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(+)-2,3-dihydrokaempferol + NADPH
cis-3,4-leucopelargonidin + NADP+
(+)-dihydrokaempferol + NADPH
cis-3,4-leucopelargonidin + NADP+
(+)-dihydrokaempferol + NADPH + H+
cis-3,4-leucopelargonidin + NADP+
(+)-dihydromyricetin + NADPH
cis-3,4-leucodelphinidin + NADP+
(+)-dihydromyricetin + NADPH + H+
cis-3,4-leucodelphinidin + NADP+
(+)-dihydroquercetin + NADPH
cis-3,4-leucocyanidin + NADP+
(+)-dihydroquercetin + NADPH + H+
cis-3,4-leucocyanidin + NADP+
(+/-)-fustin + NADPH
?
preference for (-)-isomer
-
-
?
(+/-)-taxifolin + NADPH
? + NADP+
-
-
-
-
?
(-)-fustin + NADPH
?
stereospecific for (-)-isomer
-
-
?
(2E)-hex-2-enal + NADPH + H+
(2E)-hex-2-en-1-ol + NADP+
(2R,3R)-(+)-dihydrokaempferol + NADPH
(2R,3S,4S)-cis-3,4-leucopelargonidin + NADP+
(2R,3R)-(+)-dihydrokaempferol + NADPH + H+
(2R,3S,4S)-cis-3,4-leucopelargonidin + NADP+
-
-
-
?
(2R,3R)-dihydromyricetin + NADPH
(2R,3S,4R)-3,4-leucodelphinidin + NADP+
(2R,3R)-dihydroquercetin + NADPH
(2R,3S,4R)-leucocyanidin + NADP+
(2S)-hexan-2-ol + NADP+
hexan-2-one + NADPH + H+
(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
-
-
?
2,3-dihydrorobinetin + NADPH
?
-
-
-
?
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+
-
-
-
?
benzaldehyde + NADPH + H+
benzyl alcohol + NADP+
butanal + NADPH + H+
butan-1-ol + NADP+
dihydroflavonol + NADPH
flavan-3,4-diol + NADP+
-
-
-
-
?
dihydrokaempferol + NADPH
cis-3,4-leucopelargonidin + NADP+
-
-
-
-
r
dihydrokaempferol + NADPH + H+
leucopelargonidin + NADP+
dihydromyricetin + NADPH
cis-3,4-leucodelphinidin + NADP+
-
-
-
-
?
dihydromyricetin + NADPH
leucodelphinidin + NADP+
-
-
-
-
r
dihydromyricetin + NADPH + H+
leucodelphinidin + NADP+
dihydroquercetin + NADPH
?
-
assay at 25ưC, pH 7.5
-
-
?
dihydroquercetin + NADPH
cis-3,4-leucocyanidin + NADP+
dihydroquercetin + NADPH
leucocyanidin + NADP+
-
-
-
-
r
dihydroquercetin + NADPH + H+
cis-3,4-leucocyanidin + NADP+
dihydroquercetin + NADPH + H+
leucocyanidin + NADP+
eriodictyol + NADPH + H+
luteoforol + 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
-
-
?
naringenin + NADPH + H+
apiferol + NADP+
additional information
?
-
(+)-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+
-
-
-
?
(+)-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
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+
-
-
-
?
(+)-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+
-
-
-
?
(2R,3R)-dihydroquercetin + NADPH
(2R,3S,4R)-leucocyanidin + NADP+
-
-
-
?
(2S)-hexan-2-ol + NADP+

hexan-2-one + NADPH + H+
-
-
-
r
(2S)-hexan-2-ol + NADP+
hexan-2-one + NADPH + H+
-
-
-
r
benzaldehyde + NADPH + H+

benzyl alcohol + NADP+
-
-
-
?
benzaldehyde + NADPH + H+
benzyl alcohol + 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+
M4D235, M4DRB9, M4DU26, M4DU27, M4DU28, M4E380, M4E7I9, M4E7J1, M4E7J2, M4ECU0, M4ES88, M4FB76 -
-
-
?
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+
-
-
-
?
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+
M4D235, M4DRB9, M4DU26, M4DU27, M4DU28, M4E380, M4E7I9, M4E7J1, M4E7J2, M4ECU0, M4ES88, M4FB76 -
-
-
?
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+
-
-
-
?
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

cis-3,4-leucocyanidin + NADP+
-
-
-
-
?
dihydroquercetin + NADPH
cis-3,4-leucocyanidin + NADP+
-
-
-
-
?
dihydroquercetin + NADPH
cis-3,4-leucocyanidin + NADP+
-
-
-
-
?
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+
-
-
-
?
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+
cis-3,4-leucocyanidin + NADP+
-
-
-
?
dihydroquercetin + NADPH + H+
cis-3,4-leucocyanidin + NADP+
-
-
-
?
dihydroquercetin + NADPH + H+

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+
-
-
-
?
dihydroquercetin + NADPH + H+
leucocyanidin + NADP+
-
-
-
?
dihydroquercetin + NADPH + H+
leucocyanidin + NADP+
-
-
-
?
dihydroquercetin + NADPH + H+
leucocyanidin + NADP+
-
-
-
?
dihydroquercetin + NADPH + H+
leucocyanidin + NADP+
-
-
-
?
dihydroquercetin + NADPH + H+
leucocyanidin + NADP+
-
-
-
?
dihydroquercetin + NADPH + H+
leucocyanidin + NADP+
-
-
-
?
dihydroquercetin + NADPH + H+
leucocyanidin + NADP+
-
-
-
?
dihydroquercetin + NADPH + H+
leucocyanidin + NADP+
-
-
-
-
?
eriodictyol + NADPH + H+

luteoforol + NADP+
-
-
-
?
eriodictyol + NADPH + H+
luteoforol + NADP+
-
-
-
?
eriodictyol + NADPH + H+
luteoforol + NADP+
-
-
-
?
eriodictyol + NADPH + H+
luteoforol + NADP+
-
-
-
?
eriodictyol + NADPH + H+
luteoforol + NADP+
-
-
-
?
naringenin + NADPH + H+

apiferol + NADP+
-
-
-
?
naringenin + NADPH + H+
apiferol + NADP+
-
-
-
?
naringenin + NADPH + H+
apiferol + NADP+
-
-
-
?
naringenin + NADPH + H+
apiferol + NADP+
-
-
-
?
additional information

?
-
can not reduce hesperetin or 5,7-dimethoxyflavanone
-
-
?
additional information
?
-
does not catalyze naringenin
-
-
?
additional information
?
-
stereospecific reaction
-
-
?
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
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additional information
?
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isoform FeDFR2 catalyses dihydroquercetin about 2 times as efficiently as dihydromyricetin and had least activity for dihydrokaempferol
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additional information
?
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DFR exhibits selectivity for the B-ring hydroxylation pattern of flavonoid substrates
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?
additional information
?
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DFR exhibits selectivity for the B-ring hydroxylation pattern of flavonoid substrates
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?
additional information
?
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DFR exhibits selectivity for the B-ring hydroxylation pattern of flavonoid substrates
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?
additional information
?
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DFR exhibits selectivity for the B-ring hydroxylation pattern of flavonoid substrates
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?
additional information
?
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DFR exhibits selectivity for the B-ring hydroxylation pattern of flavonoid substrates
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?
additional information
?
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DFR exhibits selectivity for the B-ring hydroxylation pattern of flavonoid substrates
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?
additional information
?
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DFR exhibits selectivity for the B-ring hydroxylation pattern of flavonoid substrates
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?
additional information
?
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DFR exhibits selectivity for the B-ring hydroxylation pattern of flavonoid substrates
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?
additional information
?
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DFR exhibits selectivity for the B-ring hydroxylation pattern of flavonoid substrates
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?
additional information
?
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DFR exhibits selectivity for the B-ring hydroxylation pattern of flavonoid substrates
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?
additional information
?
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DFR exhibits selectivity for the B-ring hydroxylation pattern of flavonoid substrates
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?
additional information
?
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DFR exhibits selectivity for the B-ring hydroxylation pattern of flavonoid substrates
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?
additional information
?
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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
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?
additional information
?
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linear and branched aliphatic aldehydes are good substrates
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?
additional information
?
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linear and branched aliphatic aldehydes are good substrates
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?
additional information
?
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does not catalyze dihydrokaempferol and naringenin
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?
additional information
?
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reaction in anthocyanidin biosynthesis in plants
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?
additional information
?
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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
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?
additional information
?
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key enzyme in flux control in biosynthetic branched pathways leading to anthocyanins and condensed tannins
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?
additional information
?
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key enzyme in flux control in biosynthetic branched pathways leading to anthocyanins and condensed tannins
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?
additional information
?
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key enzyme in flux control in biosynthetic branched pathways leading to anthocyanins and condensed tannins
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?
additional information
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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
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?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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biosynthesis of proanthocyanidin polymers (condensed tannins)
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?
additional information
?
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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
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?
additional information
?
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no activity with (+)-dihydrokaempferol
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?
additional information
?
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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
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?
additional information
?
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no activity with (+)-dihydrokaempferol
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?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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no activity in reduction of dihydromyricetin
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additional information
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no activity in reduction of dihydromyricetin
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additional information
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no substrate: dihydromyricetin. enzyme additionally shows flavanone-4-reductase activity, EC 1.1.1.234
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additional information
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no substrate: dihydromyricetin. enzyme additionally shows flavanone-4-reductase activity, EC 1.1.1.234
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?
additional information
?
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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
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?
additional information
?
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no activity with (+)-dihydrokaempferol
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?
additional information
?
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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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?
additional information
?
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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
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?
additional information
?
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DFR prefers dihydroquercetin over dihydromyricetin and only converts dihydrokaempferol to a minor extent
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additional information
?
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DFR prefers dihydroquercetin over dihydromyricetin and only converts dihydrokaempferol to a minor extent
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high expression level
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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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isoform PtrDFR2 transcripts are more than twice as abundant as isoform DFR1 in young petioles and 15 times more abundant in old petioles
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mRNA accumulation of DFR is higher in the shoots than in the leaves
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cultured from petioles
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cultured from needles
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a red callus line
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from young shoot apex
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from petioles
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from needles
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higher expression in orange flowering, moderate expression in fading and yellow flowering
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quantitative enzyme expression analysis in flowers from different cultivars, overview
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quantitative enzyme expression analysis in flowers from different cultivars, overview
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quantitative enzyme expression analysis in flowers from different cultivars, overview
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expression in early and late flowering
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expression in early flowering
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expression in late flowering
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expression in early and late flowering
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expression in early flowering
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expression in flowers is about 8fold higher compared with leaves and roots
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M4D235, M4DRB9, M4DU26, M4DU27, M4DU28, M4E380, M4E7I9, M4E7J1, M4E7J2, M4ECU0, M4ES88, M4FB76 -
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M4D235, M4DRB9, M4DU26, M4DU27, M4DU28, M4E380, M4E7I9, M4E7J1, M4E7J2, M4ECU0, M4ES88, M4FB76 high expression level
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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
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M4D235, M4DRB9, M4DU26, M4DU27, M4DU28, M4E380, M4E7I9, M4E7J1, M4E7J2, M4ECU0, M4ES88, M4FB76 -
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young
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expression is maximum in younger rather than older leaves
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expression is maximal in younger rather than older leaves
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expression is maximal in younger rather than older leaves
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young
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young
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young, high expression level
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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
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young
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low amount
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young
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young
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expression in flowers is about 8fold higher compared with leaves and roots
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young
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young
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expression is low or repressed in acyanic areas in petals
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M4D235, M4DRB9, M4DU26, M4DU27, M4DU28, M4E380, M4E7I9, M4E7J1, M4E7J2, M4ECU0, M4ES88, M4FB76 -
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high expression level
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preferential expression in root and seed
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high expression level in root hair and epidermal cells of root tips
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highest accumulation of transcripts
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expression in flowers is about 8fold higher compared with leaves and roots
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preferential expression in root and seed
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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
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high expression level
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M4D235, M4DRB9, M4DU26, M4DU27, M4DU28, M4E380, M4E7I9, M4E7J1, M4E7J2, M4ECU0, M4ES88, M4FB76 -
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M4D235, M4DRB9, M4DU26, M4DU27, M4DU28, M4E380, M4E7I9, M4E7J1, M4E7J2, M4ECU0, M4ES88, M4FB76 weak expression
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high expression level in lower stem
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additional information

spathe
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additional information
organ-specific DFR expression analysis
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additional information
organ-specific DFR expression analysis
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additional information
organ-specific DFR expression analysis
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additional information
organ-specific DFR expression analysis
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additional information
organ-specific DFR expression analysis
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additional information
organ-specific DFR expression analysis
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additional information
organ-specific DFR expression analysis
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additional information
organ-specific DFR expression analysis
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additional information
organ-specific DFR expression analysis
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additional information
organ-specific DFR expression analysis
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additional information
organ-specific DFR expression analysis
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additional information
organ-specific DFR expression analysis
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additional information
expression in all tissues analyzed, expression correlates positively with polyphenols but negatively with yellow coloration of petals
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additional information
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expression in all tissues analyzed, expression correlates positively with polyphenols but negatively with yellow coloration of petals
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additional information
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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
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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
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additional information
expression in all organs investigated
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additional information
expression in all organs investigated
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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
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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
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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
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tissue expression profiles of DFR isozymes, overview. During the annual growth cycle, the GbDFRs are significantly correlated with anthocyanin accumulation in leaves
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additional information
tissue expression profiles of DFR isozymes, overview. During the annual growth cycle, the GbDFRs are significantly correlated with anthocyanin accumulation in leaves
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additional information
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enzyme expression analysis in different tissues and anthocyanidins contents, overview
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additional information
developmental gene expression pattern
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additional information
developmental gene expression pattern
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additional information
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developmental gene expression pattern
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additional information
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transcripts are found in all tissues examined, but most concentrated in root
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additional information
transcripts are found in all tissues examined, but most concentrated in root
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additional information
expression level of SmDFR is higher in flowers compared with both leaves and roots
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additional information
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expression level of SmDFR is higher in flowers compared with both leaves and roots
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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
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

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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
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
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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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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

part of flavonoid biosynthetic pathway
metabolism
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key regulatory enzyme of the flavonoid pathway
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
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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
the enzyme is involved in anthocyanin biosynthesis
metabolism
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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
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commits phenolics to proanthocyanidin synthesis
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
M4D235, M4DRB9, M4DU26, M4DU27, M4DU28, M4E380, M4E7I9, M4E7J1, M4E7J2, M4ECU0, M4ES88, M4FB76 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
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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
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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
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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
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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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