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Literature summary for 1.2.1.16 extracted from

  • Jaeger, M.; Rothacker, B.; Ilg, T.
    Saturation transfer difference NMR studies on substrates and inhibitors of succinic semialdehyde dehydrogenases (2008), Biochem. Biophys. Res. Commun., 372, 400-406.
    View publication on PubMed
Search for more literature for 1.2.1.16

Cloned(Commentary)

Cloned (Comment) Organism
-
 Drosophila melanogaster

Protein Variants

Protein Variants Comment Organism
C311A mutant is still soluble but unable to catalyze succinate semialdehyde oxidation. Mutation leads to an inactive product binding both succinate semialdehyde aldehyde and gem-diol Drosophila melanogaster

Inhibitors

Inhibitors Comment Organism Structure
3-tolualdehyde only the aldehyde forms and not the gem-diol forms of the inhibitor 3-tolualdehyde bind to the enzyme Drosophila melanogaster

Organism

Organism UniProt Comment Textmining
Drosophila melanogaster
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information only the aldehyde forms and not the gem-diol forms of the specific substrate succinic semialdehyde , of selected aldehyde substrates, and of the inhibitor 3-tolualdehyde bind to the enzyme. Residue cysteine311 is crucial for their discrimination Drosophila melanogaster ?
-
 ?
succinate semialdehyde + NADP+ + H2O
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 Drosophila melanogaster succinate + NADPH + 2 H+
-
 ?

Cofactor

Cofactor Comment Organism Structure
NAD+ higher activity in the presence of NAD+ than in the presence of NADP+ Drosophila melanogaster
NADP+ higher activity in the presence of NAD+ than in the presence of NADP+ Drosophila melanogaster