Aspartoacylase, Aminoacylase-2, ACY-2, ASPA, ACY2, ASP
Greater than 90.0% as determined by SDS-PAGE.
ASPA Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 313 amino acids (1-313) and having a molecular mass of 35.7 kDa.
ASPA is purified by proprietary chromatographic techniques.
Aspartoacylase, Aminoacylase-2, ACY-2, ASPA, ACY2, ASP
MTSCHIAEEH IQKVAIFGGT HGNELTGVFL VKHWLENGAE IQRTGLEVKP FITNPRAVKK CTRYIDCDLN RIFDLENLGK KMSEDLPYEV RRAQEINHLF GPKDSEDSYD IIFDLHNTTS NMGCTLILED SRNNFLIQMF HYIKTSLAPL PCYVYLIEHP SLKYATTRSI AKYPVGIEVG PQPQGVLRAD ILDQMRKMIK HALDFIHHFN EGKEFPPCAI EVYKIIEKVD YPRDENGEIA AIIHPNLQDQ DWKPLHPGDP MFLTLDGKTI PLGGDCTVYP VFVNEAAYYE KKEAFAKTTK LTLNAKSIRC CLH
Aspartoacylase, also known as ASPA, is a hydrolytic enzyme that plays a crucial role in the metabolism of N-acetyl-L-aspartic acid (NAA). This enzyme is encoded by the ASPA gene in humans and is primarily found in the brain. Aspartoacylase catalyzes the deacylation of NAA to produce aspartate and acetate .
Aspartoacylase is a zinc-dependent hydrolase that promotes the deprotonation of water to use as a nucleophile, a mechanism similar to many other zinc-dependent hydrolases . The enzyme is a dimer composed of two identical monomers, each consisting of 313 amino acids. Each monomer has two distinct domains: the N-terminal domain (residues 1-212) and the C-terminal domain (residues 213-313) .
The primary function of aspartoacylase is to regulate the levels of NAA in the brain. NAA is abundant in the brain and is involved in maintaining white matter integrity. The hydrolysis of NAA by aspartoacylase is essential for the proper functioning of the central nervous system .
Mutations in the ASPA gene can lead to a rare autosomal recessive neurodegenerative disorder known as Canavan disease. This condition is characterized by the accumulation of NAA in the brain, leading to spongy degeneration of the white matter. Canavan disease results in severe developmental delays, motor dysfunction, and early mortality .
Human recombinant aspartoacylase is produced using recombinant DNA technology, which involves inserting the ASPA gene into a suitable expression system, such as bacteria or yeast. This allows for the large-scale production of the enzyme for research and therapeutic purposes. Recombinant aspartoacylase is used in studies to understand the enzyme’s structure, function, and role in diseases like Canavan disease .
Research on aspartoacylase has provided valuable insights into its role in the brain and its involvement in neurological disorders. Studies have shown that aspartoacylase activity is crucial for the maintenance of white matter and the proper functioning of oligodendrocytes, the cells responsible for myelination in the central nervous system .
In addition to its role in the brain, aspartoacylase has been implicated in the metabolic reprogramming of cancer cells. Recent studies suggest that ASPA may play a role in tumor development and progression, making it a potential target for cancer therapy .