ACY1 Human

Aminoacylase-1 (ACY1) is a cytosolic, homodimeric, zinc-binding enzyme that plays a crucial role in the hydrolysis of acylated L-amino acids into L-amino acids and an acyl group . This enzyme is encoded by the ACY1 gene in humans and is involved in the catabolism and salvage of acylated amino acids .

Aminoacylase-1 is a metalloenzyme that requires zinc for its catalytic activity . It is composed of 419 amino acids and has a predicted molecular mass of approximately 47.3 kDa . The enzyme operates as a homodimer, meaning it forms a functional unit by pairing two identical subunits . The primary function of ACY1 is to catalyze the hydrolysis of N-acylated amino acids, except for L-aspartate derivatives, which are cleaved by aminoacylase-2 .

ACY1 is widely expressed in various tissues and is believed to play a role in regulating responses to oxidative stress . It interacts with sphingosine kinase 1 (SphK1), influencing its physiological functions related to cell proliferation and apoptosis . Deficiency in ACY1 due to mutations in the ACY1 gene follows an autosomal-recessive inheritance pattern and is characterized by the accumulation of N-acetyl amino acids in the urine .

Recombinant human aminoacylase-1 is produced using various expression systems, including baculovirus-insect cells . The recombinant protein is typically expressed with a polyhistidine tag at the C-terminus to facilitate purification . The protein is then lyophilized and can be reconstituted for use in various biochemical assays and research applications .

Recombinant ACY1 is used in research to study its enzymatic activity, interaction with other proteins, and its role in metabolic pathways. It is also utilized in the development of therapeutic strategies for conditions resulting from ACY1 deficiency .