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Literature summary for 1.3.1.112 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
Search for more literature for 1.3.1.112

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Vitis vinifera

Crystallization (Commentary)

Crystallization (Comment) Organism
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

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

Organism

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

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 ?
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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