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ACY1
ACY1 Full Name
aminoacylase 1
ACY1 Introduction
ACY1 encodes aminoacylase 1, a zinc-dependent cytosolic hydrolase that catalyzes the hydrolysis of N-acetylated amino acids into free amino acids and acetate, representing the terminal step in the degradation pathway of acetyl-modified proteins. This enzymatic reaction is fundamentally important for amino acid recycling within cells, as it liberates unmodified amino acids from their N-terminal acetyl groups, enabling their reutilization in de novo protein synthesis and nitrogen metabolism. The enzyme exhibits broad substrate specificity toward aliphatic N-acetylated amino acids, with particularly high expression in the kidneys and brain. Alternative splicing of the ACY1 gene gives rise to multiple transcript variants encoding distinct protein isoforms that display differential tissue distribution patterns, suggesting specialized functional roles across organ systems. The biological significance of N-terminal acetylation itself is substantial, as this modification is one of the most common protein modifications in eukaryotes and influences protein stability, subcellular localization, and protein-protein interactions.
Mutations in ACY1 cause aminoacylase 1 deficiency (ACY1D), an autosomal recessive inborn error of metabolism that follows a recessive inheritance pattern. The biochemical hallmark of this condition is persistently elevated urinary excretion of N-acetylated amino acids, which serves as a reliable diagnostic biomarker and is detected in all affected individuals regardless of clinical severity. The clinical presentation of ACY1D is remarkably heterogeneous, ranging from complete absence of symptoms to significant neurological disability. Affected individuals may present with psychomotor developmental delay, mild to moderate intellectual disability, muscular hypotonia, epileptic seizures, movement disorders such as dystonia, and autistic behavioral features. Notably, some individuals harboring pathogenic ACY1 variants have been identified through newborn screening or family studies without any apparent clinical manifestations, raising important questions about penetrance and the contribution of environmental or genetic modifiers. Advanced neuroimaging has revealed persistent basal ganglia signal abnormalities in a subset of patients, indicating that ACY1D-related neurodegeneration follows a recognizable radiologic pattern and expanding the previously described phenotypic spectrum. Despite detailed characterization of the biochemical defect, the precise mechanistic link between impaired N-acetylated amino acid hydrolysis and the observed neurodevelopmental deficits remains incompletely elucidated, though hypotheses include accumulation of toxic metabolites, deficiency of recycled amino acid precursors for neurotransmitter synthesis, and disruption of acetyl-coenzyme A homeostasis.
Alternate Names for ACY1
ACY1; aminoacylase 1; ACY-1; ACY1D; HEL-S-5; aminoacylase-1; acylase; epididymis secretory protein Li 5; N-acyl-L-amino-acid amidohydrolase;
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