ACY1 Mouse

The mouse ACY1 gene encodes the aminoacylase enzyme, which consists of 402 amino acids and has a calculated molecular mass of approximately 45 kDa . The enzyme is expressed with a C-terminal polyhistidine tag, which aids in its purification and detection . The recombinant mouse aminoacylase-1 protein is typically produced in HEK293 cells or mouse myeloma cell lines .

Aminoacylase-1 catalyzes the hydrolysis of N-acetylated amino acids, such as N-acetyl-L-methionine (Ac-Met), into their corresponding free amino acids and acyl groups . This activity is essential for the breakdown and recycling of acetylated amino acids generated during protein degradation .

Aminoacylase-1 is involved in various physiological processes, including the regulation of responses to oxidative stress . It has been shown to interact with sphingosine kinase 1 (SphK1), influencing its physiological functions related to cell proliferation and apoptosis . The enzyme’s activity is crucial for maintaining cellular homeostasis and preventing the accumulation of toxic metabolites.

Deficiency of aminoacylase-1 due to mutations in the ACY1 gene follows an autosomal-recessive trait of inheritance and is characterized by the accumulation of N-acetyl amino acids in the urine . This condition, known as aminoacylase 1 deficiency, can lead to various metabolic disorders and requires careful monitoring and management.

Recombinant mouse aminoacylase-1 protein is produced using advanced biotechnological methods to ensure high purity and activity. The protein is typically purified to >95% purity as determined by SDS-PAGE and has a specific activity of >4,000 pmol/min/µg when measured by its ability to cleave N-acetyl-L-methionine . The recombinant protein is supplied in a lyophilized form or as a solution in Tris and NaCl, and it is stable for several months when stored under appropriate conditions .