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Literature summary extracted from

  • Vallari, R.C.; Pietruszko, R.
    Kinetic mechanism of the human cytoplasmic aldehyde dehydrogenase E1 (1981), Arch. Biochem. Biophys., 212, 9-19.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.2.1.3 adenosine 5'-monophosphate competitive with NAD+ and noncompetitive with acetaldehyde Homo sapiens
1.2.1.3 Chloral hydrate competitive with respect to acetaldehyde Homo sapiens
1.2.1.3 Disulfiram strong inhibition of isoenzyme 1, no inhibition of isoenzyme 2 Homo sapiens
1.2.1.3 NADH competitive with NAD+ at high and low concentrations of acetaldehyde, product inhibitor Homo sapiens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.2.1.3 0.002 0.003 acetaldehyde isoenzyme 2 Homo sapiens

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.2.1.3 cytoplasm
-
 Homo sapiens 5737
-

Organism

EC Number Organism UniProt Comment Textmining
1.2.1.3 Homo sapiens
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.2.1.3 enzyme I and II Homo sapiens

Reaction

EC Number Reaction Comment Organism Reaction ID
1.2.1.3 an aldehyde + NAD+ + H2O = a carboxylate + NADH + H+ mechanism proceeds mainly through an enzyme*NAD+ binary complex, but at high concentrations of acetaldehyde a small degree of randomness is observed, the rate-limiting step of the dehydrogenase reaction occurs after ternary complex interconversion Homo sapiens
a

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.2.1.3 liver
-
 Homo sapiens
-

Cofactor

EC Number Cofactor Comment Organism Structure
1.2.1.3 NAD+
-
 Homo sapiens