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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Cofactor
Cofactor on EC 1.2.1.24 - succinate-semialdehyde dehydrogenase (NAD+)
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NAD+
NAD+ is the more efficient coenzyme compared to NADP+, but the preference is not exclusive
NADP+
is also accepted as coenzyme substrate but leads to 7fold lower reaction rates compared to NAD+ at saturating succinate semialdehyde concentrations
additional information
human SSADH is active in the reduced state but not in the oxidized state because of disulfide bonding between Cys340 and Cys342 residues. Oxidation induces a large conformational change in the dynamic catalytic loop that consists of 11 residues, including the two cysteines that connect helix alpha8 and strand beta13. As a result, the loop blocks both substrate succinate semialdehyde and cofactor NAD+ binding
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