EC Number   |
General Information |
Reference  |
|---|
    1.2.1.24 | metabolism |
SSADH plays an essential role in the metabolism of the inhibitory neurotransmitter c-aminobutyric acid |
710394 |
| 1.2.1.24 | malfunction |
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 |
710898 |
| 1.2.1.24 | malfunction |
SSADH enzyme activity is deficient in patients with gamma-hydroxybutyric aciduria |
710898 |
| 1.2.1.24 | 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 |
710898 |
| 1.2.1.24 | 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 |
741570 |
| 1.2.1.24 | metabolism |
the enzyme is involved in the metabolism of the inhibitory neurotransmitter gamma-aminobutyric acid (GABA) |
743762 |
| 1.2.1.24 | more |
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 |
743762 |
| 1.2.1.24 | 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 |
763330 |
| 1.2.1.24 | 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 |
763330 |
| 1.2.1.24 | 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 |
763330 |
