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Literature summary extracted from

  • Gargouri, M.; Gallois, B.; Chaudiere, J.
    Binding-equilibrium and kinetic studies of anthocyanidin reductase from Vitis vinifera (2009), Arch. Biochem. Biophys., 491, 61-68.
    View publication on PubMed

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.3.1.112 0.0028
-
 cyanidin pH 7.5, 30°C Vitis vinifera
1.3.1.112 0.111
-
 NADPH pH 7.5, 30°C Vitis vinifera

Organism

EC Number Organism UniProt Comment Textmining
1.3.1.112 Vitis vinifera Q5FB34
-
-

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+
-
 Vitis vinifera (+)-epicatechin + (-)-catechin + 4 NADP+
-
 ?
1.3.1.112 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 Vitis vinifera ?
-
 ?

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.3.1.112 7.5
-
 assay at Vitis vinifera

Cofactor

EC Number Cofactor Comment Organism Structure
1.3.1.112 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+ Vitis vinifera
1.3.1.112 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+ Vitis vinifera