1.2.1.24: succinate-semialdehyde dehydrogenase (NAD+)
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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
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aldhs
-
gamma-hydroxybutyric
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ssadhd
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4-hydroxybutyric
- propionaldehyde
- trans-4-hydroxy-2-nonenal
- aldh4a1
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akr7a2
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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
1.2.1.24 succinate-semialdehyde dehydrogenase (NAD+)Advanced search results
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General Information on EC 1.2.1.24 - succinate-semialdehyde dehydrogenase (NAD+)
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
malfunction
metabolism
physiological function
additional information
human SSADH intrinsic regulatory mechanism, redox-switch modulation, by which large conformational changes are brought about in the catalytic loop through disulfide bonding, enzyme molecular structure, overview
malfunction
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at approximately postnatal day 16-22 SSADH-deficient mice display ataxia and loss of motor control, and develop generalized seizures leading to rapid death by the fourth week of life. D-2-hydroxyglutarate and 4,5-dihydroxyhexanoic acid are elevated in SSADH-deficient mice. SSADH-deficient mice demonstrate a 20% reduction in the ethanolamine glycerophospholipid content as compared to wild type littermates while other brain phospholipids (choline glycerophospholipid, phosphatidylserine and phosphatidylinositol) are not affected
malfunction
SSADH enzyme activity is deficient in patients with gamma-hydroxybutyric aciduria
malfunction
mutation of gene ALDH5A1 with amino acid exchange K301E is associated with succinic semialdehyde dehydrogenase deficiency and severe intellectual disability in an Iranian family. Succinic semialdehyde dehydrogenase (SSADH) deficiency is a rare autosomal recessive inherited metabolic disorder of the catabolism of the neurotransmitter gamma-aminobutyric acid (GABA) with a very variable clinical phenotype ranging from mild intellectual disability to severe neurological defects. The disorder results in the accumulation of gamma-hydroxybutyrate in the brain, 30fold increased level compared to wild-type. No SSADH enzyme activity is detected in the patient's lymphoblasts
malfunction
GABA addition to glioma cells increased proliferation rates. Expression of mutated IDH1 and treatment with 2-HG reduced glutamine and GABA oxidation, diminishes the pro-proliferative effect of GABA in succinic semialdehyde dehydrogenase (SSADH) expressing cells. The enzyme SSADH is overexpressed in almost all glioma cells. No significant association between SSADH expression and clinicopathological parameters (e.g. IDH mutation). IDH mutation and 2-HG production inhibit GABA oxidation in glioma cells
malfunction
succinic semialdehyde dehydrogenase (SSADH) deficiency (SSADHD) is a heritable disorder of gamma-aminobutyric acid (GABA) metabolism associating with elevated GABA and gamma-hydroxybutyrate (GHB). The heterogeneous phenotype ranges from mild to severe, including developmental delay, movement abnormalities, neuropsychiatric morbidity, and seizures murine succinic semialdehyde dehydrogenase deficiency (SSADHD) manifests with high concentrations of gamma-aminobutyric acid (GABA) and gamma-hydroxybutyrate (GHB) and low glutamine in the brain
malfunction
succinic semialdehyde dehydrogenase deficiency (SSADHD) is a rare autosomal-recessively inherited metabolic disorder of GABA catabolism that results in the accumulation of 4-hydroxybutyrate (GHB) in tissues, cerebrospinal fluid, blood and urine. The clinical phenotype of SSADHD is highly variable, ranging from mild intellectual and developmental disabilities to severe neurological defects such as seizures, hypotonia, ataxia and behavioural problems, especially in older patients. The most common abnormalities on cerebral MRI consist of increased T2-weighted signal involving the cerebellar dentate nuclei, globus pallidus, and subthalamic nuclei symmetrically, as well as the subcortical white matter and brainstem. In SSADHD, the final step of the GABA degradation pathway shifts towards a massive reduction of SSA to gamma-hydroxybutyrate (GHB) through either specific or non-specific oxidoreductase reactions. The abnormal accumulation of GHB, eventually excreted in urine, is the pathognomonic disease marker
malfunction
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succinic semialdehyde dehydrogenase (SSADH) deficiency (SSADHD) is a heritable disorder of gamma-aminobutyric acid (GABA) metabolism associating with elevated GABA and gamma-hydroxybutyrate (GHB). The heterogeneous phenotype ranges from mild to severe, including developmental delay, movement abnormalities, neuropsychiatric morbidity, and seizures murine succinic semialdehyde dehydrogenase deficiency (SSADHD) manifests with high concentrations of gamma-aminobutyric acid (GABA) and gamma-hydroxybutyrate (GHB) and low glutamine in the brain
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metabolism
SSADH plays an essential role in the metabolism of the inhibitory neurotransmitter c-aminobutyric acid
metabolism
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under normal physiological conditions, SSADH works in tandem with GABA transaminase to convert the carbon backbone of gamma-aminobutyric acid to succinate, the latter a source of energy within the tricarboxylic acid cycle. SSADH, in brain, is the major aldehyde dehydrogenase responsible for 4-hydroxy-trans-2-nonenal disposition, but only a minor contributor to its metabolism in liver
metabolism
under normal physiological conditions, SSADH works in tandem with GABA transaminase to convert the carbon backbone of gamma-aminobutyric acid to succinate, the latter a source of energy within the tricarboxylic acid cycle. SSADH, in brain, is the major aldehyde dehydrogenase responsible for 4-hydroxy-trans-2-nonenal disposition, but only a minor contributor to its metabolism in liver
metabolism
the enzyme is involved in the metabolism of the inhibitory neurotransmitter gamma-aminobutyric acid (GABA)
metabolism
astrocytomas and oligodendrogliomas, collectively called diffuse gliomas, are derived from astrocytes and oligodendrocytes that are in metabolic symbiosis with neurons. Astrocytes can catabolize neuron-derived glutamate and gamma-aminobutyric acid (GABA) for supporting and regulating neuronal functions. Succinic semialdehyde dehydrogenase (SSADH) expression is correlated to GABA oxidation. SSADH expression may participate in the oxidation and/or consumption of GABA in gliomas, furthermore, GABA oxidation capacity may contribute to proliferation and worse prognosis of gliomas
physiological function
enzyme SSADH is a NAD+-dependent mitochondrial homotetrameric allosteric enzyme and works with gamma-aminobutyric acid (GABA) transaminase to convert GABA to succinic semialdehyde (SSA) which is, in turn, oxidized by SSADH to succinic acid. Besides its established role in GABA catabolism, SSADH is reported to contribute to the antioxidative mitochondrial defence by oxidation of 4-hydroxynonenal, a degradation end product of peroxidated lipids
physiological function
GABA can feed the TCA cycle via the activities of GABA transaminase and succinic semialdehyde dehydrogenase (SSADH) to produce succinate. Potential role of GABA shunt and SSADH activity in the survival and the proliferation of SSADH expressing U-251 wild-type cells
