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Literature summary 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

EC Number Inhibitors Comment Organism Structure
1.2.1.19 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
1.2.1.19 NADH
-
Glycine max

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.2.1.19 0.02006
-
NAD+
-
Glycine max
1.2.1.19 0.02612
-
4-Aminobutyraldehyde
-
Glycine max

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.2.1.19 64000
-
x * 64000 Glycine max

Organism

EC Number Organism UniProt Comment Textmining
1.2.1.19 Glycine max
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.2.1.19
-
Glycine max

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.2.1.19 axis
-
Glycine max
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.2.1.19 4-aminobutanal + NAD+ + H2O specific for Glycine max 4-aminobutanoate + NADH + H+
-
ir

Subunits

EC Number Subunits Comment Organism
1.2.1.19 ? x * 64000 Glycine max

Cofactor

EC Number Cofactor Comment Organism Structure
1.2.1.19 NAD+
-
Glycine max