ALDH9A1 Recombinant Rabbit mAb (S-4115-48)

ALDH9A1, also known as gamma-aminobutyraldehyde dehydrogenase (GABALDH) or succinic semialdehyde dehydrogenase (SSADH), is a crucial mitochondrial enzyme belonging to the aldehyde dehydrogenase superfamily that plays a pivotal role in the catabolic pathways of several neurotransmitters and polyamines. Primarily localized within the mitochondria, this NAD+-dependent enzyme catalyzes the irreversible oxidation of succinic semialdehyde (SSA) to succinate, thereby serving as the final step in the degradation pathway of gamma-aminobutyric acid (GABA), the major inhibitory neurotransmitter in the central nervous system, as well as contributing to the metabolism of 4-guanidinobutyrate and polyamines such as spermidine and spermine. By converting SSA into succinate, ALDH9A1 not only prevents the toxic accumulation of SSA—which can otherwise be reduced to gamma-hydroxybutyrate (GHB), a compound associated with neurological disturbances when elevated due to enzyme deficiency—but also links neurotransmitter breakdown directly to the tricarboxylic acid (TCA) cycle, thus integrating neuronal signaling regulation with cellular energy production. Deficiencies or mutations in the ALDH9A1 gene are associated with SSADH deficiency, a rare autosomal recessive neurometabolic disorder characterized by elevated levels of GABA and GHB in the brain and body fluids, leading to symptoms such as developmental delay, hypotonia, ataxia, and seizures, highlighting the protein's essential function in maintaining neurochemical homeostasis and metabolic balance.