Mutations in ACY1, the gene encoding aminoacylase 1, cause a novel inborn error of metabolism

Jorn Oliver Sass1, Verena Mohr, Heike Olbrich

  • 1Department of General Pediatrics and Adolescent Medicine, University Children's Hospital Freiburg, Freiburg, Germany. Sass@kikLi.ukL.uni-freiburg.de

Insights

Genetic deficiency of Aminoacylase 1 (ACY1) was identified in four children, leading to increased urinary N-acetylated amino acids. The clinical significance of this ACY1 deficiency remains uncertain.

Area of Science:

  • Biochemistry
  • Genetics
  • Metabolic Disorders

Background:

  • N-terminal acetylation is a crucial protein modification.
  • Aminoacylase 1 (ACY1) hydrolyzes N-acetylated proteins and is evolutionarily conserved.
  • ACY1 is expressed in the central nervous system (CNS).

Purpose of the Study:

  • To investigate genetic deficiency of ACY1 in children.
  • To characterize the metabolic and clinical phenotype associated with ACY1 deficiency.
  • To determine the clinical significance of ACY1 deficiency.

Main Methods:

  • Gas chromatography-mass spectrometry (GC-MS) for organic acid analysis.
  • Nuclear magnetic resonance (NMR) spectroscopy for metabolite profiling.
  • Functional assays on patient lymphoblasts and mutation analysis of the ACY1 gene.

Main Results:

  • Four children identified with increased urinary excretion of N-acetylated amino acids.
  • Distinct urinary N-acetylated metabolite patterns confirmed ACY1 dysfunction.
  • Recessive loss-of-function or missense ACY1 mutations found in all affected individuals.

Conclusions:

  • Identified ACY1 mutations cause functional ACY1 deficiency and altered amino acid metabolism.
  • The clinical significance of ACY1 deficiency is currently unclear.
  • Further research is needed to establish the role of ACY1 in CNS function and potential clinical impact.

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