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Literature summary for 1.2.1.19 extracted from

  • Kang, H.; Cho, Y.D.
    The kinetic mechanism and chemical modification of gamma-aminobutyraldehyde dehydrogenase from soybean (glycine max) axes (1994), Korean Biochem. J., 27, 526-533.
No PubMed abstract available

Inhibitors

Inhibitors Comment Organism Structure
N-ethylmaleimide inactivation ocurrs due to interaction with a cysteine residue located at or near the cofactor binding site of the enzyme molecule Glycine max
NADH
-
Glycine max

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.02006
-
NAD+
-
Glycine max
0.02612
-
4-Aminobutyraldehyde
-
Glycine max

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
64000
-
x * 64000 Glycine max

Organism

Organism UniProt Comment Textmining
Glycine max
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Glycine max

Source Tissue

Source Tissue Comment Organism Textmining
axis
-
Glycine max
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-aminobutanal + NAD+ + H2O specific for Glycine max 4-aminobutanoate + NADH + H+
-
ir

Subunits

Subunits Comment Organism
? x * 64000 Glycine max

Cofactor

Cofactor Comment Organism Structure
NAD+
-
Glycine max