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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Subunits
Subunits on EC 1.2.1.24 - succinate-semialdehyde dehydrogenase (NAD+)
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dimer
homotetramer
homotrimer
tetramer
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. Human SSADH activity is regulated by redox-switch modulation, which depends on reversible intra-disulfide binding to the dynamic catalytic loop. Simulations, and protein transformation and configuration modelling to explain the dynamic redox modulation, method optimization, detailed overview
additional information
each SSADH monomer comprises an N-terminal domain (for NAD+ binding), a catalytic domain (for SSA recognition), and an oligomerization beta-structured domain. In a dynamic catalytic loop, Cys340 and Glu306 are involved in SSA binding and oxidation. Analysis of the tetramer stability by in silico protein modelling analysis
additional information
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4-aminobutyrate aminotransferase and succinate semialdehyde dehydrogenase form a stable enzymatic complex under in vivo conditions