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Literature summary for 1.2.1.24 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
Search for more literature for 1.2.1.24

Inhibitors

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

KM Value [mM]

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

Molecular Weight [Da]

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

Organism

Organism UniProt Comment Textmining
Sus scrofa
-
-
-

Substrates and Products (Substrate)

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

Subunits

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

Cofactor

Cofactor Comment Organism Structure
NAD+
-
 Sus scrofa