Information on EC 1.3.1.77 - anthocyanidin reductase

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The expected taxonomic range for this enzyme is: Spermatophyta

EC NUMBER
COMMENTARY
1.3.1.77
-
RECOMMENDED NAME
GeneOntology No.
anthocyanidin reductase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
a flavan-3-ol + 2 NAD(P)+ = an anthocyanidin + 2 NAD(P)H + H+
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
oxidation
Q84XT1
-
oxidation
Q6DV46
-
redox reaction
Q84XT1
-
reduction
Q84XT1
-
reduction
Q6DV46
-
PATHWAY
KEGG Link
MetaCyc Link
2,3-cis-flavanols biosynthesis
-
Biosynthesis of secondary metabolites
-
Flavonoid biosynthesis
-
proanthocyanidin biosynthesis from flavanols
-
SYSTEMATIC NAME
IUBMB Comments
flavan-3-ol:NAD(P)+ oxidoreductase
Forms 2,3-cis-flavan-3-ols. The isomeric 2,3-trans-flavan-3-ols are formed from flavan-3,4-diols by EC 1.17.1.3 leucoanthocyanidin reductase. While the enzyme from the legume Medicago truncatula (MtANR) uses both NADPH and NADH as reductant, that from the crucifer Arabidopsis thaliana (AtANR) uses only NADPH. Also, while the substrate preference of MtANR is cyanidin>pelargonidin>delphinidin, the reverse preference is found with AtANR.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
ANR
A4PB65
-
ANR
A2IBG2
-
ANR
A1XEG2, A1XEG3, A1XEG4, A1XEG5, A1XEG6, A1XEG7, A1XEG8
-
ANR
Vitis vinifera Cabernet Sauvignon
-
-
-
ANR
-
-
ANR1
-
-
ANR2
-
-
anthocyanidin reductase
-
-
anthocyanidin reductase
Q6DV46
-
anthocyanidin reductase
-
-
anthocyanidin reductase
-
-
anthocyanidin reductase
Q5FB34
-
AtANR
Q84XT1
-
CsANR1
-
enzymes possess epimerase activity
CsANR2
-
enzymes possess epimerase activity
dihydroflavonol 4-reductase-like protein
-
-
flavan-3-ol C3-epimerase
-
-
flavan-3-ol C3-epimerase
Vitis vinifera Cabernet Sauvignon
-
-
-
MtANR
Q84XT1
-
VvANR
Q7PCC4
-
CAS REGISTRY NUMBER
COMMENTARY
93389-48-1
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
gene BANYULS orthologue, BAN
UniProt
Manually annotated by BRENDA team
genetic transformation of Arabidopsis thaliana with the Arabidopsis TT2 MYB transcription factor results in ectopic expression of the BANYULS gene, encoding anthocyanidin reductase, AHA10 encoding a P-type proton-pump and TT12 encoding a transporter involved in proanthocyanidin biosynthesis. When coupled with constitutive expression of PAP1, a positive regulator of anthocyanin biosynthesis, TT2 expression in Arabidopsis leads to the accumulation of proanthocyanidins, but only in a subset of cells in which the BANYULS promoter is naturally expressed. Ectopic expression of the maize Lc MYC transcription factor weakly induces AHA10 but does not induce BANYULS, TT12 or accumulation of proanthocyanidins
-
-
Manually annotated by BRENDA team
Arabidopsis thaliana Wassilevskija-2 ecotype
gene BANYULS orthologue, BAN
UniProt
Manually annotated by BRENDA team
gene BANYULS orthologue, four copies of BAN, two originating from each diploid progenitor
UniProt
Manually annotated by BRENDA team
Brassica napus Westar
gene BANYULS orthologue, four copies of BAN, two originating from each diploid progenitor
UniProt
Manually annotated by BRENDA team
gene BANYULS orthologue, BAN
D0QXJ3, D0QXJ3 AND D0QXJ4
UniProt
Manually annotated by BRENDA team
gene BANYULS orthologue, BAN
D0QXJ5
UniProt
Manually annotated by BRENDA team
gene BANYULS orthologue, BAN
UniProt
Manually annotated by BRENDA team
-
Q6DV46
UniProt
Manually annotated by BRENDA team
cultivar Hiratanenashi
UniProt
Manually annotated by BRENDA team
cultivar Queen Elisa
-
-
Manually annotated by BRENDA team
brown-fiber cotton line T586
UniProt
Manually annotated by BRENDA team
isozyme ANR1-1; genotype S41, cultivar Leo
UniProt
Manually annotated by BRENDA team
isozyme ANR1-2; genotype S41, cultivar Leo
A1XEG3
UniProt
Manually annotated by BRENDA team
isozyme ANR1-3; genotype S41, cultivar Leo
UniProt
Manually annotated by BRENDA team
isozyme ANR1-4; genotype S41, cultivar Leo
UniProt
Manually annotated by BRENDA team
isozyme ANR1; genotype S41, cultivar Leo
UniProt
Manually annotated by BRENDA team
isozyme ANR2; genotype S41, cultivar Leo
UniProt
Manually annotated by BRENDA team
isozyme ANR3; genotype S41, cultivar Leo
UniProt
Manually annotated by BRENDA team
cultivar Golden Delicious, Niedzwetz-kyana, Weirouge, Klarapfel, Red Delicious, Elstar, Holsteiner Cox, Pinova and Pilot
-
-
Manually annotated by BRENDA team
cultivar Cabernet Sauvignon
UniProt
Manually annotated by BRENDA team
L. cv. Cabernet-Sauvignon
-
-
Manually annotated by BRENDA team
L. cv. Shiraz
SwissProt
Manually annotated by BRENDA team
Vitis vinifera Cabernet Sauvignon
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
malfunction
-
ectopic expression of CsANR2 leads to the accumulation of low levels of proanthocyanidin precursors and their conjugates in Medicago truncatula hairy roots and anthocyanin-overproducing tobacco (Nicotiana tabacum), but levels of oligomeric proanthocyanidins are low
malfunction
-
overexpression of PtrANR1 in poplar results in a significant increase in proanthocyanidin levels but no impact on catechin levels. Antisense down-regulation of PtrANR1 shows reduced proanthocyanidin accumulation in transgenic lines, but increased levels of anthocyanin content
malfunction
-
overexpression of tea dihydroflavonol 4-reductase (DFR) and anthocyanidin reductase (ANR) proteins in transgenic tobacco induces early flowering and improves seed yield. The CsDFR/CsANR overexpression increases the accumulation of flavonoids, thereby improves antioxidant potential and redox state of transgenic tobacco plants. Improved antioxidant potential upon CsDFR and CsANR overexpression in transgenic tobacco provides biotic stress tolerance against Spodoptera litura
physiological function
Q9SEV0
ANR is a key enzyme of procyanidin biosynthesis in Arabidopsis seed
physiological function
Arabidopsis thaliana Wassilevskija-2 ecotype
-
ANR is a key enzyme of procyanidin biosynthesis in Arabidopsis seed
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(+)-epicatechin + 2 NADP+
cyanidin + 2 NADPH + 2 H+
show the reaction diagram
-
-
-
-
?
(+)-epicatechin + 2 NADP+
cyanidin + 2 NADPH + 2 H+
show the reaction diagram
-
-, a mixture of C3-epimers of 2S configuration is produced in the reverse reaction
-
-
r
(+)-epicatechin + 2 NADP+
cyanidin + 2 NADPH + 2 H+
show the reaction diagram
Vitis vinifera Cabernet Sauvignon
-
-, a mixture of C3-epimers of 2S configuration is produced in the reverse reaction
-
-
r
(-)-catechin + 2 NADP+
cyanidin + 2 NADPH + 2 H+
show the reaction diagram
-
-, a mixture of C3-epimers of 2S configuration is produced in the reverse reaction
-
-
r
(-)-catechin + 2 NADP+
cyanidin + 2 NADPH + 2 H+
show the reaction diagram
Vitis vinifera Cabernet Sauvignon
-
-, a mixture of C3-epimers of 2S configuration is produced in the reverse reaction
-
-
r
(2S,3R)-flavan-3-ol + 2 NADP+
an anthocyanidin + 2 NADPH + H+
show the reaction diagram
-
Vitis vinifera anthocyanidin reductase, ANR, catalyzes an NADPH-dependent double reduction of anthocyanidins producing a mixture of (2S,3R)- and (2S,3S)-flavan-3-ols, product identification, overview. At pH 7.5 and 30C, the first hydride transfer to anthocyanidin is irreversible, and no intermediate is released during catalysis. ANR reverse activity is assessed in the presence of excess NADP+
-
-
r
(2S,3S)-flavan-3-ol + 2 NADP+
an anthocyanidin + 2 NADPH + H+
show the reaction diagram
-
Vitis vinifera anthocyanidin reductase, ANR, catalyzes an NADPH-dependent double reduction of anthocyanidins producing a mixture of (2S,3R)- and (2S,3S)-flavan-3-ols, product identification, overview. At pH 7.5 and 30C, the first hydride transfer to anthocyanidin is irreversible, and no intermediate is released during catalysis. ANR reverse activity is assessed in the presence of excess NADP+
-
-
r
2,3-cis-flavan-3-ol + NAD(P)+
anthocyanidin + NAD(P)H + H+
show the reaction diagram
Q84XT1
the enzyme is involved in formation of condensed tannins. The enzyme competes with anthocyanidin synthase, for the pool of flavan-3,4-diol
-
-
?
anthocyanidin + NAD(P)H
2,3-cis-flavan-3-ol + NAD(P)+
show the reaction diagram
-
enzyme of flavonoid pathway involved in the biosynthesis of condensed tannins
-
-
?
anthocyanidin + NAD(P)H + H+
2,3-cis-flavan-3-ol + NAD(P)+
show the reaction diagram
-
-
-
-
?
anthocyanidin + NAD(P)H + H+
2,3-cis-flavan-3-ol + NAD(P)+
show the reaction diagram
A4PB65
-
-
-
?
anthocyanidin + NAD(P)H + H+
2,3-cis-flavan-3-ol + NAD(P)+
show the reaction diagram
A2IBG2, -
-
-
-
?
anthocyanidin + NAD(P)H + H+
2,3-cis-flavan-3-ol + NAD(P)+
show the reaction diagram
Q5FB34
-
-
-
?
cyanidin + NAD(P)H + H+
(-)-epicatechin + NAD(P)+
show the reaction diagram
-
-
-
-
?
cyanidin + NAD(P)H + H+
(-)-epicatechin + NAD(P)+
show the reaction diagram
-
-
-
-
?
cyanidin + NAD(P)H + H+
(-)-epicatechin + NAD(P)+
show the reaction diagram
Q5FB34
-
-
-
?
cyanidin + NAD(P)H + H+
(-)-epicatechin + NAD(P)+
show the reaction diagram
-
100% activity
-
-
?
cyanidin + NADPH
(-)-epicatechin + NAD(P)+
show the reaction diagram
-
-
-
-
?
cyanidin + NADPH
(-)-epicatechin + NAD(P)+
show the reaction diagram
-
preference of anthocyanidin substrates in decreasing order: cyanidin, pelargonidin and delphinidin
-
-
?
cyanidin + NADPH
epicatechin + NADP+
show the reaction diagram
-
-
-
-
?
cyanidin + NADPH + H+
(-)-epicatechin + NADP+
show the reaction diagram
-
-
-
-
?
cyanidin + NADPH + H+
(-)-epicatechin + NADP+
show the reaction diagram
-
-
-
-
?
cyanidin + NADPH + H+
(-)-epicatechin + NADP+
show the reaction diagram
A1XEG2, A1XEG3, A1XEG4, A1XEG5, A1XEG6, A1XEG7, A1XEG8, -
-
-
-
?
cyanidin + NADPH + H+
(-)-epicatechin + NADP+
show the reaction diagram
A4PB65
-
-
-
?
cyanidin + NADPH + H+
(-)-epicatechin + NADP+
show the reaction diagram
-
ANR1 or ANR2 converts cyanidin to a mixture of (+)-epicatechin and (-)-catechin, although in different proportions, indicating that both enzymes possess epimerase activity
-
-
?
cyanidin + NADPH + H+
(-)-epicatechin + NADP+
show the reaction diagram
-
changes in the concentration of products and coenzyme in the ANR assay are determined by thin layer chromatography (TLC), HPLC, mass spectrometry (MS) and UV spectrophotometry
-
-
?
cyanidin + NADPH + H+
(2S,3R)-3',4',5,7-tetrahydroxyflavan-3-ol + NADP+
show the reaction diagram
-
enzyme produces a 50:50 mixture of (2S,3S)-flavan-3-ol and (2S,3R)-flavan-3-ol, i.e. (+)-epicatechin and (-)-catechin
-
-
?
cyanidin + NADPH + H+
(2S,3S)-3',4',5,7-tetrahydroxyflavan-3-ol + NADP+
show the reaction diagram
-
enzyme produces a 50:50 mixture of (2S,3S)-flavan-3-ol and (2S,3R)-flavan-3-ol, i.e. (+)-epicatechin and (-)-catechin
-
-
?
cyanidin + NADPH + H+
(+)-epicatechin + NADP+
show the reaction diagram
Q5FB34
enzyme produces a 50:50 mixture of 2S,3S-flavan-3-ol and 2S,3R-flavan-3-ol, i.e. (+)-epicatechin and (-)-catechin
-
-
?
cyanidin + NADPH + H+
(-)-catechin + NADP+
show the reaction diagram
Q5FB34
enzyme produces a 50:50 mixture of 2S,3S-flavan-3-ol and 2S,3R-flavan-3-ol, i.e. (+)-epicatechin and (-)-catechin
-
-
?
cyanidin + NADPH + H+
epicatechin + NADP+
show the reaction diagram
-, Q6DV46
-
-
-
?
delphinidin + 2 NADPH + H+
(-)-epigallocatechin + 2 NADP+
show the reaction diagram
-
-
-
-
?
delphinidin + 2 NADPH + H+
(-)-epigallocatechin + 2 NADP+
show the reaction diagram
-
preference of anthocyanidin substrates in decreasing order: cyanidin, pelargonidin and delphinidin
-
-
?
delphinidin + NADPH
(-)-epigallocatechin + NAD(P)+
show the reaction diagram
-
changes in the concentration of products and coenzyme in the ANR assay are determined by thin layer chromatography (TLC), HPLC, mass spectrometry (MS) and UV spectrophotometry
-
-
?
delphinidin + NADPH
(-)-epigallocatechin + NADP+
show the reaction diagram
-
-
-
-
?
delphinidin + NADPH + H+
epigallocatechin + NADP+
show the reaction diagram
Q5FB34
-
-
-
?
NADPH + H+ + cyanidin
NADP+ + (-)-epicatechin
show the reaction diagram
-
-
-
-
?
NADPH + H+ + delphinidin
NADP+ + (-)-epigallocatechin
show the reaction diagram
-
-
-
-
?
NADPH + H+ + delphinidin
NADP+ + (-)-epigallocatechin
show the reaction diagram
A4PB65
-
-
-
?
NADPH + H+ + pelargonidin
NADP+ + (-)-epiafzelechin
show the reaction diagram
-
-
-
-
?
NADPH + H+ + petunidin
NADP+ + ?
show the reaction diagram
-
-
-
-
?
pelargonidin + 2 NADPH + H+
(-)-epiafzelechin + 2 NADP+
show the reaction diagram
-
-
-
-
?
pelargonidin + 2 NADPH + H+
(-)-epiafzelechin + 2 NADP+
show the reaction diagram
-
preference of anthocyanidin substrates in decreasing order: cyanidin, pelargonidin and delphinidin
-
-
?
pelargonidin + 2 NADPH + H+
(-)-epiafzelechin + 2 NADP+
show the reaction diagram
-
24% activity compared to cyanidin
-
-
?
pelargonidin + NAD(P)H + H+
epiafzelechin + NAD(P)+
show the reaction diagram
-
-
-
-
?
pelargonidin + NADPH + H+
afzelechin + NADP+
show the reaction diagram
Q5FB34
-
-
-
?
pelargonidin + NADPH + H+
epiafzelechin + NADP+
show the reaction diagram
-
-
-
-
?
pelargonidin + NADPH + H+
epiafzelechin + NADP+
show the reaction diagram
Q5FB34
-
-
-
?
delphinidin + NADPH + H+
gallocatechin + NADP+
show the reaction diagram
Q5FB34
-
-
-
?
additional information
?
-
-
no activity with paeonidin and malvidin
-
-
-
additional information
?
-
Vitis vinifera, Vitis vinifera Cabernet Sauvignon
-
the enzyme shows regiospecific hydride transfers, and epimerase activity but only with 2R-flavan-3-ols, not with 2S-flavan-3-ols produced by the enzyme in the forward reaction. C3-epimerization is achieved by tautomerization between the two hydride transfers, which produces a quinone methide intermediate which serves as C4 target of the second hydride transfer, thereby avoiding any stereospecific modification of C3. The inversion of C2 stereochemistry required for reverse epimerization suggests that the 2S configuration induces an irreversible product dissociation
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(+)-epicatechin + 2 NADP+
cyanidin + 2 NADPH + 2 H+
show the reaction diagram
Vitis vinifera, Vitis vinifera Cabernet Sauvignon
-
-
-
-
r
(-)-catechin + 2 NADP+
cyanidin + 2 NADPH + 2 H+
show the reaction diagram
Vitis vinifera, Vitis vinifera Cabernet Sauvignon
-
-
-
-
r
(2S,3R)-flavan-3-ol + 2 NADP+
an anthocyanidin + 2 NADPH + H+
show the reaction diagram
-
Vitis vinifera anthocyanidin reductase, ANR, catalyzes an NADPH-dependent double reduction of anthocyanidins producing a mixture of (2S,3R)- and (2S,3S)-flavan-3-ols, product identification, overview. At pH 7.5 and 30C, the first hydride transfer to anthocyanidin is irreversible, and no intermediate is released during catalysis. ANR reverse activity is assessed in the presence of excess NADP+
-
-
r
(2S,3S)-flavan-3-ol + 2 NADP+
an anthocyanidin + 2 NADPH + H+
show the reaction diagram
-
Vitis vinifera anthocyanidin reductase, ANR, catalyzes an NADPH-dependent double reduction of anthocyanidins producing a mixture of (2S,3R)- and (2S,3S)-flavan-3-ols, product identification, overview. At pH 7.5 and 30C, the first hydride transfer to anthocyanidin is irreversible, and no intermediate is released during catalysis. ANR reverse activity is assessed in the presence of excess NADP+
-
-
r
2,3-cis-flavan-3-ol + NAD(P)+
anthocyanidin + NAD(P)H + H+
show the reaction diagram
Q84XT1
the enzyme is involved in formation of condensed tannins. The enzyme competes with anthocyanidin synthase, for the pool of flavan-3,4-diol
-
-
?
anthocyanidin + NAD(P)H
2,3-cis-flavan-3-ol + NAD(P)+
show the reaction diagram
-
enzyme of flavonoid pathway involved in the biosynthesis of condensed tannins
-
-
?
cyanidin + NADPH + H+
(2S,3R)-3',4',5,7-tetrahydroxyflavan-3-ol + NADP+
show the reaction diagram
-
enzyme produces a 50:50 mixture of (2S,3S)-flavan-3-ol and (2S,3R)-flavan-3-ol, i.e. (+)-epicatechin and (-)-catechin
-
-
?
cyanidin + NADPH + H+
(2S,3S)-3',4',5,7-tetrahydroxyflavan-3-ol + NADP+
show the reaction diagram
-
enzyme produces a 50:50 mixture of (2S,3S)-flavan-3-ol and (2S,3R)-flavan-3-ol, i.e. (+)-epicatechin and (-)-catechin
-
-
?
cyanidin + NADPH + H+
(+)-epicatechin + NADP+
show the reaction diagram
Q5FB34
enzyme produces a 50:50 mixture of 2S,3S-flavan-3-ol and 2S,3R-flavan-3-ol, i.e. (+)-epicatechin and (-)-catechin
-
-
?
cyanidin + NADPH + H+
(-)-catechin + NADP+
show the reaction diagram
Q5FB34
enzyme produces a 50:50 mixture of 2S,3S-flavan-3-ol and 2S,3R-flavan-3-ol, i.e. (+)-epicatechin and (-)-catechin
-
-
?
cyanidin + NADPH + H+
epicatechin + NADP+
show the reaction diagram
-, Q6DV46
-
-
-
?
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
NAD(P)H
A2IBG2, -
-
NAD(P)H
Q5FB34
-
NAD(P)H
A4PB65
-
NAD(P)H
-
-
NADH
-
slight preference for NADPH over NADH
NADPH
-
slight preference for NADPH over NADH
NADPH
A1XEG2, A1XEG3, A1XEG4, A1XEG5, A1XEG6, A1XEG7, A1XEG8, -
-
NADPH
-
dependent on, ANR from Vitis vinifera exclusively uses pro(S) hydrogen from NADPH
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
(+)-catechin
-
0.5 mM, 50% inhibition
(+/-)-dihydroquercetin
-
0.025 mM
Na+
-
above 200 mM
abscisic acid
-
decreases ANR activity and represses the expression a few days after application
additional information
-
no inhibition by Na+ up to 400 mM
-
additional information
-
no inhibition by (+)-catechin and (+/-)-dihydroquercetin
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.00282
-
cyanidin
-
-
0.0129
-
cyanidin
-
pH 6.0
0.0131
-
cyanidin
-
pH 6.5, temperature not specified in the publication
0.0267
-
cyanidin
-
pH 6.5, temperature not specified in the publication
0.0739
-
cyanidin
-
pH 8.0
0.0142
-
delphinidin
-
pH 6.5, temperature not specified in the publication
0.0178
-
delphinidin
-
pH 8.0
0.0244
-
delphinidin
-
pH 6.5, temperature not specified in the publication
0.0498
-
delphinidin
-
pH 6.0
0.94
-
NADH
-
pH 6.0
0.097
-
NADPH
-
co-substrate: cyanidin, pH 6.5, temperature not specified in the publication
0.219
-
NADPH
-
co-substrate: cyanidin, pH 6.5, temperature not specified in the publication
0.45
-
NADPH
-
pH 6.0
0.013
-
pelargonidin
-
pH 6.5, temperature not specified in the publication
0.0145
-
pelargonidin
-
pH 6.0
0.0201
-
pelargonidin
-
pH 6.5, temperature not specified in the publication
0.0528
-
pelargonidin
-
pH 8.0
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0012
-
cyanidin
-
pH 6.5, temperature not specified in the publication
0.0028
-
cyanidin
-
pH 6.5, temperature not specified in the publication
0.18
-
cyanidin
-
pH 6.0
1.045
-
cyanidin
-
pH 8.0
0.0012
-
delphinidin
-
pH 6.5, temperature not specified in the publication
0.0026
-
delphinidin
-
pH 6.5, temperature not specified in the publication
0.058
-
delphinidin
-
pH 8.0
1.34
-
delphinidin
-
pH 6.0
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.111
-
NADPH
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.5
-
-
in 50 mM citrate/phosphate buffer
6
-
-
in 50 mM MES buffer
6
-
-
activity assay
6.5
-
-
assay at
6.5
-
-
assay at
7
-
-
activity assay
7
-
-
studies of binding at equilibrium
7.5
-
-
kinetic studies
7.5
-
-
assay at, forward and reverse directions of the reaction
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7
8.9
-
pH 7.0: about 40% of maximal activity, pH 8.9: about 90% of maximal activity
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
-
-
studies of binding at equilibrium
30
-
-
activity assay
30
-
-
kinetic studies
30
-
-
assay at, forward and reverse directions of the reaction
35
-
-
activity assay
35
-
-
assay at
45
-
-
assay at
45
-
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
Q7PCC4
VvANR is expressed throughout early flower and berry development, with expression increasing after fertilization. Expression in berry skin and seeds until the onset of the ripening
Manually annotated by BRENDA team
Q7PCC4
VvANR is expressed throughout early flower and berry development, with expression increasing after fertilization
Manually annotated by BRENDA team
Q84XT1
very weak
Manually annotated by BRENDA team
-
leaves of transgenic Medicago truncatula constitutively expressing MtANR contain up to three times more proanthocyanidins than those of wild-type plants at the same stage of development
Manually annotated by BRENDA team
Q7PCC4
expression in expanding leaves
Manually annotated by BRENDA team
A1XEG2, A1XEG3, A1XEG4, A1XEG5, A1XEG6, A1XEG7, A1XEG8, -
-
Manually annotated by BRENDA team
-, D0QXI9, D0QXJ0, D0QXJ1, D0QXJ2
-
Manually annotated by BRENDA team
-, D0QXJ3 AND D0QXJ4, D0QXJ3
;
Manually annotated by BRENDA team
-
preferentially expressed in roots
Manually annotated by BRENDA team
Q84XT1
strong expression
Manually annotated by BRENDA team
-, D0QXI9, D0QXJ0, D0QXJ1, D0QXJ2
-
Manually annotated by BRENDA team
-, D0QXJ3 AND D0QXJ4, D0QXJ3
;
Manually annotated by BRENDA team
Arabidopsis thaliana Wassilevskija-2 ecotype, Brassica napus Westar
-
-
-
Manually annotated by BRENDA team
-
preferrently expressed
Manually annotated by BRENDA team
Arabidopsis thaliana Wassilevskija-2 ecotype, Brassica napus Westar
-
-
-
Manually annotated by BRENDA team
additional information
-
in Medicago truncatula expression of MtANR driven by the 35S promoter results in a decrease of approximately 50% in anthocyanin pigmentation in the red spot compared with that of wild-type plants at the same stage of development
Manually annotated by BRENDA team
additional information
-
ANR2 shows minor expression in all organs
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
36850
-
-
determined by SDS-PAGE and by MALDI mass spectrometry; theoretical mass without the initiator methionine
37000
-
-
calculated from cDNA
39000
-
-
SDS-PAGE, recombinant protein
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
the structure of anthocyanidin reductase is described at a resolution of 2.2 A
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
extraction from plants, using a Sephadex G-25 column
-
recombinant His6-tag fused GB1-ANR construct from Escherichia coli, Tev-mediated removal of the GB1 domain including the hexahistidine tag at its N-terminal end, and purification of Vv-ANR to homogeneity
-
using a HiTrap Chelated HP column, the His-tag and GB1 domain are removed by digestion with TEV protease
-
using a HiTrap Chelated HP column, the His-tag is removed by digestion with TEV protease, the cleaved fraction is loaded on a gel filtration column
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression in Escherichia coli as a fusion protein with maltose-binding protein
-
gene BAN, DNA and amino acid sequence determination and analysis, sequence comparisons and genetic mapping, phylogenetic tree, overview
Q9SEV0
genetic transformation of Arabidopsis thaliana with the Arabidopsis TT2 MYB transcription factor results in ectopic expression of the BANYULS gene, encoding anthocyanidin reductase, AHA10 encoding a P-type proton-pump and TT12 encoding a transporter involved in proanthocyanidin biosynthesis. When coupled with constitutive expression of PAP1, a positive regulator of anthocyanin biosynthesis, TT2 expression in Arabidopsis leads to the accumulation of proanthocyanidins, but only in a subset of cells in which the BANYULS promoter is naturally expressed. Ectopic expression of the maize Lc MYC transcription factor weakly induces AHA10 but does not induce BANYULS, TT12 or accumulation of proanthocyanidins
-
gene BAN, DNA and amino acid sequence determination and analysis, sequence comparisons and genetic mapping, phylogenetic tree, overview; gene BAN, DNA and amino acid sequence determination and analysis, sequence comparisons and genetic mapping, phylogenetic tree, overview; gene BAN, DNA and amino acid sequence determination and analysis, sequence comparisons and genetic mapping, phylogenetic tree, overview; gene BAN, DNA and amino acid sequence determination and analysis, sequence comparisons and genetic mapping, phylogenetic tree, overview
-, D0QXI9, D0QXJ0, D0QXJ1, D0QXJ2
gene BAN, DNA and amino acid sequence determination and analysis, sequence comparisons and genetic mapping, phylogenetic tree, overview; gene BAN, DNA and amino acid sequence determination and analysis, sequence comparisons and genetic mapping, phylogenetic tree, overview
-, D0QXJ3 AND D0QXJ4, D0QXJ3
gene BAN, DNA and amino acid sequence determination and analysis, sequence comparisons and genetic mapping, phylogenetic tree, overview
-, D0QXJ5
gene BAN, DNA and amino acid sequence determination and analysis, sequence comparisons and genetic mapping, phylogenetic tree, overview
D0QXJ6
expressed in Escherichia coli; expressed in Escherichia coli. Overexpressed in Nicotiana tabacum and Medicago truncatula for functional analysis
-
for expression in Escherichia coli cells
Q6DV46
expressed in Escherichia coli strain BL21
-
recombinantly expressed in Escherichia coli
-
expressed in Escherichia coli; expressed in Escherichia coli; expressed in Escherichia coli; expressed in Escherichia coli; expressed in Escherichia coli; expressed in Escherichia coli; expressed in Escherichia coli
A1XEG2, A1XEG3, A1XEG4, A1XEG5, A1XEG6, A1XEG7, A1XEG8, -
constitutive expression of the enzyme under control of the cauliflower mosaic virus 35S promoter in Nicotiana tabacum and Arabidopsis. Tobacco lines expressing the enzyme from Medicago trunculata lose the pink flower pigmentation characteristics of wild-type and empty vector control plants
Q84XT1
expression in Escherichia coli as a fusion protein with maltose-binding protein
-
expressed in Escherichia coli. To investigate the function of PtrANR1, the open reading frame in sense or antisense orientation is introduced into Populus tomentosa Carr. plants for ectopic expression under the control of the cauliflower mosaic virus 35S promoter, respectively
-
into the vector pGEM-T and subsequently into pETGB_1a for expression in Escherichia coli BL21DE3 cells
Q5FB34
production of a His6-tag fused GB1-ANR construct, expression of His6-tagged fused protein GB1-ANR in Escherichia coli
-
the full-length VvANR cDNA is cloned into the vector pART7 and transformed into tobacco via the pART27 vector under the control of the CaMV 35S promoter
Q7PCC4
expressed in Malus domestica via Agrobacterium tumefaciens-mediated transformation
-
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression of anthocyanidin reductase is down-regulated in response to drought, abscisic acid and gibberellic acid
Q6DV46
expression of anthocyanidin reductase is up-regulated in response to wounding
Q6DV46
gene expression and enzymatic activity are higher in the developping leaves than in the mature leaves and lower than in the tender bud and first leaves
-
abscisic acid decreases ANR activity and represses the expression a few days after application
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
N185I/G214A
-
mutant shows minor reductions in activity. Calculated Km and Vmax values are not given as the enzymes are intensely inhibited by cyanidin concentrations above 0.1 mM
V122A/G214A
-
mutant shows minor reductions in activity. Calculated Km and Vmax values are not given as the enzymes are intensely inhibited by cyanidin concentrations above 0.1 mM
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
molecular biology
-
a method for the analysis of ANR activity using the detection of coenzyme is established