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Literature summary extracted from

  • Burgos, J.; Martin, R.; Diez, V.
    Pigeon liver diacetyl reductase. Kinetic and thermodynamic studies with NADH as coenzyme (1974), Biochim. Biophys. Acta, 364, 9-16.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.1.1.304 2-oxoglutarate noncompetitive Columba livia
1.1.1.304 acetoin noncompetitive, product inhibition Columba livia
1.1.1.304 acetone competitive for diacetyl, uncompetitive for NADH Columba livia
1.1.1.304 hexane-2,5-dione noncompetitive Columba livia
1.1.1.304 NAD+ competitive, product inhibition Columba livia
1.1.1.304 Pentane-3-one competitive for diacetyl, uncompetitive for NADH Columba livia

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.304 0.1
-
NADH pH 6.1, 25°C Columba livia
1.1.1.304 3.1
-
diacetyl pH 6.1, 25°C Columba livia

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.304 Columba livia
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.1.1.304 (S)-acetoin + NAD+ = diacetyl + NADH + H+ Theorell-Chance mechanism with NADH as the leading substrate Columba livia

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.1.1.304 liver
-
Columba livia
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.304 diacetyl + NADH + H+
-
Columba livia (S)-acetoin + NAD+
-
?
1.1.1.304 diacetyl + NADPH + H+
-
Columba livia (S)-acetoin + NADP+
-
ir

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.304 6.1
-
-
Columba livia

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.304 NADH
-
Columba livia