Disease relevance of Aldh5a1

• Biochemical and molecular characterization of a succinate semialdehyde dehydrogenase involved in the catabolism of 4-hydroxybutyric acid in Ralstonia eutropha [1].
• Aminobutyrate aminotransferase and succinate semialdehyde dehydrogenase in regions of rat brain after insulin-induced hypoglycemia [2].

High impact information on Aldh5a1

• SSADH is critical in the detoxification of the GABA metabolite, succinic semialdehyde (SSA) [3].
• Inhibition and competition studies in rat brain mitochondria showed that SSADH was the predominant oxidizing enzyme for HNE but only contributed a portion of the total oxidizing activity in liver mitochondria [3].
• The above data suggest that, as for gamma-aminobutyric acid, SSA is present in an unfolded, transoid conformation at the active site of SSADH [4].
• The methyl ester of succinic semialdehyde (SSA) was examined as a substrate for succinate semialdehyde dehydrogenase (SSADH) from rat brain [4].
• Cyclopropyl analogues of SSA, cis- and trans-1-formyl-cyclopropan-2-carboxylic acids, were also individually tested as substrates of SSADH [4].

Biological context of Aldh5a1

• In this study, we tested the hypothesis that aldehyde products of lipid peroxidation inhibit SSADH activity using the endogenous substrate, succinic semialdehyde (SSA, 50 microM) [5].

Anatomical context of Aldh5a1

• 1. The specific activities of 4-aminobutyrate aminotransferase (EC 2.6.1.19) and succinate semialdehyde dehydrogenase (EC 1.2.1.16) were significantly higher in brain mitochondria of non-synaptic origin (fraction M) than those derived from the lysis of synaptosomes (fraction SM2) [6].
• A method is presented for the ultrastructural demonstration of succinate semialdehyde dehydrogenase (SSADH) activity in cerebellar Purkinje neurons and liver hepatocytes; SSADH is an enzyme involved in the degradation of gamma-aminobutyric acid (GABA) [7].
• The SSADH-specific activity seems to appear early, within the first week of postnatal life, in a few Purkinje cells [8].

Associations of Aldh5a1 with chemical compounds

• A subcellular distribution study showed that low- and high-Km activities with acetaldehyde as well as the substrate-specific enzyme succinate semialdehyde dehydrogenase were located mainly in the mitochondrial compartment [9].
• In contrast to the effects obtained in vivo, disulfiram was found to be an inhibitor in vitro of brain succinate semialdehyde dehydrogenase and liver monoamine oxidase [10].
• Formazan granules, which can be ascribed only to specific succinate semialdehyde dehydrogenase activity, are obtained by adding malonate to the incubation medium in order to inhibit both succinate dehydrogenase activity and nothing dehydrogenase [11].
• The formation of these granules is completely inhibited by p-hydroxybenzaldehyde, an inhibitor of succinate semialdehyde dehydrogenase activity [11].

Other interactions of Aldh5a1

• Differential effects of GABA analogues and zinc on glutamate decarboxylase, 4-aminobutyric-2-oxoglutaric acid transaminase and succinate semialdehyde dehydrogenase in rat brain tissue [12].

Analytical, diagnostic and therapeutic context of Aldh5a1

• Molecular cloning of the mature NAD(+)-dependent succinic semialdehyde dehydrogenase from rat and human. cDNA isolation, evolutionary homology, and tissue expression [13].

References