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Information on EC 1.3.1.112 - anthocyanidin reductase [(2S)-flavan-3-ol-forming] and Organism(s) Vitis vinifera and UniProt Accession Q5FB34
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1.3.1.112 anthocyanidin reductase [(2S)-flavan-3-ol-forming]IUBMB Comments
The enzyme, characterized from Vitis vinifera (grape), participates in the flavonoid biosynthesis pathway. It catalyses the double reduction of anthocyanidins, producing a mixture of (2S,3S)- and (2S,3R)-flavan-3-ols. The enzyme catalyses sequential hydride transfers to C-2 and C-4, respectively. Epimerization at C-3 is achieved by tautomerization that occurs between the two hydride transfers. cf. EC 1.3.1.77, anthocyanidin reductase [(2R,3R)-flavan-3-ol-forming].
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The taxonomic range for the selected organisms is: Vitis vinifera
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
ANR, anthocyanidin reductase ((2S)-flavan-3-ol-forming), 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
SYSTEMATIC NAME
IUBMB Comments
(2S)-flavan-3-ol:NAD(P)+ oxidoreductase
The enzyme, characterized from Vitis vinifera (grape), participates in the flavonoid biosynthesis pathway. It catalyses the double reduction of anthocyanidins, producing a mixture of (2S,3S)- and (2S,3R)-flavan-3-ols. The enzyme catalyses sequential hydride transfers to C-2 and C-4, respectively. Epimerization at C-3 is achieved by tautomerization that occurs between the two hydride transfers. cf. EC 1.3.1.77, anthocyanidin reductase [(2R,3R)-flavan-3-ol-forming].
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2 delphinidin + 4 NADPH + 4 H+
(-)-gallocatechin + (+)-epigallocatechin + 4 NADP+
-
-
-
ir
2 pelargonidin + 4 NADPH + 4 H+
(-)-afzelechin + (+)-epiafzelechin + 4 NADP+
-
-
-
ir
peonidin + 2 NADPH + 2 H+
(2S,3S)-3,5,7-trihydroxy-2-(4-hydroxy-3-methoxyphenyl)-2,3-dihydro-1-benzopyran-1-ium + 2 NADP+
-
-
-
?
2 cyanidin + 4 NADPH + 4 H+
(+)-epicatechin + (-)-catechin + 4 NADP+
-
-
-
?
2 cyanidin + 4 NADPH + 4 H+
(+)-epicatechin + (-)-catechin + 4 NADP+
-
at pH 7.5 and 30°C, the first hydride transfer to anthocyanidin is irreversible, and no intermediate is released during catalysis
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ir
2 cyanidin + 4 NADPH + 4 H+
(+)-epicatechin + (-)-catechin + 4 NADP+
-
the relative concentration of catechin versus epicatechin remains nearly constant and is close to 1
-
?
additional information
?
-
ANR is strictly pro-S stereospecific and the reaction mechanism involves two hydride transfers from two distinct NADPH molecules. ANR produces a 50:50 mixture of 2,3-cis and 2,3-trans flavan-3-ols, i.e. 2S,3S- and 2S,3R-flavan-3-ols
-
-
?
additional information
?
-
hyperbolic and rapid-equilibrium ordered mechanism, with NADPH binding first. The most likely mechanism is sequential ordered Bi Uni Uni Bi, with NADPH binding first and NADP+ released last, and internal conversion of the first ternary complex, i.e. that associated with the first hydride transfer, is rate-limiting
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-
?
additional information
?
-
in the presence of excess NADP+, ANR acts as a flavan-3-ol C3-epimerase, but only with 2R-flavan-3-ols, not with 2S-flavan-3-ols produced by the enzyme in the forward reaction. C3-epimerization should be achieved by tautomerization between the two hydride transfers and this produces a quinone methide intermediate which serves as C4 target of the second hydride transfer, avoiding any stereospecific modification of carbon 3. The inversion of C2 stereochemistry required for reverse epimerization suggests that the 2S configuration induces an irreversible product dissociation
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADP+
hyperbolic binding of NADPH and NADP+ to the free enzyme, with a single binding site each and with dissociation constants of 0.046 mM for NADPH and 0.083 for NADP+
NADPH
hyperbolic binding of NADPH and NADP+ to the free enzyme, with a single binding site each and with dissociation constants of 0.046 mM for NADPH and 0.083 for NADP+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
mRNA accumulates at the early stage of berry development and decreases toward the ripening stage. Proanthocyanidins accumulate in the berry skins and seeds before veraison, especially during the early stages of development
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grape flowers have high levels of proanthocyanidins. ANR is expressed throughout early flower and berry development
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grape flowers have high levels of proanthocyanidins, and accumulation continues in skin and seeds from fruit set until the onset of ripening. ANR is expressed throughout early flower and berry development, with expression increasing after fertilization. During grape ripening, proanthocyanidin levels decrease in both skin and seeds, and expression of genes encoding ANR and LAR are no longer detected
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a high amount of leucoanthocyanidin reductases LAR1 and LAR2 and of ANR is present at the pre-veraison stage, localized on the outer layer of the berry skin, the vascular bundle and the inner layer of the seed coat
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grape flowers have high levels of proanthocyanidins, and accumulation continues in skin and seeds from fruit set until the onset of ripening. ANR is expressed throughout early flower and berry development, with expression increasing after fertilization. During grape ripening, proanthocyanidin levels decrease in both skin and seeds, and expression of genes encoding ANR and LAR are no longer detected
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). ANRCS_VITVI
338
0
36763
Swiss-Prot
Secretory Pathway (Reliability: 4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
to 2.2 A resolution. The active site is wide open with the side chains of the catalytic residues Tyr168 and Lys172 turned away from the nucleotide-binding site
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
trreatment with abscisic acid affects tannin content and is involved in the tannin biosynthesis pathway in grape skin by decreasing leucoanthocyanidin reductase and ANR activity and repressing the expression of related genes a few days after application
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bogs, J.; Downey, M.O.; Harvey, J.S.; Ashton, A.R.; Tanner, G.J.; Robinson, S.P.
Proanthocyanidin synthesis and expression of genes encoding leucoanthocyanidin reductase and anthocyanidin reductase in developing grape berries and grapevine leaves
Plant Physiol.
139
652-663
2005
Vitis vinifera
Pfeiffer, J.; Kuehnel, C.; Brandt, J.; Duy, D.; Punyasiri, P.A.; Forkmann, G.; Fischer, T.C.
Biosynthesis of flavan 3-ols by leucoanthocyanidin 4-reductases and anthocyanidin reductases in leaves of grape (Vitis vinifera L.), apple (Malus x domestica Borkh.) and other crops
Plant Physiol. Biochem.
44
323-334
2006
Vitis vinifera (Q7PCC4)
Gargouri, M.; Manigand, C.; Mauge, C.; Granier, T.; Langlois dEstaintot, B.; Cala, O.; Pianet, I.; Bathany, K.; Chaudiere, J.; Gallois, B.
Structure and epimerase activity of anthocyanidin reductase from Vitis vinifera
Acta Crystallogr. Sect. D
65
989-1000
2009
Vitis vinifera (Q5FB34)
Gargouri, M.; Gallois, B.; Chaudiere, J.
Binding-equilibrium and kinetic studies of anthocyanidin reductase from Vitis vinifera
Arch. Biochem. Biophys.
491
61-68
2009
Vitis vinifera (Q5FB34)
Gargouri, M.; Chaudiere, J.; Manigand, C.; Mauge, C.; Bathany, K.; Schmitter, J.M.; Gallois, B.
The epimerase activity of anthocyanidin reductase from Vitis vinifera and its regiospecific hydride transfers
Biol. Chem.
391
219-227
2010
Vitis vinifera (Q5FB34)
Lacampagne, S.; Gagne, S.; Geny, L.
Involvement of abscisic acid in controlling the proanthocyanidin biosynthesis pathway in grape skin: new elements regarding the regulation of tannin composition and leucoanthocyanidin reductase (LAR) and anthocyanidin reductase (ANR) activities and expres
J. Plant Growth Regul.
29
81-90
2010
Vitis vinifera (Q5FB34)
-
Fujita, A.; Soma, N.; Goto-Yamamoto, N.; Shindo, H.; Kakuta, T.; Koizumi, T.; Hashizume, K.
Anthocyanidin reductase gene expression and accumulation of flavan-3-ols in grape berry
Am. J. Enol. Vitic.
56
336-342
2005
Vitis vinifera (Q5FB34)
He, F.; Fang, X.; Hu, M.; Pan, Q.; Shi, Y.; Duan, C.
Preparation and biological application of antibodies against leucoanthocyanidin reductase and anthocyanidin reductase from grape berry
Vitis
48
69-75
2009
Vitis vinifera
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