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Literature summary for 1.1.1.1 extracted from

  • Heinstra, P.W.H.; Thoerig, G.E.W.; Scharloo, W.; Drenth, W.; Nolte, R.J.M.
    Kinetics and thermodynamics of ethanol oxidation catalyzed by genetic variants of the alcohol dehydrogenase from Drosophila melanogaster and D. simulans (1988), Biochim. Biophys. Acta, 967, 224-233.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
NADH competitive towards NAD+ Drosophila melanogaster

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information kinetics of ethanol oxidation Drosophila melanogaster
additional information
-
additional information kinetics of ethanol oxidation Drosophila simulans

Organism

Organism UniProt Comment Textmining
Drosophila melanogaster
-
-
-
Drosophila simulans
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Drosophila simulans
alleloenzyme Adh71k Drosophila melanogaster

Reaction

Reaction Comment Organism Reaction ID
a primary alcohol + NAD+ = an aldehyde + NADH + H+ rapid equilibrium random mechanism Drosophila melanogaster
a primary alcohol + NAD+ = an aldehyde + NADH + H+ rapid equilibrium random mechanism Drosophila simulans

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
additional information kinetics of ethanol oxidation Drosophila melanogaster
additional information
-
additional information kinetics of ethanol oxidation Drosophila simulans

Cofactor

Cofactor Comment Organism Structure
NAD+
-
Drosophila melanogaster
NAD+
-
Drosophila simulans
NADH
-
Drosophila melanogaster
NADH
-
Drosophila simulans