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Literature summary for 1.2.1.19 extracted from

  • Kurys, G.; Shah, P.C.; Kikonyogo, A.; Reed, D.; Ambroziak, W.; Pietruzko, R.
    Human aldehyde dehydrogenase, cDNA cloning and primary structure of the enzyme that catalyzes dehydrogenation of 4-aminobutyraldehyde (1993), Eur. J. Biochem., 218, 311-320.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
-
Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.005
-
4-Aminobutyraldehyde E3 isozyme Homo sapiens
0.5
-
4-Aminobutyraldehyde E2 isozyme Homo sapiens
0.8
-
4-Aminobutyraldehyde E1 isozyme Homo sapiens

Localization

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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4-aminobutanal + NAD+ + H2O Homo sapiens involved in amino aldehyde metabolism, connects metabolism of a diamine putrescine with that of the inhibitory neurotransmitter 4-aminobutyric acid 4-aminobutanoate + NADH + H+
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-aminobutanal + NAD+ + H2O
-
Homo sapiens 4-aminobutanoate + NADH + H+
-
?
4-aminobutanal + NAD+ + H2O involved in amino aldehyde metabolism, connects metabolism of a diamine putrescine with that of the inhibitory neurotransmitter 4-aminobutyric acid Homo sapiens 4-aminobutanoate + NADH + H+
-
?

Cofactor

Cofactor Comment Organism Structure
NAD+
-
Homo sapiens