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Literature summary for 1.1.1.304 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
Search for more literature for 1.1.1.304

Inhibitors

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

KM Value [mM]

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

Organism

Organism UniProt Comment Textmining
Columba livia
-
-
-

Reaction

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

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
 Columba livia
-

Substrates and Products (Substrate)

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.1
-
-
 Columba livia

Cofactor

Cofactor Comment Organism Structure
NADH
-
 Columba livia