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Enzyme Nomenclature
Information on EC 1.1.1.219 - dihydroflavonol 4-reductase
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EC Tree
1.1.1.219 dihydroflavonol 4-reductaseIUBMB Comments
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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Word Map
- 1.1.1.219
- chalcone
- flower
- anthocyanidins
-
3\'-hydroxylase
- flavonols
- flavanone
- cultivar
- proanthocyanidins
-
purple
-
phenylpropanoids
- petunia
-
leucoanthocyanidins
-
ammonia-lyase
-
colour
- catechin
-
3',5'-hydroxylase
- pelargonidin
- hybrida
-
ornamental
- delphinidin
-
camellia
- 3-o-glucosyltransferase
-
b-ring
- naringenin
-
r2r3-myb
- anr
- majus
- antirrhinum
- snapdragon
- 3-o-glucoside
- leucocyanidin
- eriodictyol
-
flavan-3-ols
- glory
-
flavonoid-related
- gerbera
-
white-flowered
-
udp-glucose:flavonoid
- tepal
-
3-o-glucosyl
-
4-coumarate-coa
- molecular biology
- agriculture
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
DFR
DFR1
DFR2
DHM reductase
-
-
-
-
DHQ reductase
-
-
-
-
dihydroflavanol 4-reductase
dihydroflavonol 4-reductase
dihydroflavonol-4-reductase
dihydrokaempferol 4-reductase
-
-
-
-
dihydromyricetin reductase
-
-
-
-
dihydroquercetin reductase
-
-
-
-
NADPH-dihydromyricetin reductase
-
-
-
-
PAS_chr3_0449
reductase, dihydromyricetin
-
-
-
-
reductase, dihydroquercetin
-
-
-
-
TRANSPARENT TESTA 3 protein
-
-
-
-
DFR
-
-
-
-
DFR
-
dihydroflavanol 4-reductase
-
-
-
-
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
-
-
-
-
reduction
-
-
-
-
oxidation
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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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
-
98668-58-7
-
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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
(2R,3R)-(+)-dihydrokaempferol + NADPH + H+
(2R,3S,4S)-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+
enzyme specifically reduces the S-enantiomer
-
-
?
2,3-dihydromyricetin + NADPH
cis-3,4-leucodelphinidin + NADP+
low activity
-
-
?
2,3-dihydromyricetin + NADPH + H+
cis-3,4-leucodelphinidin + NADP+
-
-
-
?
2,3-dihydroquercetin + NADPH
cis-3,4-leucocyanidin + NADP+
i.e. (+)-taxifolin, stereospecific for (+)-isomer
-
-
?
2-methylpentanal + NADPH + H+
2-methyl-pentan-1-ol + NADP+
249% of the activity with benzaldehyde
-
-
?
7-hydroxyflavanone + NADPH + H+
2,4-cis-7-hydroxyflavan-4-ol + 2,4-trans-7-hydroxyflavan-4-ol + NADP+
-
-
-
?
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 + H+
hexan-1-ol + NADP+
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+
-
-
-
?
(+)-dihydrokaempferol + NADPH + H+
cis-3,4-leucopelargonidin + NADP+
-
-
-
?
(+)-dihydrokaempferol + NADPH + H+
cis-3,4-leucopelargonidin + NADP+
-
-
-
?
(+)-dihydrokaempferol + NADPH + H+
cis-3,4-leucopelargonidin + NADP+
-
-
-
?
(+)-dihydrokaempferol + NADPH + H+
cis-3,4-leucopelargonidin + NADP+
-
-
-
?
(+)-dihydrokaempferol + NADPH + H+
cis-3,4-leucopelargonidin + NADP+
-
-
-
?
(+)-dihydrokaempferol + NADPH + H+
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
?
(+)-dihydromyricetin + NADPH + H+
cis-3,4-leucodelphinidin + NADP+
-
-
-
?
(+)-dihydromyricetin + NADPH + H+
cis-3,4-leucodelphinidin + NADP+
-
-
-
?
(+)-dihydromyricetin + NADPH + H+
cis-3,4-leucodelphinidin + NADP+
preferred substrate
-
-
?
(+)-dihydromyricetin + NADPH + H+
cis-3,4-leucodelphinidin + NADP+
-
-
-
?
(+)-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+
-
-
-
?
(+)-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+
-
-
-
?
(2E)-hex-2-enal + NADPH + H+
(2E)-hex-2-en-1-ol + NADP+
97% of the activity with benzaldehyde
-
-
?
(2E)-hex-2-enal + NADPH + H+
(2E)-hex-2-en-1-ol + NADP+
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)-3,4-leucodelphinidin + NADP+
-
-
-
?
(2R,3R)-dihydromyricetin + NADPH
(2R,3S,4R)-3,4-leucodelphinidin + NADP+
-
-
-
?
(2R,3R)-dihydromyricetin + NADPH
(2R,3S,4R)-3,4-leucodelphinidin + NADP+
-
-
-
?
(2R,3R)-dihydromyricetin + NADPH
(2R,3S,4R)-3,4-leucodelphinidin + NADP+
-
-
-
-
?
(2R,3R)-dihydromyricetin + NADPH
(2R,3S,4R)-3,4-leucodelphinidin + NADP+
-
-
-
?
(2R,3R)-dihydromyricetin + NADPH
(2R,3S,4R)-3,4-leucodelphinidin + NADP+
-
-
-
?
(2R,3R)-dihydromyricetin + NADPH
(2R,3S,4R)-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+
-
-
-
?
butanal + NADPH + H+
butan-1-ol + NADP+
176% of the activity with benzaldehyde
-
-
?
butanal + NADPH + H+
butan-1-ol + NADP+
176% 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+
-
-
-
?
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+
-
-
-
?
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+
-
-
-
?
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
?
-
isoform DFR1a catalyses dihydromyricetin and dihydrokaempferol with almost the same efficiency, but catalyses dihydroquercetin with a lower efficiency
-
-
-
additional information
?
-
isoform DFR1a catalyses dihydromyricetin and dihydrokaempferol with almost the same efficiency, but catalyses dihydroquercetin with a lower efficiency
-
-
-
additional information
?
-
isoform FeDFR2 catalyses dihydroquercetin about 2 times as efficiently as dihydromyricetin and had least activity for dihydrokaempferol
-
-
-
additional information
?
-
isoform FeDFR2 catalyses dihydroquercetin about 2 times as efficiently as dihydromyricetin and had least activity for dihydrokaempferol
-
-
-
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
?
-
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
-
-
?
additional information
?
-
DFR prefers dihydroquercetin over dihydromyricetin and only converts dihydrokaempferol to a minor extent
-
-
-
additional information
?
-
-
DFR prefers dihydroquercetin over dihydromyricetin and only converts dihydrokaempferol to a minor extent
-
-
-
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NATURAL SUBSTRATE
NATURAL 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+
leucopelargonidin + NADP+
-
-
-
?
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+
-
-
-
?
dihydromyricetin + NADPH + H+
leucodelphinidin + NADP+
-
-
-
?
dihydromyricetin + NADPH + H+
leucodelphinidin + NADP+
-
-
-
?
dihydromyricetin + NADPH + H+
leucodelphinidin + NADP+
-
-
-
?
dihydromyricetin + NADPH + H+
leucodelphinidin + NADP+
-
-
-
?
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+
-
-
-
?
dihydroquercetin + NADPH + H+
cis-3,4-leucocyanidin + NADP+
-
-
-
?
dihydroquercetin + NADPH + H+
cis-3,4-leucocyanidin + NADP+
-
-
-
?
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
?
-
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
?
-
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
?
-
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
?
-
-
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
?
-
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 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
?
-
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
-
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
additional information
-
ascorbate cannot replace NADPH, the reaction occurs equally well anaerobically
-
additional information
-
FMN, FAD or 6,7-dimethyl-5,6,7,8-tetrahydropterine cannot replace NADPH
-
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INHIBITOR
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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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Vaccinia
Expansion of the mammalian 3 beta-hydroxysteroid dehydrogenase/plant dihydroflavonol reductase superfamily to include a bacterial cholesterol dehydrogenase, a bacterial UDP-galactose-4-epimerase, and open reading frames in vaccinia virus and fish lymphocystis disease virus.
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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
0.0003
0.0004
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
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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
line N89-53 and line YN01-429 (a yellow-seeded canola-quality germplasm)
-
-
brenda
var. miniata, an orange flowered variety, and var. citrina, a yellow flowered variety
UniProt
brenda
cvs. Palgangbaechu, 8053, and Seoulbaechu
UniProt
brenda
Fragaria chiloensis x Fragaria virginiana, cv. Elsanta
UniProt
brenda
cultivars Royalty (ever-red leaf cultivar) and Flame (ever-green leaf cultivar)
UniProt
brenda
isozyme MtDFR1; cv. Jemalong, 2 isozymes MtDFR1 and MtDFR2
SwissProt
brenda
isozyme MtDFR2; cv. Jemalong, 2 isozymes MtDFR1 and MtDFR2
SwissProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
high expression level
brenda
-
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
brenda
isoform PtrDFR2 transcripts are more than twice as abundant as isoform DFR1 in young petioles and 15 times more abundant in old petioles
brenda
mRNA accumulation of DFR is higher in the shoots than in the leaves
brenda
additional information
higher expression in orange flowering, moderate expression in fading and yellow flowering
brenda
quantitative enzyme expression analysis in flowers from different cultivars, overview
brenda
quantitative enzyme expression analysis in flowers from different cultivars, overview
brenda
quantitative enzyme expression analysis in flowers from different cultivars, overview
brenda
expression in early and late flowering
brenda
expression in early flowering
brenda
expression in late flowering
brenda
expression in early and late flowering
brenda
expression in early flowering
brenda
expression in flowers is about 8fold higher compared with leaves and roots
brenda
-
brenda
high expression level
brenda
-
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
brenda
-
brenda
expression is maximum in younger rather than older leaves
brenda
expression is maximal in younger rather than older leaves
brenda
-
expression is maximal in younger rather than older leaves
-
brenda
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
brenda
expression in flowers is about 8fold higher compared with leaves and roots
brenda
expression is low or repressed in acyanic areas in petals
brenda
-
brenda
high expression level
brenda
preferential expression in root and seed
brenda
high expression level in root hair and epidermal cells of root tips
brenda
expression in flowers is about 8fold higher compared with leaves and roots
brenda
preferential expression in root and seed
brenda
-
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
brenda
-
brenda
weak expression
brenda
high expression level in lower stem
brenda
additional information
organ-specific DFR expression analysis
brenda
additional information
organ-specific DFR expression analysis
brenda
additional information
organ-specific DFR expression analysis
brenda
additional information
organ-specific DFR expression analysis
brenda
additional information
organ-specific DFR expression analysis
brenda
additional information
organ-specific DFR expression analysis
brenda
additional information
organ-specific DFR expression analysis
brenda
additional information
organ-specific DFR expression analysis
brenda
additional information
organ-specific DFR expression analysis
brenda
additional information
organ-specific DFR expression analysis
brenda
additional information
organ-specific DFR expression analysis
brenda
additional information
organ-specific DFR expression analysis
brenda
additional information
expression in all tissues analyzed, expression correlates positively with polyphenols but negatively with yellow coloration of petals
brenda
additional information
-
expression in all tissues analyzed, expression correlates positively with polyphenols but negatively with yellow coloration of petals
brenda
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
brenda
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
brenda
additional information
expression in all organs investigated
brenda
additional information
expression in all organs investigated
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
additional information
-
tissue expression profiles of DFR isozymes, overview. During the annual growth cycle, the GbDFRs are significantly correlated with anthocyanin accumulation in leaves
brenda
additional information
tissue expression profiles of DFR isozymes, overview. During the annual growth cycle, the GbDFRs are significantly correlated with anthocyanin accumulation in leaves
brenda
additional information
-
enzyme expression analysis in different tissues and anthocyanidins contents, overview
brenda
additional information
developmental gene expression pattern
brenda
additional information
developmental gene expression pattern
brenda
additional information
-
transcripts are found in all tissues examined, but most concentrated in root
brenda
additional information
transcripts are found in all tissues examined, but most concentrated in root
brenda
additional information
expression level of SmDFR is higher in flowers compared with both leaves and roots
brenda
additional information
-
expression level of SmDFR is higher in flowers compared with both leaves and roots
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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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
-
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
evolution
-
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
-
malfunction
-
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
overexpressing the Triticum aestivum dihydroflavonol 4-reductase gene TaDFR increases anthocyanin accumulation in an Arabidopsis thaliana dfr mutant
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
-
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
-
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
-
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
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
metabolism
-
dihydroflavonol-4-reductase (DFR) is a key enzyme in the catalysis of the stereospecific reduction of dihydroflavonols to leucoanthocyanidins in anthocyanin biosynthesis
metabolism
the enzyme is involved in anthocyanin biosynthesis
metabolism
-
the enzyme is involved in anthocyanin biosynthesis
metabolism
the enzyme is involved in flavonoid pathway. Flavonol synthase and dihydroflavonol-4-reductase compete for common substrates in order to direct the biosynthesis of flavonols and anthocyanins, respectively, thereby determining white vs. red coloration of flowers
metabolism
the enzyme is involved in flavonoid pathway. Flavonol synthase and dihydroflavonol-4-reductase compete for common substrates in order to direct the biosynthesis of flavonols and anthocyanins, respectively, thereby determining white vs. red coloration of flowers
metabolism
the enzyme is involved in flavonoid pathway. Flavonol synthase and dihydroflavonol-4-reductase compete for common substrates in order to direct the biosynthesis of flavonols and anthocyanins, respectively, thereby determining white vs. red coloration of flowers
physiological function
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
DFR can fully complement the potato locus R, both in terms of tuber color and anthocyanin composition
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
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
synthesis of(+)-catechin by leucoanthocyanidin reductase may be tied to regulation of DFR
physiological function
overexpressing isoform DFR2 in Populus tomentosa Carr improves condensed tannin accumulations
physiological function
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
the enzyme is of importance in plant development
physiological function
BrDFR isozymes are regulated by two transcription factors, BrMYB2-2 and BrTT8, contrasting with anthocyanin accumulation and cold and freezing stress
physiological function
dihydroflavonol 4-reductase, DFR, is a key enzyme responsible for the NADPH-dependent reduction of dihydroflavonols to colourless leucoanthocyanidins
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
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
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, 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
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 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 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 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
physiological function
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
physiological function
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
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
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
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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
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
the concentrations of anthocyanins and flavonols correlates with leaf color. It is proposed that the expression of dihydroflavonol 4-reductase and flavonol synthase influences their accumulation. Overexpression of dihydroflavonol 4-reductase, or silencing of flavonol synthase, increases anthocyanin production, resulting in red-leaf and red fruit peel phenotypes. Conversely, elevated flavonol production and green phenotypes in crabapple leaves and apple peel are observed when dihydroflavonol 4-reductase is overexpressed or dihydroflavonol 4-reductase is silenced. These results suggest that the relative activities of dihydroflavonol 4-reductase and flavonol synthase are important determinants of the red color of crabapple leaves, via the regulation of the metabolic fate of substrates that these enzymes have in common
physiological function
the enzyme is involved in flavonoid pathway. Flavonol synthase and dihydroflavonol-4-reductase compete for common substrates in order to direct the biosynthesis of flavonols and anthocyanins, respectively, thereby determining white vs. red coloration of flowers
physiological function
the enzyme is involved in flavonoid pathway. Flavonol synthase and dihydroflavonol-4-reductase compete for common substrates in order to direct the biosynthesis of flavonols and anthocyanins, respectively, thereby determining white vs. red coloration of flowers
physiological function
the enzyme is involved in flavonoid pathway. Flavonol synthase and dihydroflavonol-4-reductase compete for common substrates in order to direct the biosynthesis of flavonols and anthocyanins, respectively, thereby determining white vs. red coloration of flowers
physiological function
dihydroflavanol-4-reductase-like protein DFL1 interacts with Nod factor receptor NFR5. DFL1 mutants produce significantly fewer infection threads than wild-type follwing rhizobial treatment. Roots of stable transgenic Lotus japonicus plants overexpressing DFL1 form more infection threads than control roots
physiological function
ectopic overexpression in Nicotiana tabacum enhances the biosynthesis of polyphenols, while no accumulation of anthocyanins is detected
physiological function
enzyme is able to complement an Arabidopsis thaliana Dfr mutant (tt3-1) at seedling stage and to restore proanthocyanidin biosynthesis in the seed
physiological function
enzyme is not able to complement an Arabidopsis thaliana Dfr mutant
physiological function
expression of DFR in Nicotiana tabacum results in increased anthocyanin accumulation, leading to a darker flower color
physiological function
silencing of DFR1 results in a substantial decrease in anthocyanin accumulation, overexpression of DFR1 restores some anthocyanin accumulation. Enzyme is involved in anthocyanin accumulation in pink-leaved ornamental plants
physiological function
transgenic overexpression in Nicotiana tabacum increases anthocyanin production in flowers. Transgenic flowers produce pelargonidin and delphinidin, which are not found in controls
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
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
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
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
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
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
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
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
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
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
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
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
additional information
-
the gene encoding dihydroflavonol 4-reductase is a candidate for the anthocyaninless locus of rapid cycling Brassica rapa (fast plants type)
additional information
-
the gene encoding dihydroflavonol 4-reductase is a candidate for the anthocyaninless locus of rapid cycling Brassica rapa (fast plants type)
-
Show AA Sequence and Transmembrane Helices (693 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
34762
-
34860
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35420
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35520
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35860
-
35910
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36158
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36320
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38670
39650
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40300
40450
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41000
38670
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
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
?
x * 34760, sequence calculation
?
x * 34860, 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
?
x * 38670, calculated, x * 41000, SDS-PAGE of recombinant protein with fusion peptide
?
-
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
additional information
sequence analysis and structure homology, overview
additional information
sequence analysis and structure homology, overview
additional information
sequence analysis and structure homology, overview
additional information
sequence analysis and structure homology, overview
additional information
sequence analysis and structure homology, overview
additional information
sequence analysis and structure homology, overview
additional information
sequence analysis and structure homology, overview
additional information
sequence analysis and structure homology, overview
additional information
sequence analysis and structure homology, overview
additional information
sequence analysis and structure homology, overview
additional information
sequence analysis and structure homology, overview
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
molecular docking of substrates. A phenol ring of dihydrokaempferol, a catechol ring of dihydroquercetin, and a pyrogallol ring of dihydromyricetin respectively have two, three, and four hydrogen bonds formed with side chains of residue Asn132
molecular docking of substrates. The number of hydrogen bonds is one, two, and two for the corresponding p