ASPA Human, His

Aspartoacylase (ASPA) is a hydrolytic enzyme that plays a crucial role in the brain by regulating the levels of N-acetyl-L-aspartate (NAA). The enzyme is encoded by the ASPA gene in humans and is also known by other names such as aminoacylase II and ACY-2 . The recombinant form of this enzyme, tagged with a histidine (His) tag, is commonly used in research and biotechnology for various applications.

Aspartoacylase is a zinc-dependent hydrolase that catalyzes the deacylation of NAA into aspartate and acetate . The enzyme is a dimer, consisting of two identical monomers, each containing 313 amino acids . The structure of aspartoacylase includes two distinct domains: the N-terminal domain (residues 1-212) and the C-terminal domain (residues 213-313) .

The His-tagged recombinant form of aspartoacylase is produced in E. coli and purified using conventional chromatographic techniques . The His tag, typically a sequence of six histidine residues, is fused to the N-terminus of the protein, facilitating its purification and detection.

Aspartoacylase is predominantly found in the brain, where it is essential for the proper functioning of the central nervous system. It is involved in the catabolic process of aspartate and plays a role in myelination, the formation of the myelin sheath around nerve fibers . Mutations in the ASPA gene that lead to a loss of aspartoacylase activity are associated with Canavan disease, a rare autosomal recessive neurodegenerative disorder .

The recombinant form of aspartoacylase, especially the His-tagged variant, is widely used in research to study the enzyme’s structure, function, and role in various biological processes. It is also used in drug development and therapeutic research, particularly in the context of Canavan disease.

The recombinant aspartoacylase (His-tagged) is typically stored at -20°C for long-term storage, with the addition of a carrier protein such as HSA or BSA to enhance stability . It is recommended to avoid multiple freeze-thaw cycles to maintain the enzyme’s activity and integrity.