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Literature summary extracted from

  • 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 (2009), Acta Crystallogr. Sect. D, 65, 989-1000.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.3.1.112 expression in Escherichia coli Vitis vinifera

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.3.1.112 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 Vitis vinifera

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.3.1.112 sodium chloride complete inhibition above 200 mM Vitis vinifera

Organism

EC Number Organism UniProt Comment Textmining
1.3.1.112 Vitis vinifera Q5FB34
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.3.1.112 2 cyanidin + 4 NADPH + 4 H+
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 Vitis vinifera (+)-epicatechin + (-)-catechin + 4 NADP+ the relative concentration of catechin versus epicatechin remains nearly constant and is close to 1 ?
1.3.1.112 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 Vitis vinifera ?
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