1.2.1.24: succinate-semialdehyde dehydrogenase (NAD+)
This is an abbreviated version!
For detailed information about succinate-semialdehyde dehydrogenase (NAD+), go to the full flat file.
Word Map on EC 1.2.1.24
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1.2.1.24
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aldhs
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gamma-hydroxybutyric
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ssadhd
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4-hydroxybutyric
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propionaldehyde
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trans-4-hydroxy-2-nonenal
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aldh4a1
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akr7a2
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ssadh-deficient
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medicine
- 1.2.1.24
-
aldhs
-
gamma-hydroxybutyric
-
ssadhd
-
4-hydroxybutyric
- propionaldehyde
- trans-4-hydroxy-2-nonenal
- aldh4a1
-
akr7a2
-
ssadh-deficient
- medicine
Reaction
Synonyms
aldehyde dehydrogenase 5a1, ALDH5A, ALDH5A1, alphaKGSA dehydrogenase, dehydrogenase, succinate semialdehyde, NAD(+)-dependent succinic semialdehyde dehydrogenase, SSADH, SSADH-I, SSADH/ALDH5A1, SSALDH, SSO1629, succinate semialdehyde dehydrogenase, succinate semialdehyde:NAD+ oxidoreductase, succinic semialdehyde dehydrogenase, succinyl semialdehyde dehydrogenase, YneI dehydrogenase
ECTree
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Inhibitors
Inhibitors on EC 1.2.1.24 - succinate-semialdehyde dehydrogenase (NAD+)
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4-dimethylaminoazobenzene-4-iodoacetamide
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time-dependent loss of activity, pseudo first-order kinetics. The inhibitor binds to a cysteine residue or near its active site. Inactivation is prevented by preincubation with succinate semialdehyde, but not by preincubation with coenzyme NAD+
o-phthalaldehyde
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binding of 10 mol per mol of enzyme results in irreversible loss of activity
4-hydroxybenzaldehyde
linear dead-end inhibition, competitive versus succinate semialdehyde, uncompetitive versus NAD+
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4 mM, 40% inhibition, reversible, competitive with respect to succinate semialdehyde, uncompetitive with respect to NAD+
NADH
product inhibition, competitive versus NAD+, uncompetitive versus succinate semialdehyde
NADH
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NADH is a strong competitive inhibitor with respect to NAD+ and behaves as a non-competitive inhibitor with respect to succinate semialdehyde
NADH
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competitive with respect to NAD+; mixed with respect to succinate semialdehyde
pyridoxal 5'-phosphate
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catalytic function is modulated by binding of pyridoxal-5'-phosphate to specific Lys347 residue at or near the coenzyme-binding site of the protein, NAD+ protects from inactivation
substrate inhibition, uncompetitive versus NAD+
succinate semialdehyde
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inhibition by the succinate semialdehyde substrate is starting already at a concentration as low as 0.02 mM
succinate semialdehyde
inhibition by the succinate semialdehyde substrate is starting already at a concentration as low as 0.02 mM
succinate semialdehyde
the enzyme loses more than 80% of its enzymatic potential at 0.5 mM and shows 8% residual activity at 3 mM succinate semialdehyde
succinate semialdehyde
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substrate inhibition, uncompetitive with respect to NAD+
succinate semialdehyde
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the enzyme loses more than 80% of its enzymatic potential at 0.5 mM and shows 8% residual activity at 3 mM succinate semialdehyde
additional information
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no inhibition by 0.1 mM trans-2-hexenal and 0.1 mM crotonaldehyde
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