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Literature summary extracted from

  • Blaner, W.S.; Churchich, J.E.
    The binding of NADH to succinic semialdehyde dehydrogenase (1980), Eur. J. Biochem., 109, 431-437.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.2.1.24 NADH competitive with NAD+ Sus scrofa
1.2.1.24 succinate semialdehyde
-
Sus scrofa

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.2.1.24 0.0034
-
Glutaric semialdehyde
-
Sus scrofa
1.2.1.24 0.015
-
succinate semialdehyde
-
Sus scrofa
1.2.1.24 0.31
-
NAD+
-
Sus scrofa

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.2.1.24 41000
-
4 * 41000, SDS-PAGE Sus scrofa
1.2.1.24 160000
-
non-denaturing PAGE, gel filtration Sus scrofa

Organism

EC Number Organism UniProt Comment Textmining
1.2.1.24 Sus scrofa
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.2.1.24 glutaric semialdehyde + NAD+ + H2O 25% of the activity with succinate semialdehyde Sus scrofa glutarate + NADH
-
?
1.2.1.24 succinate semialdehyde + NAD+ + H2O
-
Sus scrofa succinate + NADH
-
?

Subunits

EC Number Subunits Comment Organism
1.2.1.24 tetramer 4 * 41000, SDS-PAGE Sus scrofa

Cofactor

EC Number Cofactor Comment Organism Structure
1.2.1.24 NAD+
-
Sus scrofa