerobically
-
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
myricetin
-
flavonol that can be an inhibitor of the activity of DFR towards dihydroflavonols
quercetin
-
flavonol that can be an inhibitor of the activity of DFR towards dihydroflavonols
additional information
is unaffected by gibberellic acid treatment
-
additional information
is unaffected by gibberellic acid treatment
-
additional information
-
no inhibition with PCMB, EDTA, Mg2+, Co2+, Fe2+, Ca2+, Mn2+, Zn2+
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
enzyme expression is increased with time during a 24 h exposure to UV-A irradiation, but not by irradiation with red, blue, UV-B, and a combination of blue with red light
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.15
(4S)-5,5,5-trifluoro-4-hydroxy-4-phenylpentan-2-one
pH 7.0, 25°C
0.0004
dihydrokaempferol
pH 6.3, temperature not specified in the publication
0.0023
dihydromyricetin
pH 6.3, temperature not specified in the publication
0.0004
dihydroquercetin
pH 6.3, temperature not specified in the publication
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
44.5
(4S)-5,5,5-trifluoro-4-hydroxy-4-phenylpentan-2-one
pH 7.0, 25°C
11.4
dihydrokaempferol
pH 6.3, temperature not specified in the publication
11.2
dihydromyricetin
pH 6.3, temperature not specified in the publication
3.1
dihydroquercetin
pH 6.3, temperature not specified in the publication
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
28500
dihydrokaempferol
pH 6.3, temperature not specified in the publication
4870
dihydromyricetin
pH 6.3, temperature not specified in the publication
7750
dihydroquercetin
pH 6.3, temperature not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.000012
-
pigmented cultivar Tarocco in 0.05 M Tris-HCl pH 7.5, l M dihydroquercetin, 2 mM NADPH, 1 U glucose-6-phosphate dehydrogenase, 6 mM glucose-6-phosphate and enzyme extract at 25°C
0.0004
with dihydrokaempferol as substrate; with naringenin as substrate
0.0006
0.0007
0.001
0.0012
0.0013
0.0014
0.042
-
sample callus control in 25 mM Tris-HCl (pH 7.0), 4 mM NADPH and 0.1 mM dihydroquercetin at 25°C
0.103
-
sample callus L-1 in 25 mM Tris-HCl (pH 7.0), 4 mM NADPH and 0.1 mM dihydroquercetin at 25°C
0.155
-
sample callus L-2 in 25 mM Tris-HCl (pH 7.0), 4 mM NADPH and 0.1 mM dihydroquercetin at 25°C
0.202
-
sample plant control in 25 mM Tris-HCl (pH 7.0), 4 mM NADPH and 0.1 mM dihydroquercetin at 25°C
0.268
-
sample plant L-2 in 25 mM Tris-HCl (pH 7.0), 4 mM NADPH and 0.1 mM dihydroquercetin at 25°C
0.349
-
sample plant L-1 in 25 mM Tris-HCl (pH 7.0), 4 mM NADPH and 0.1 mM dihydroquercetin at 25°C
additional information
0.0014
-
with dihydromyricetin as substrate; with dihydroquercitin as substrate
additional information
-
no specific activity detectable for non-pigmented cultivars Navel and Ovale
additional information
-
crude extract 12.1 microgram per h and mg protein
additional information
-
measurement of reductase activity during leaf development
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.8 - 6.3
dependent on the substrate
7.5
7
-
broad optimum with Tris buffer, sharp optimum with citric acid-sodium phosphate buffer
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 7
-
maximum DFR activities achieved towards dihydroflavonols and flavanones
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
30
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25 - 30
-
maximum DFR activities achieved towards dihydroflavonols and flavanones
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.2
sequence calculation
5.21
sequence calculation
5.26
sequence calculation
5.36
sequence calculation
5.41
sequence calculation
5.45
sequence calculation
5.49
sequence calculation
5.66
sequence calculation
5.9
sequence calculation
6.09
sequence calculation
6.2
8.65
sequence calculation
6.2
sequence calculation
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
flavanone 3-hydroxylase, dihydroflavonol 4-reductase and flavonoid 3',5'-hydrolase are expressed in progeny with colored tuber skin, while dihydroflavonol 4-reductase and flavonoid 3',5'-hydrolase are not expressed, and flavanone 3-hydroxylase is only weakly expressed, in progeny with white tuber skin. Expression is regulated by transcription factor Stan2
isoform PtrDFR2 transcripts are more than twice as abundant as isoform DFR1 in young petioles and 15 times more abundant in old petioles
mRNA accumulation of DFR is higher in the shoots than in the leaves
additional information
quantitative enzyme expression analysis in flowers from different cultivars, overview
quantitative enzyme expression analysis in flowers from different cultivars, overview
quantitative enzyme expression analysis in flowers from different cultivars, overview
expression in early and late flowering; expression in early flowering; expression in early flowering; expression in late flowering; expression in late flowering; expression in late flowering
expression in early and late flowering; expression in early and late flowering; expression in early flowering
; expression in flowers is about 8fold higher compared with leaves and roots
high expression level
-
enzyme expression profile at different developmental stages of the bud. The highest expression is observed at 50 days of the stage of flower bud differentiation period
-
expression is maximal in younger rather than older leaves; expression is maximum in younger rather than older leaves
levels of anthocyanins and the transcript abundance of the anthocyanin biosynthetic gene, dihydroflavonol 4-reductase (McDFR) during the leaf development in two crabapple cultivars, overview. The concentrations of anthocyanins and flavonols correlate with leaf color and the expression of McDFR and McFLS influences their accumulation
; expression in flowers is about 8fold higher compared with leaves and roots
-
highest accumulation of transcripts; highest accumulation of transcripts
; expression in flowers is about 8fold higher compared with leaves and roots
-
DFR activity is lower in YN01-429 as compared to N89-53 seed coats. Two copies of the DFR gene, which are both functional in YN01-429, homeoallelic repression or silencing, together they show very low expression levels (17fold fewer transcripts) relative to DFR acitvity in N89-53 seed coats
weak expression
additional information
organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis
additional information
organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis
additional information
organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis
additional information
organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis
additional information
organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis
additional information
organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis
additional information
organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis
additional information
organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis
additional information
organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis
additional information
organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis
additional information
organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis
additional information
organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis; organ-specific DFR expression analysis
additional information
-
enzyme expression profile at different developmental stages of the flower bud and at different periods of flowering in different tissues, highest at period I in the tubular flower, lowest at peroid II in the receptable
additional information
enzyme expression in two different varieties during six stages of flower development in tepal, stamen, and carpel tissues, enzyme expression increases in both varieties during flower developmental stages contantly, overview
additional information
quantitative expression of DFR1 and DFR2 normalized to glyceraldehyde 3-phosphate dehydrogenase in receptacle and achenes of Fragaria fruits during the different stages of fruit development, overview; quantitative expression of DFR1 and DFR2 normalized to glyceraldehyde 3-phosphate dehydrogenase in receptacle and achenes of Fragaria fruits during the different stages of fruit development, overview; quantitative expression of DFR1 and DFR2 normalized to glyceraldehyde 3-phosphate dehydrogenase in receptacle and achenes of Fragaria fruits during the different stages of fruit development, overview; quantitative expression of DFR1 and DFR2 normalized to glyceraldehyde 3-phosphate dehydrogenase in receptacle and achenes of Fragaria fruits during the different stages of fruit development, overview; quantitative expression of DFR1 and DFR2 normalized to glyceraldehyde 3-phosphate dehydrogenase in receptacle and achenes of Fragaria fruits during the different stages of fruit development, overview; quantitative expression of DFR1 and DFR2 normalized to glyceraldehyde 3-phosphate dehydrogenase in receptacle and achenes of Fragaria fruits during the different stages of fruit development, overview
additional information
quantitative expression of DFR1 and DFR2 normalized to glyceraldehyde 3-phosphate dehydrogenase in receptacle and achenes of Fragaria fruits during the different stages of fruit development, overview; quantitative expression of DFR1 and DFR2 normalized to glyceraldehyde 3-phosphate dehydrogenase in receptacle and achenes of Fragaria fruits during the different stages of fruit development, overview; quantitative expression of DFR1 and DFR2 normalized to glyceraldehyde 3-phosphate dehydrogenase in receptacle and achenes of Fragaria fruits during the different stages of fruit development, overview; quantitative expression of DFR1 and DFR2 normalized to glyceraldehyde 3-phosphate dehydrogenase in receptacle and achenes of Fragaria fruits during the different stages of fruit development, overview; quantitative expression of DFR1 and DFR2 normalized to glyceraldehyde 3-phosphate dehydrogenase in receptacle and achenes of Fragaria fruits during the different stages of fruit development, overview; quantitative expression of DFR1 and DFR2 normalized to glyceraldehyde 3-phosphate dehydrogenase in receptacle and achenes of Fragaria fruits during the different stages of fruit development, overview
additional information
quantitative expression of DFR1 and DFR2 normalized to glyceraldehyde 3-phosphate dehydrogenase in receptacle and achenes of Fragaria fruits during the different stages of fruit development, overview; quantitative expression of DFR1 and DFR2 normalized to glyceraldehyde 3-phosphate dehydrogenase in receptacle and achenes of Fragaria fruits during the different stages of fruit development, overview; quantitative expression of DFR1 and DFR2 normalized to glyceraldehyde 3-phosphate dehydrogenase in receptacle and achenes of Fragaria fruits during the different stages of fruit development, overview; quantitative expression of DFR1 and DFR2 normalized to glyceraldehyde 3-phosphate dehydrogenase in receptacle and achenes of Fragaria fruits during the different stages of fruit development, overview; quantitative expression of DFR1 and DFR2 normalized to glyceraldehyde 3-phosphate dehydrogenase in receptacle and achenes of Fragaria fruits during the different stages of fruit development, overview; quantitative expression of DFR1 and DFR2 normalized to glyceraldehyde 3-phosphate dehydrogenase in receptacle and achenes of Fragaria fruits during the different stages of fruit development, overview
additional information
quantitative expression of DFR1 and DFR2 normalized to glyceraldehyde 3-phosphate dehydrogenase in receptacle and achenes of Fragaria fruits during the different stages of fruit development, overview; quantitative expression of DFR1 and DFR2 normalized to glyceraldehyde 3-phosphate dehydrogenase in receptacle and achenes of Fragaria fruits during the different stages of fruit development, overview; quantitative expression of DFR1 and DFR2 normalized to glyceraldehyde 3-phosphate dehydrogenase in receptacle and achenes of Fragaria fruits during the different stages of fruit development, overview; quantitative expression of DFR1 and DFR2 normalized to glyceraldehyde 3-phosphate dehydrogenase in receptacle and achenes of Fragaria fruits during the different stages of fruit development, overview; quantitative expression of DFR1 and DFR2 normalized to glyceraldehyde 3-phosphate dehydrogenase in receptacle and achenes of Fragaria fruits during the different stages of fruit development, overview; quantitative expression of DFR1 and DFR2 normalized to glyceraldehyde 3-phosphate dehydrogenase in receptacle and achenes of Fragaria fruits during the different stages of fruit development, overview
additional information
quantitative expression of DFR1 and DFR2 normalized to glyceraldehyde 3-phosphate dehydrogenase in receptacle and achenes of Fragaria fruits during the different stages of fruit development, overview; quantitative expression of DFR1 and DFR2 normalized to glyceraldehyde 3-phosphate dehydrogenase in receptacle and achenes of Fragaria fruits during the different stages of fruit development, overview; quantitative expression of DFR1 and DFR2 normalized to glyceraldehyde 3-phosphate dehydrogenase in receptacle and achenes of Fragaria fruits during the different stages of fruit development, overview; quantitative expression of DFR1 and DFR2 normalized to glyceraldehyde 3-phosphate dehydrogenase in receptacle and achenes of Fragaria fruits during the different stages of fruit development, overview; quantitative expression of DFR1 and DFR2 normalized to glyceraldehyde 3-phosphate dehydrogenase in receptacle and achenes of Fragaria fruits during the different stages of fruit development, overview; quantitative expression of DFR1 and DFR2 normalized to glyceraldehyde 3-phosphate dehydrogenase in receptacle and achenes of Fragaria fruits during the different stages of fruit development, overview
additional information
quantitative expression of DFR1 and DFR2 normalized to glyceraldehyde 3-phosphate dehydrogenase in receptacle and achenes of Fragaria fruits during the different stages of fruit development, overview; quantitative expression of DFR1 and DFR2 normalized to glyceraldehyde 3-phosphate dehydrogenase in receptacle and achenes of Fragaria fruits during the different stages of fruit development, overview; quantitative expression of DFR1 and DFR2 normalized to glyceraldehyde 3-phosphate dehydrogenase in receptacle and achenes of Fragaria fruits during the different stages of fruit development, overview; quantitative expression of DFR1 and DFR2 normalized to glyceraldehyde 3-phosphate dehydrogenase in receptacle and achenes of Fragaria fruits during the different stages of fruit development, overview; quantitative expression of DFR1 and DFR2 normalized to glyceraldehyde 3-phosphate dehydrogenase in receptacle and achenes of Fragaria fruits during the different stages of fruit development, overview; quantitative expression of DFR1 and DFR2 normalized to glyceraldehyde 3-phosphate dehydrogenase in receptacle and achenes of Fragaria fruits during the different stages of fruit development, overview
additional information
quantitative expression of DFR1 and DFR2 normalized to glyceraldehyde 3-phosphate dehydrogenase in receptacle and achenes of Fragaria fruits during the different stages of fruit development, overview; quantitative expression of DFR1 and DFR2 normalized to glyceraldehyde 3-phosphate dehydrogenase in receptacle and achenes of Fragaria fruits during the different stages of fruit development, overview; quantitative expression of DFR1 and DFR2 normalized to glyceraldehyde 3-phosphate dehydrogenase in receptacle and achenes of Fragaria fruits during the different stages of fruit development, overview; quantitative expression of DFR1 and DFR2 normalized to glyceraldehyde 3-phosphate dehydrogenase in receptacle and achenes of Fragaria fruits during the different stages of fruit development, overview
additional information
quantitative expression of DFR1 and DFR2 normalized to glyceraldehyde 3-phosphate dehydrogenase in receptacle and achenes of Fragaria fruits during the different stages of fruit development, overview; quantitative expression of DFR1 and DFR2 normalized to glyceraldehyde 3-phosphate dehydrogenase in receptacle and achenes of Fragaria fruits during the different stages of fruit development, overview; quantitative expression of DFR1 and DFR2 normalized to glyceraldehyde 3-phosphate dehydrogenase in receptacle and achenes of Fragaria fruits during the different stages of fruit development, overview; quantitative expression of DFR1 and DFR2 normalized to glyceraldehyde 3-phosphate dehydrogenase in receptacle and achenes of Fragaria fruits during the different stages of fruit development, overview
additional information
quantitative expression of DFR1 and DFR2 normalized to glyceraldehyde 3-phosphate dehydrogenase in receptacle and achenes of Fragaria fruits during the different stages of fruit development, overview; quantitative expression of DFR1 and DFR2 normalized to glyceraldehyde 3-phosphate dehydrogenase in receptacle and achenes of Fragaria fruits during the different stages of fruit development, overview; quantitative expression of DFR1 and DFR2 normalized to glyceraldehyde 3-phosphate dehydrogenase in receptacle and achenes of Fragaria fruits during the different stages of fruit development, overview; quantitative expression of DFR1 and DFR2 normalized to glyceraldehyde 3-phosphate dehydrogenase in receptacle and achenes of Fragaria fruits during the different stages of fruit development, overview
additional information
quantitative expression of DFR1 and DFR2 normalized to glyceraldehyde 3-phosphate dehydrogenase in receptacle and achenes of Fragaria fruits during the different stages of fruit development, overview; quantitative expression of DFR1 and DFR2 normalized to glyceraldehyde 3-phosphate dehydrogenase in receptacle and achenes of Fragaria fruits during the different stages of fruit development, overview; quantitative expression of DFR1 and DFR2 normalized to glyceraldehyde 3-phosphate dehydrogenase in receptacle and achenes of Fragaria fruits during the different stages of fruit development, overview; quantitative expression of DFR1 and DFR2 normalized to glyceraldehyde 3-phosphate dehydrogenase in receptacle and achenes of Fragaria fruits during the different stages of fruit development, overview
additional information
-
tissue expression profiles of DFR isozymes, overview. During the annual growth cycle, the GbDFRs are significantly correlated with anthocyanin accumulation in leaves; tissue expression profiles of DFR isozymes, overview. During the annual growth cycle, the GbDFRs are significantly correlated with anthocyanin accumulation in leaves
additional information
tissue expression profiles of DFR isozymes, overview. During the annual growth cycle, the GbDFRs are significantly correlated with anthocyanin accumulation in leaves; tissue expression profiles of DFR isozymes, overview. During the annual growth cycle, the GbDFRs are significantly correlated with anthocyanin accumulation in leaves
additional information
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enzyme expression analysis in different tissues and anthocyanidins contents, overview
additional information
transcripts are found in all tissues examined, but most concentrated in root; transcripts are found in all tissues examined, but most concentrated in root
additional information
transcripts are found in all tissues examined, but most concentrated in root; transcripts are found in all tissues examined, but most concentrated in root
additional information
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transcripts are found in all tissues examined, but most concentrated in root; transcripts are found in all tissues examined, but most concentrated in root
additional information
expression level of SmDFR is higher in flowers compared with both leaves and roots
additional information
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expression level of SmDFR is higher in flowers compared with both leaves and roots
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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PDB
SCOP
CATH
ORGANISM
UNIPROT
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
38670
sequence analysis; x * 38670, calculated, x * 41000, SDS-PAGE of recombinant protein with fusion peptide
41000
x * 38670, calculated, x * 41000, SDS-PAGE of recombinant protein with fusion peptide; x * 41000, SDS-PAGE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
?
x * 34760, sequence calculation; x * 34860, sequence calculation; x * 35420, sequence calculation; x * 35420, sequence calculation; x * 35520, sequence calculation; x * 35860, sequence calculation; x * 35910, sequence calculation; x * 36150, sequence calculation; x * 36320, sequence calculation; x * 39650, sequence calculation; x * 40450, sequence calculation
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x * 38670, calculated, x * 41000, SDS-PAGE of recombinant protein with fusion peptide; x * 41000, SDS-PAGE
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x * 38670, calculated, x * 41000, SDS-PAGE of recombinant protein with fusion peptide
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additional information
sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview
additional information
sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview
additional information
sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview
additional information
sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview
additional information
sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview
additional information
sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview
additional information
sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview
additional information
sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview
additional information
sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview
additional information
sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview
additional information
sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview
additional information
sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview; sequence analysis and structure homology, overview
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DFR-NADP+-flavonol (myricetin and quercetin) complexes, at room temperature, by hanging-drop vapour diffusion method. Complex DFR-NADP+-myricetin belongs to space group P21 (unit-cell parameters a = 47.23, b = 177.96, c = 92.60 A, beta = 104.8°). Complex DFR-NADP+-quercetin belongs to space group P6122 (unit-cell parameters a = b = 174.94, c = 290.18 A)
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purified recombinant enzyme in complex with NADPH and dihydroquercetin, X-ray diffraction structure determination and analysis at 1.8 A resolution
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 57% loss of activity after 4 months, 2-mercaptoethanol protects
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
allele of DFR associated with red color, under the control of a doubled CaMV 35S promoter and tobacco etch virus translational enhancer introduced into the potato cultivar Prince Hairy (genotype dddd rrrr P-), which has white tubers and pale blue flowers
Escherichia coli strains transformed with plasmid pTrcHis2-DFR to only express DFR. Escherichia coli strains harboring plasmid pET-DFR-LAR expressing DFR and leucoanthocyanidin reductase
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expression in Escherichia coli
expression in Escherichia coli; into expression vector pQE-30 UA, and transformed into Escherichia coli M15 pREP-4 competent cells
expression in Nicotiana tabacum; expression in Nicotiana tabacum
expression in Saccharomyces cerevisiae; gene SmDFR, DNA and amino acid sequence determination and analysis, phylogenetic analysis, quantitative real-time PCR expression analysis, functional expression in Saccharomyces cerevisiae strain INV Sc1
functional expression in tobacco protoplasts via electroporation, subcloning and overexpression in Escherichia coli strain GI724 and in Saccharomyces cerevisiae strain INV Sc1, the recombinant Escherichia coli strain shows no enzyme activity
gene BrDFR10, on chromosome A06, genotyping, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, RT-PCR expression profiling of genotypes, and real-time quantitative PCR analysis; gene BrDFR11, on chromosome A03, genotyping, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, RT-PCR expression profiling of genotypes, and real-time quantitative PCR analysis; gene BrDFR12, on chromosome A08, genotyping, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, RT-PCR expression profiling of genotypes, and real-time quantitative PCR analysis; gene BrDFR1, on chromosome A02, genotyping, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, RT-PCR expression profiling of genotypes, and real-time quantitative PCR analysis; gene BrDFR2, on chromosome A09, genotyping, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, RT-PCR expression profiling of genotypes, and real-time quantitative PCR analysis; gene BrDFR3, genotyping, DNA and amino acid sequence determination and analysis, sequence comparisons, RT-PCR expression profiling of genotypes, and real-time quantitative PCR analysis; gene BrDFR3, on chromosome A02, genotyping, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, RT-PCR expression profiling of genotypes, and real-time quantitative PCR analysis; gene BrDFR4, on chromosome A09, genotyping, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, RT-PCR expression profiling of genotypes, and real-time quantitative PCR analysis; gene BrDFR5, on chromosome A09, genotyping, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, RT-PCR expression profiling of genotypes, and real-time quantitative PCR analysis; gene BrDFR6, on chromosome A09, genotyping, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, RT-PCR expression profiling of genotypes, and real-time quantitative PCR analysis; gene BrDFR7, on chromosome A09, genotyping, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, RT-PCR expression profiling of genotypes, and real-time quantitative PCR analysis; gene BrDFR8, on chromosome A06, genotyping, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, RT-PCR expression profiling of genotypes, and real-time quantitative PCR analysis; gene BrDFR9, on chromosome A06, genotyping, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, RT-PCR expression profiling of genotypes, and real-time quantitative PCR analysis
gene CsDFR, recombinant overexpression in Nicotiana tabacum cv. Xanthi leaves
gene DcDFR, genotyping, quantitative enzyme expression analysis
gene DFR, cloned from the capitulum, DNA and amino acid sequence determination and analysis, quantitative RT-PCR expression analysis
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gene DFR, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, functional recombinant expression in Saccharomyces cerevisiae; gene DFR, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, functional recombinant expression in Saccharomyces cerevisiae; gene DFR, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, functional recombinant expression in Saccharomyces cerevisiae; gene DFR, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, functional recombinant expression in Saccharomyces cerevisiae
gene DFR, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, functional recombinant expression in Saccharomyces cerevisiae; gene DFR, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, functional recombinant expression in Saccharomyces cerevisiae; gene DFR, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, functional recombinant expression in Saccharomyces cerevisiae; gene DFR, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, functional recombinant expression in Saccharomyces cerevisiae; gene DFR, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, functional recombinant expression in Saccharomyces cerevisiae; gene DFR, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, functional recombinant expression in Saccharomyces cerevisiae
gene DgDFR, genotyping, quantitative enzyme expression analysis
gene DnDFR, genotyping, quantitative enzyme expression analysis
gene GbDFR1, DNA and amino acid sequence determination and analysis, sequence comparison, phylogenetic analysis, quantitative isozyme expression analysis; gene GbDFR2, DNA and amino acid sequence determination and analysis, sequence comparison, phylogenetic analysis, quantitative isozyme expression analysis; gene GbDFR3, DNA and amino acid sequence determination and analysis, sequence comparison, phylogenetic analysis, quantitative isozyme expression analysis
gene IbDFR, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, quantitative real-time PCR enzyme expression analysis
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gene McDFR, relative enzyme expression analysis and quantitative RT-PCR enzyme expression analysis, transient overexpression of McDFR in leaves of cultivars Royalty and Flame. McDFR is overexpressed in fruits using the vector pBI121-McDFR
gene TaDFR-A, from cv. Iksan370, DNA and amino acid sequencdetermination and analysis, quantitative PCR enzyme expression analysis, overexpressing the Triticum aestivum dihydroflavonol 4-reductase gene TaDFR under the control of the CaMV35S promoter via Agrobacterium tumefaciens strain GV3101 (C58) transfection in a Arabidopsis thaliana dfr mutant increases anthocyanin accumulation in the mutant
genetic mapping and genotyping, the gene encoding dihydroflavonol 4-reductase is a candidate for the anthocyaninless locus of rapid cycling Brassica rapa (fast plants type)
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into pTrcHis2-TOPO and heterologously expressed in Escherichia coli TOP10F' strain. DFR cDNA cloned into pRSF-FHT and inserted into Escherichia coli BL21Star to create E-color strain
isozyme MtDFR1, from a young seed cDNA library, functional expression in Escherichia coli; isozyme MtDFR2, from a young seed cDNA library, functional expression in Escherichia coli
overexpression in Escherichia coli strain GI724 and in Saccharomyces cerevisiae strain INV Sc1
vector pC1-DFR overexpressed in transgenic tobacco plants, having distinctive petal colors, showing some variation in their intensity
into pTrcHis2-TOPO and heterologously expressed in Escherichia coli TOP10F' strain. DFR cDNA cloned into pRSF-FHT and inserted into Escherichia coli BL21Star to create E-color strain
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into pTrcHis2-TOPO and heterologously expressed in Escherichia coli TOP10F' strain. DFR cDNA cloned into pRSF-FHT and inserted into Escherichia coli BL21Star to create E-color strain
into pTrcHis2-TOPO and heterologously expressed in Escherichia coli TOP10F' strain. DFR cDNA cloned into pRSF-FHT and inserted into Escherichia coli BL21Star to create E-color strain
into pTrcHis2-TOPO and heterologously expressed in Escherichia coli TOP10F' strain. DFR cDNA cloned into pRSF-FHT and inserted into Escherichia coli BL21Star to create E-color strain
into pTrcHis2-TOPO and heterologously expressed in Escherichia coli TOP10F' strain. DFR cDNA cloned into pRSF-FHT and inserted into Escherichia coli BL21Star to create E-color strain
into pTrcHis2-TOPO and heterologously expressed in Escherichia coli TOP10F' strain. DFR cDNA cloned into pRSF-FHT and inserted into Escherichia coli BL21Star to create E-color strain
overexpression in Escherichia coli strain GI724 and in Saccharomyces cerevisiae strain INV Sc1
overexpression in Escherichia coli strain GI724 and in Saccharomyces cerevisiae strain INV Sc1
overexpression in Escherichia coli strain GI724 and in Saccharomyces cerevisiae strain INV Sc1
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overexpression in Escherichia coli strain GI724 and in Saccharomyces cerevisiae strain INV Sc1
overexpression in Escherichia coli strain GI724 and in Saccharomyces cerevisiae strain INV Sc1
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression is down-regulated in response to drought stress and abscisic acid, and unaffected by gibberellic acid treatment
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expression is down-regulated in response to drought stress and abscisic acid, and unaffected by gibberellic acid treatment; in response to drought stress
expression is up-regulated in response to wounding, with concomitant modulation of catechins content
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expression is up-regulated in response to wounding, with concomitant modulation of catechins content; in response to wounding, with concomitant modulation of catechins content. Expression is maximum in younger rather than older leaves
flavanone 3-hydroxylase, dihydroflavonol 4-reductase and flavonoid 3',5'-hydrolase are expressed in progeny with colored tuber skin, while dihydroflavonol 4-reductase and flavonoid 3',5'-hydrolase are not expressed, and flavanone 3-hydroxylase is only weakly expressed, in progeny with white tuber skin. Expression is regulated by transcription factor Stan2
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GbDFR1 expression is induced by UVB radiation, abscisic acid, 5-aminolevulinic acid, and ethephon; GbDFR2 expression is induced by UVB radiation, abscisic acid, ethephon, and salicylic acid , and highly induced by wounding; the GbDFR3 expression is induced by wounding and ethephon
GbDFR1 expression is suppressed by salicylic acid; the GbDFR3 expression is downregulated by abscisic acid
induction of gene BrDFR10 by cold stress dependent on the genotypes, overview; induction of gene BrDFR2 by cold stress dependent on the genotypes, overview; induction of gene BrDFR3 by cold stress dependent on the genotypes, overview; induction of gene BrDFR4 by cold stress dependent on the genotypes, overview; induction of gene BrDFR5 by cold stress dependent on the genotypes, overview; induction of gene BrDFR6 by cold stress dependent on the genotypes, overview; induction of gene BrDFR8 by cold stress dependent on the genotypes, overview; induction of gene BrDFR9 by cold stress dependent on the genotypes, overview
low-dose UV treatment, and 5-aminolevulinic acid, and salicylic acid have no obvious induction effect on GbDFR3; no effect on GbDFR2 expression by 5-aminolevulinic acid; wounding has no effect on GbDFR1 expression
the abundance of endogenous McDFR transcripts is greatly reduced in TRV-McDFR infected leaves
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
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strain DWRCBr57 with the recessive nonpurple phenotype has a transposon-related insertion in the DFR which is predicted to disrupt gene function. Non-purple strains bear an insertion mutation in exon 4 of the DFR gene. Some purple plants have an insertion mutation in the last intron
additional information
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strain DWRCBr57 with the recessive nonpurple phenotype has a transposon-related insertion in the DFR which is predicted to disrupt gene function. Non-purple strains bear an insertion mutation in exon 4 of the DFR gene. Some purple plants have an insertion mutation in the last intron
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additional information
transgenic tobacco overexpressing tea cDNA encoding dihydroflavonol 4-reductase and anthocyanidin reductase induces early flowering, and better seed yield, and provides biotic stress tolerance
additional information
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downregulation of IbDFR expression in transgenic sweet potato by RNAi approach
additional information
fusion of ADH to the N-terminal His-tag causes a strong improvement of about 95% in activity
additional information
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fusion of ADH to the N-terminal His-tag causes a strong improvement of about 95% in activity
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additional information
transient overexpression of McDFR gene in the stem tips of the evergreen cultivar Strawberry Jelly promotes anthocyanin accumulation and a deep green coloration in most of the new buds.
additional information
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overexpression of the isozyme in transgenic Nicotiana tabacum cv. Xanthi under control of the CaMV35S promotor does not lead to increased anthocyanin production in the flowers; overexpression of the isozyme in transgenic Nicotiana tabacum cv. Xanthi under control of the CaMV35S promotor leads to increased anthocyanin production in the flowers
additional information
overexpression of the isozyme in transgenic Nicotiana tabacum cv. Xanthi under control of the CaMV35S promotor does not lead to increased anthocyanin production in the flowers; overexpression of the isozyme in transgenic Nicotiana tabacum cv. Xanthi under control of the CaMV35S promotor leads to increased anthocyanin production in the flowers
additional information
overexpression of the isozyme in transgenic Nicotiana tabacum cv. Xanthi under control of the CaMV35S promotor does not lead to increased anthocyanin production in the flowers; overexpression of the isozyme in transgenic Nicotiana tabacum cv. Xanthi under control of the CaMV35S promotor leads to increased anthocyanin production in the flowers
additional information
expression of TaDFR-I from cultivar Iksan370 lines in Arabidopsis thaliana and detection of the presence of transcriptional regulatory factors similar to those of Arabidopsis that regulate TaDFR expression in response to various abiotic stresses
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
molecular biology
agriculture
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genetic transformation of Melastoma malabathricum and Tibouchina semidecandra, with sense and antisense dihydroflavonol-4-reductase genes using the Agrobacterium-mediated method. Approximately 4.0% of shoots and 6.7% of nodes for Melastoma malabathricum regenerate after transforming with sense dihydroflavonol-4-reductase gene, whereas only 3.7% of shoots and 5.3% of nodes regenerate with antisense dihydroflavonol-4-reductase gene transformation. For the selection of Tibouchina semidecandra, 5.3% of shoots and 9.3% of nodes regenerate with sense dihydroflavonol-4-reductase gene transformation, while only 4.7% of shoots and 8.3% of nodes regenerate after being transformed with antisense dihydroflavonol-4-reductase gene. The colour changes caused by transformation are observed at the budding stage of putative Tibouchina semidecandra transformants The production of four-petal flowers also indicates another morphological difference of putative Tibouchina semidecandra transformants from the wild type plants which produce five-petal flowers
agriculture
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flavanone 3-hydroxylase, dihydroflavonol 4-reductase and flavonoid 3',5'-hydroxylase are expressed in progeny with colored tuber skin, while dihydroflavonol 4-reductase and flavonoid 3,5-hydroxylase are not expressed, and flavanone 3-hydroxylase is only weakly expressed, in progeny with white tuber skin. Expression is regulated by transcription factor Stan2
molecular biology
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the gene encoding dihydroflavonol 4-reductase is a candidate for the anthocyaninless locus of rapid cycling Brassica rapa (fast plants type)
molecular biology
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the gene encoding dihydroflavonol 4-reductase is a candidate for the anthocyaninless locus of rapid cycling Brassica rapa (fast plants type)
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