ASPA cDNA Clone – Aspartoacylase (Canavan Disease) (Human)

This gene encodes an enzyme that catalyzes the conversion of N-acetyl_L-aspartic acid (NAA) to aspartate and acetate. NAA is abundant in the brain where hydrolysis by aspartoacylase is thought to help maintain white matter. This protein is an NAA scavenger in other tissues. Mutations in this gene cause Canavan disease. Alternatively spliced transcript variants have been found for this gene. [provided by RefSeq, Jul 2008]

ASPA: Catalyzes the deacetylation of N-acetylaspartic acid (NAA) to produce acetate and L-aspartate. NAA occurs in high concentration in brain and its hydrolysis NAA plays a significant part in the maintenance of intact white matter. In other tissues it act as a scavenger of NAA from body fluids. Defects in ASPA are the cause of Canavan disease (CAND); also known as spongy degeneration of the brain. CAND is a rare neurodegenerative condition of infancy or childhood characterized by white matter vacuolization and demeylination that gives rise to a spongy appearance. The clinical features are onset in early infancy, atonia of neck muscles, hypotonia, hyperextension of legs and flexion of arms, blindness, severe mental defect, megalocephaly, and death by 18 months on the average. Belongs to the AspA/AstE family. Aspartoacylase subfamily.

Protein type: Amino Acid Metabolism - alanine, aspartate and glutamate; Cell development/differentiation; Hydrolase; EC 3.5.1.15; Amino Acid Metabolism - histidine

Chromosomal Location of Human Ortholog: 17p13.3

Cellular Component: cytoplasm; cytosol

Molecular Function: aminoacylase activity; aspartoacylase activity; protein binding

Biological Process: amino acid biosynthetic process; aspartate catabolic process

Disease: Canavan Disease