The ACY3 gene encodes Aminoacylase, a hydrolase enzyme responsible for removing the acyl group from acylated aromatic amino acids such as N-acetyl-L-histidine, N-acetyl-L-tyrosine, N-acetyl-L-phenylalanine, and S-benzyl-N-acetyl-L-cysteine. Of these, ACY3 has the highest affinity for the substrate S-benzyl-N-acetyl-L-cysteine.
The ACY3 enzyme exists as a mixture of catalytically active homodimers and homotetramers. Studies have found the enzyme to interact with the hepatitis C virus core protein; it is thus involved in the viral process and the xenobiotic metabolic process.
The ACY3 gene is located on the long arm of chromosome 11. It spans a length of 8.2 kb of DNA and its coding sequence is spread across 9 exons. The gene encodes a 35 kDa protein product consisting of 319 amino acids. It is found to be overexpressed in the kidney, liver and small intestine. Weaker expression is also seen in the heart, brain, lung, testes and stomach.
Monies et al. (2017) reported the findings of 1000 diagnostic panels and exomes carried out at a next generation sequencing lab in Saudi Arabia. One patient, a 7-year-old female, presented with microcephaly, seizures, spasticity and brain atrophy. She was from a consanguineous family and had a family history of the phenotype. Whole exome sequencing carried out on the patient and her parents helped identify a homozygous mutation (c.512C>A, p.A171D) in exon 5 of the patient’s ACY3 gene. This gene mutation was considered a candidate for pathogenicity as it was a novel variant located within the autozygome. It was predicted to be deleterious, and the gene belonged to the same family as ACY2, which is responsible for Canavan disease. Further studies are required to independently confirm this association.
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