Information on EC 1.3.1.77 - anthocyanidin reductase [(2R,3R)-flavan-3-ol-forming]

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.3.1.77
-
RECOMMENDED NAME
GeneOntology No.
anthocyanidin reductase [(2R,3R)-flavan-3-ol-forming]
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
a (2R,3R)-flavan-3-ol + 2 NAD(P)+ = an anthocyanidin with a 3-hydroxy group + 2 NAD(P)H + H+
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
redox reaction
-
-
reduction
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
2,3-cis-flavanols biosynthesis
-
-
proanthocyanidins biosynthesis from flavanols
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-
Flavonoid biosynthesis
-
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Biosynthesis of secondary metabolites
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-
SYSTEMATIC NAME
IUBMB Comments
(2R,3R)-flavan-3-ol:NAD(P)+ 3,4-oxidoreductase
The enzyme participates in the flavonoid biosynthesis pathway found in plants. It catalyses the double reduction of anthocyanidins, producing (2R,3R)-flavan-3-ol monomers required for the formation of proanthocyanidins. While the enzyme from the legume Medicago truncatula (MtANR) can use 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. cf. EC 1.3.1.112, anthocyanidin reductase [(2S)-flavan-3-ol-forming].
CAS REGISTRY NUMBER
COMMENTARY hide
93389-48-1
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene BANYULS orthologue, BAN
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
gene BANYULS orthologue, four copies of BAN, two originating from each diploid progenitor
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
gene BANYULS orthologue, BAN
D0QXJ3, D0QXJ3, D0QXJ4
UniProt
Manually annotated by BRENDA team
gene BANYULS orthologue, BAN
UniProt
Manually annotated by BRENDA team
gene BANYULS orthologue, BAN
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
cultivar Hiratanenashi
UniProt
Manually annotated by BRENDA team
cvs. Sachiizumi, Harunoibuki, 2SL05-1, Asahimurazairai, and Asahimurazairai/Kyushu PL4, from Japan
UniProt
Manually annotated by BRENDA team
cvs. Hokkai T8 and Hokkai T10
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
var. nana, Aihuahong
-
-
Manually annotated by BRENDA team
var. nana, Aihuahong
-
-
Manually annotated by BRENDA team
Xiongyuehaitang
-
-
Manually annotated by BRENDA team
Xijinhaitang
-
-
Manually annotated by BRENDA team
Medicago truncatula ecotype R108
-
SwissProt
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
cv. Feng Hua
A0A0C5DIU7
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(+)-epicatechin + 2 NADP+
cyanidin + 2 NADPH + 2 H+
show the reaction diagram
-
-
-
-
?
2 cyanidin + 4 NADPH + H+
(-)-catechin + (-)-epicatechin + 4 NADP+
show the reaction diagram
-
?
-
-
2 delphinidin + 4 NADPH + H+
(-)-gallocatechin and (-)-epigallocatechin + 4 NADP+
show the reaction diagram
-
?
-
-
2 pelargonidin + 4 NADPH + H+
(-)-afzelechin and (-)-epiafzelechin + 4 NADP+
show the reaction diagram
-
?
-
-
2,3-cis-flavan-3-ol + NAD(P)+
anthocyanidin + NAD(P)H + H+
show the reaction diagram
the enzyme is involved in formation of condensed tannins. The enzyme competes with anthocyanidin synthase, for the pool of flavan-3,4-diol
-
-
?
a (2R,3R)-flavan-3-ol + 2 NAD(P)+
an anthocyanidin with a 3-hydroxy group + 2 NAD(P)H + H+
show the reaction diagram
-
-
-
?
anthocyanidin + 2 NADPH + H+
2,3-trans-(2S,3R)-flavan-3-ol + 2 NADP+
show the reaction diagram
-
-
?
-
-
anthocyanidin + 2 NADPH + H+
epicatechin + 2 NAD(P)+
show the reaction diagram
A0A0C5DIU7;
-
?
-
-
anthocyanidin + 2 NADPH + H+
epicatechin + 2 NADP+
show the reaction diagram
anthocyanidin + NAD(P)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
cyanidin + 2 NADH + H+
(2R,3R)-epicatechin + 2 NAD+
show the reaction diagram
-
-
?
-
-
cyanidin + 2 NADPH + 2 H+
(-)-catechin + (-)-epicatechin + 2 NADP+
show the reaction diagram
-
-
-
?
cyanidin + 2 NADPH + 2 H+
epicatechin + 2 NADP+
show the reaction diagram
-
-
-
-
?
cyanidin + 2 NADPH + H+
(2R,3R)-epicatechin + 2 NADP+
show the reaction diagram
cyanidin + NAD(P)H + H+
(-)-epicatechin + NAD(P)+
show the reaction diagram
cyanidin + NADPH
(-)-epicatechin + NAD(P)+
show the reaction diagram
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
-
-
-
?
delphinidin + 2 NADH + 2 H+
(-)-epigallocatechin + (-)-gallocatechin + 2 NAD+
show the reaction diagram
-
-
-
?
delphinidin + 2 NADH + H+
(2R,3R)-epigallocatechin + 2 NAD+
show the reaction diagram
-
-
?
-
-
delphinidin + 2 NADPH + 2 H+
epigallocatechin + 2 NADP+
show the reaction diagram
-
-
-
-
?
delphinidin + 2 NADPH + H+
(-)-epigallocatechin + 2 NADP+
show the reaction diagram
delphinidin + 2 NADPH + H+
(2R,3R)-epigallocatechin + 2 NADP+
show the reaction diagram
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
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-
?
delphinidin + NADPH
(-)-epigallocatechin + NADP+
show the reaction diagram
-
-
-
-
?
NADPH + H+ + cyanidin
NADP+ + (-)-epicatechin
show the reaction diagram
-
-
-
-
?
NADPH + H+ + delphinidin
NADP+ + (-)-epigallocatechin
show the reaction diagram
NADPH + H+ + pelargonidin
NADP+ + (-)-epiafzelechin
show the reaction diagram
-
-
-
-
?
NADPH + H+ + petunidin
NADP+ + ?
show the reaction diagram
-
-
-
-
?
pelargonidin + 2 NADH + H+
(2R,3R)-epiafzelechin + 2 NAD+
show the reaction diagram
-
-
?
-
-
pelargonidin + 2 NADPH + 2 H+
(-)-epiafzelechin + (-)-afzelechin + 2 NADP+
show the reaction diagram
-
-
-
?
pelargonidin + 2 NADPH + 2 H+
epiafzelechin + 2 NADP+
show the reaction diagram
-
-
-
-
?
pelargonidin + 2 NADPH + H+
(-)-epiafzelechin + 2 NADP+
show the reaction diagram
pelargonidin + 2 NADPH + H+
(2R,3R)-epiafzelechin + 2 NADP+
show the reaction diagram
pelargonidin + NAD(P)H + H+
epiafzelechin + NAD(P)+
show the reaction diagram
-
-
-
-
?
pelargonidin + NADPH + H+
epiafzelechin + NADP+
show the reaction diagram
-
-
-
-
?
petunidin + 2 NADPH + 2 H+
? + 2 NADP+
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2 cyanidin + 4 NADPH + H+
(-)-catechin + (-)-epicatechin + 4 NADP+
show the reaction diagram
A2IBG2
-
?
-
-
2 delphinidin + 4 NADPH + H+
(-)-gallocatechin and (-)-epigallocatechin + 4 NADP+
show the reaction diagram
A2IBG2
-
?
-
-
2 pelargonidin + 4 NADPH + H+
(-)-afzelechin and (-)-epiafzelechin + 4 NADP+
show the reaction diagram
A2IBG2
-
?
-
-
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
-
-
?
a (2R,3R)-flavan-3-ol + 2 NAD(P)+
an anthocyanidin with a 3-hydroxy group + 2 NAD(P)H + H+
show the reaction diagram
F8V3W3, H9LBK6
-
-
-
?
anthocyanidin + 2 NADPH + H+
epicatechin + 2 NAD(P)+
show the reaction diagram
A0A0C5DIU7
-
?
-
-
anthocyanidin + 2 NADPH + H+
epicatechin + 2 NADP+
show the reaction diagram
anthocyanidin + NAD(P)H
2,3-cis-flavan-3-ol + NAD(P)+
show the reaction diagram
cyanidin + 2 NADPH + H+
(2R,3R)-epicatechin + 2 NADP+
show the reaction diagram
cyanidin + NADPH + H+
epicatechin + NADP+
show the reaction diagram
Q6DV46
-
-
-
?
delphinidin + 2 NADPH + H+
(2R,3R)-epigallocatechin + 2 NADP+
show the reaction diagram
pelargonidin + 2 NADPH + H+
(2R,3R)-epiafzelechin + 2 NADP+
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAD(P)H
additional information
-
enzyme VbANR uses both NADPH and NADH but prefers to employ NADPH
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(+)-catechin
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0.5 mM, 50% inhibition
(+/-)-dihydroquercetin
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0.025 mM
Na+
-
above 200 mM
NaCl
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purified recombinant VbANR almost loses its catalytic activity at 500 mM
quercetin
sodium chloride
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500 mm, almost complete loss of activity
additional information
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0129 - 0.176
cyanidin
0.0142 - 0.131
delphinidin
0.8169 - 0.94
NADH
0.097 - 0.45
NADPH
0.013 - 0.135
pelargonidin
additional information
additional information
-
kinetics of Trx-VbANR with NADPH and NADH, overview
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0012 - 1.665
cyanidin
0.0012 - 2.012
delphinidin
2
pelargonidin
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
9.48
cyanidin
15.38 - 16.4
delphinidin
14.87 - 14.9
pelargonidin
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5
-
in 50 mM citrate/phosphate buffer
6
-
in 50 mM MES buffer
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3 - 8
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activity range, profile overview
7 - 8.9
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pH 7.0: about 40% of maximal activity, pH 8.9: about 90% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 50
-
activity profile, overview
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.42
sequence calculation
6.54
sequence calculation
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
grown under light or dark condition
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37000
-
calculated from cDNA
39000
-
SDS-PAGE, recombinant protein
56000
-
x * 56000, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
three-dimensional structure modeling and analysis, overview
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant His-Trx-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
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expressed in Escherichia coli strain BL21
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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
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expressed in Escherichia coli; expressed in Escherichia coli. Overexpressed in Nicotiana tabacum and Medicago truncatula for functional analysis
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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;
expressed in Malus domestica via Agrobacterium tumefaciens-mediated transformation
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expression in Escherichia coli
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expression in Escherichia coli as a fusion protein with maltose-binding protein
expression in Saccharomyces cerevisiae
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for expression in Escherichia coli cells
gene ANR, cloned from dormant bud-specific complementary DNA (cDNA) library, DNA and amino acid sequence analysis, sequence comparisons and phylogenetic analysis, semiquantitative RT-PCR expression analysis
gene anr, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, cloned from two cultivars, Hokkai T8 and T10, quantitative real-time RT-PCR enzyme expression analysis
gene ANR, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, recombinant expression of His-Trx-tagged enzyme in Escherichia coli strain BL21(DE3), recombinant expression of GFP-tagged enzyme in Arabidopsis thaliana ban mutant
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gene ANR1, co-overexpression with leucoanthocyanidin reductase (LAR) in Nicotiana tabacum cv. Xanthi by Agrobacterium tumefaciens-mediated transformation, semiquantitative expression analysis; gene ANR2, co-overexpression with leucoanthocyanidin reductase (LAR) in Nicotiana tabacum cv. Xanthi by Agrobacterium tumefaciens-mediated transformation, semiquantitative expression analysis
gene ANR1, quantitative real-time PCR enzyme expression analysis; gene ANR2, quantitative real-time PCR enzyme expression analysis
gene ANRa, cloned from leaves, recombinant expression of His-tagged ANRa, recombinant overexpression in Nicotiana tabacum leaves leading to the formation of proanthocyanidins in flowers and the reduction of anthocyanins
gene ANRb, cloned from leaves, recombinant expression of His-tagged ANRa, recombinant overexpression in Nicotiana tabacum leaves leading to the formation of proanthocyanidins in flowers and the reduction of anthocyanins
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
D0QXJ3; D0QXJ4;, D0QXJ3;
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
gene BAN, overexpression of the enzyme in Medicago truncatula hairy roots. Recombinant enzyme ANR does not generate epicatechin from epicatechin-cysteine conjugate in hairy roots
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gene BpANR, sequence comparisons, quantitative RT-PCR expression analysis
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gene FeANR, cloned from leaves, DNA and amino acid sequence determination and analysis, phylogenetic analysis
gene GhANR1, cloned from developing fibers, DNA and amino acid sequence determination and analysis, ectopic expression of GhANR11 in the Arabidopsis thaliana ban mutant, via transformation by Agrobacterium tumefaciens strain EHA 105, allows for the reconstruction of the ANR pathway and proanthocyanidin biosynthesis in the seed coat, recombinant expression of His-Trx-tagged enzyme in Escherichia coli strain BL21(DE3)
genes ANR1 and ANR2, quantitative real-time PCR enzyme expression analysis
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
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overexpression of gene ANR under control of the CaMV35S promoter via Agrobacterium tumefaciens strain EHA105 transformation, real-time quantitative PCR expression analysis, a number of genes encoding stress-responsivefunctional proteins are upregulated in the RrANR-overexpressing tobacco lines, phenotype, detailed overview. Rosa rugosa anthocyanidin reductase overexpression in Nicotiana tabacum enhances tobacco tolerance to abiotic stress through increased reactive oxygen species scavenging and modulation of abscisic acid signaling
A0A0C5DIU7;
recombinantly expressed in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
abscisic acid decreases ANR activity and represses the expression a few days after application
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expression of anthocyanidin reductase is down-regulated in response to drought, abscisic acid and gibberellic acid
expression of anthocyanidin reductase is up-regulated in response to wounding
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
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overexpression of the myeloblastosis (MYB)14 or MYB5 transcription factors induces proanthocyanidin biosynthesis in hairy roots, ANR is highly induced in MYB5 overexpressing hairy roots
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
N185I/G214A
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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
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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
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
molecular biology
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a method for the analysis of ANR activity using the detection of coenzyme is established