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Literature summary extracted from

  • Blaner, W.S.; Churchich, J.
    Succinic semialdehyde dehydrogenase. Reactivity of lysyl residues (1979), J. Biol. Chem., 254, 1794-1798.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.2.1.24 4-hydroxybenzaldehyde
-
Sus scrofa
1.2.1.24 m-hydroxybenzaldehyde
-
Sus scrofa
1.2.1.24 o-phthalaldehyde binding of 10 mol per mol of enzyme results in irreversible loss of activity Sus scrofa
1.2.1.24 pyridoxal 5'-phosphate NAD+ protects Sus scrofa

Organism

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

Purification (Commentary)

EC Number Purification (Comment) Organism
1.2.1.24
-
Sus scrofa

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.2.1.24 brain
-
Sus scrofa
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.2.1.24 5.3
-
-
Sus scrofa

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.2.1.24 succinate semialdehyde + NAD+ + H2O
-
Sus scrofa succinate + NADH
-
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pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.2.1.24 8 9.5
-
Sus scrofa

Cofactor

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