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ACY1 encodes a cytosolic, homodimeric, zinc-binding enzyme that catalyzes the hydrolysis of acylated L-amino acids to L-amino acids and an acyl group, and has been postulated to function in the catabolism and salvage of acylated amino acids. This gene is located on chromosome 3p21. 1, a region reduced to homozygosity in small-cell lung cancer (SCLC), and its expression has been reported to be reduced or undetectable in SCLC cell lines and tumors. The amino acid sequence of human aminoacylase-1 is highly homologous to the porcine counterpart, and this enzyme is the first member of a new family of zinc-binding enzymes. Mutations in this gene cause aminoacylase-1 deficiency, a metabolic disorder characterized by central nervous system defects and increased urinary excretion of N-acetylated amino acids. Alternative splicing of this gene results in multiple transcript variants. Read-through transcription also exists between this gene and the upstream ABHD14A (abhydrolase domain containing 14A) gene. A related pseudogene has been identified on chromosome 18.
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Protein Aliases: ACY-1; acylase; Aminoacylase-1; epididymis secretory protein Li 5; N-acyl-L-amino-acid amidohydrolase
Gene Aliases: ACY-1; ACY1; ACY1D; HEL-S-5
UniProt ID: (Human) Q03154
Entrez Gene ID: (Human) 95
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