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Literature summary for 1.2.1.3 extracted from

  • Moon, K.H.; Abdelmegeed, M.A.; Song, B.J.
    Inactivation of cytosolic aldehyde dehydrogenase via S-nitrosylation in ethanol-exposed rat liver (2007), FEBS Lett., 581, 3967-3972.
    View publication on PubMedView publication on EuropePMC

Inhibitors

Inhibitors Comment Organism Structure
ethanol chronic or binge ethanol-exposure significantly decreases ALDH1 activity via S-nitrosylation, activity is restored by addition of dithiothreitol, ALDH1 activity (using 0.015 mM propionaldehyde as a substrate) is significantly inhibited (by 61%) in chronically ethanol-fed rats Rattus norvegicus

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol
-
Rattus norvegicus 5829
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
55000
-
SDS-PAGE Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
Rattus norvegicus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetaldehyde + NAD+ + H2O
-
Rattus norvegicus acetate + NADH + H+
-
?
propionaldehyde + NAD+ + H2O
-
Rattus norvegicus propionate + NADH + H+
-
?

Synonyms

Synonyms Comment Organism
ALDH1
-
Rattus norvegicus

Cofactor

Cofactor Comment Organism Structure
NAD+
-
Rattus norvegicus