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Literature summary for 1.2.1.3 extracted from

  • Hill, J.P.; Dickinson, F.M.
    Steady-state kinetics of aldehyde by pig liver cytosolic aldehyde dehydrogenase (1988), Biochem. Soc. Trans., 16, 857-858.
No PubMed abstract available
Search for more literature for 1.2.1.3

Activating Compound

Activating Compound Comment Organism Structure
acetaldehyde substrate activation at elevated aldehyde concentrations Sus scrofa
Butanal substrate activation at elevated aldehyde concentrations Sus scrofa
additional information at high NAD+ concentrations, above 0.5 mM, and high aldehyde concentrations, above 0.05 mM propanal or above 1 mM acetaldehyde substrate activation of oxidation rates is observed Sus scrofa
propanal substrate activation at elevated aldehyde concentrations Sus scrofa

Inhibitors

Inhibitors Comment Organism Structure
cyclohexanal substrate inhibition at elevated aldehyde concentration, increase of NAD+ concentration from 0.85 mM to 2.55 mM removes substrate inhibition Sus scrofa
Indole-3-acetaldehyde substrate inhibition at elevated aldehyde concentration, increase of NAD+ concentration from 0.85 mM to 2.55 mM removes substrate inhibition Sus scrofa
additional information at low coenzyme concentrations, below 0.005 mM, and high aldehyde concentrations substrate inhibition of oxidation rates is observed Sus scrofa
p-hydroxyphenylacetaldehyde substrate inhibition at elevated aldehyde concentration, increase of NAD+ concentration from 0.85 mM to 2.55 mM removes substrate inhibition Sus scrofa
p-nitrobenzaldehyde substrate inhibition at elevated aldehyde concentration, increase of NAD+ concentration from 0.85 mM to 2.55 mM removes substrate inhibition Sus scrofa
pivaldehyde substrate inhibition at elevated aldehyde concentration, increase of NAD+ concentration from 0.85 mM to 2.55 mM removes substrate inhibition Sus scrofa
pyridine 3-aldehyde substrate inhibition at elevated aldehyde concentration, increase of NAD+ concentration from 0.85 mM to 2.55 mM removes substrate inhibition Sus scrofa

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol
-
 Sus scrofa 5829
-
cytosol
-
 Ovis aries 5829
-

Organism

Organism UniProt Comment Textmining
Ovis aries
-
-
-
Sus scrofa
-
-
-

Reaction

Reaction Comment Organism Reaction ID
an aldehyde + NAD+ + H2O = a carboxylate + NADH + H+ compulsory ordered mechanism Sus scrofa
a

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
 Sus scrofa
-
liver
-
 Ovis aries
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-hydroxyphenyl-3-methoxyglycolaldehyde + NAD+ + H2O
-
 Sus scrofa 4-hydroxyphenyl-3-methoxyglycolate + NADH
-
 ?
4-hydroxyphenylglycolaldehyde + NAD+ + H2O
-
 Sus scrofa 4-hydroxyphenylglycolate + NADH
-
 ?
acetaldehyde + NAD+ + H2O
-
 Sus scrofa acetate + NADH + H+
-
 ?
acetaldehyde + NAD+ + H2O
-
 Ovis aries acetate + NADH + H+
-
 ?
butanal + NAD+ + H2O
-
 Sus scrofa butyrate + NADH + H+
-
 ?
butanal + NAD+ + H2O
-
 Ovis aries butyrate + NADH + H+
-
 ?
cyclohexanaldehyde + NAD+ + H2O
-
 Sus scrofa cyclohexanoate + NADH
-
 ?
decanal + NAD+ + H2O
-
 Sus scrofa decanoate + NADH
-
 ?
decanal + NAD+ + H2O
-
 Ovis aries decanoate + NADH
-
 ?
indole-3-aldehyde + NAD+ + H2O
-
 Sus scrofa indole-3-carboxylate + NADH
-
 ?
p-hydroxyphenylacetaldehyde + NAD+ + H2O
-
 Sus scrofa p-hydroxyphenylacetate + NADH
-
 ?
p-hydroxyphenylacetaldehyde + NAD+ + H2O
-
 Ovis aries p-hydroxyphenylacetate + NADH
-
 ?
p-nitrobenzaldehyde + NAD+ + H2O
-
 Sus scrofa p-nitrobenzoate + NADH
-
 ?
p-nitrobenzaldehyde + NAD+ + H2O
-
 Ovis aries p-nitrobenzoate + NADH
-
 ?
pivaldehyde + NAD+ + H2O
-
 Sus scrofa pivalate + NADH
-
 ?
propanal + NAD+ + H2O
-
 Sus scrofa propionate + NADH
-
 ?
propanal + NAD+ + H2O
-
 Ovis aries propionate + NADH
-
 ?
pyridine 3-aldehyde + NAD+ + H2O
-
 Sus scrofa pyridine-3-carboxylate + NADH
-
 ?
trans-cinnamaldehyde + NAD+ + H2O
-
 Sus scrofa trans-cinnamate + NADH
-
 ?

Cofactor

Cofactor Comment Organism Structure
NAD+
-
 Sus scrofa
NAD+
-
 Ovis aries