Related Experiment Video
Updated: Aug 11, 2026

A Facile Protocol to Generate Site-Specifically Acetylated Proteins in Escherichia Coli
Published on: December 9, 2017
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.
Abstract:
N-terminal acetylation of proteins is a widespread and highly conserved process. Aminoacylase 1 (ACY1; EC 3.5.14) is the most abundant of the aminoacylases, a class of enzymes involved in hydrolysis of N-acetylated proteins. Here, we present four children with genetic deficiency of ACY1. They were identified through organic acid analyses using gas chromatography-mass spectrometry, revealing increased urinary excretion of several N-acetylated amino acids, including the derivatives of methionine, glutamic acid, alanine, leucine, glycine, valine, and isoleucine. Nuclear magnetic resonance spectroscopy analysis of urine samples detected a distinct pattern of N-acetylated metabolites, consistent with ACY1 dysfunction. Functional analyses of patients' lymphoblasts demonstrated ACY1 deficiency. Mutation analysis uncovered recessive loss-of-function or missense ACY1 mutations in all four individuals affected. We conclude that ACY1 mutations in these children led to functional ACY1 deficiency and excretion of N-acetylated amino acids. Questions remain, however, as to the clinical significance of ACY1 deficiency. The ACY1-deficient individuals were ascertained through urine metabolic screening because of unspecific psychomotor delay (one subject), psychomotor delay with atrophy of the vermis and syringomyelia (one subject), marked muscular hypotonia (one subject), and follow-up for early treated biotinidase deficiency and normal clinical findings (one subject). Because ACY1 is evolutionarily conserved in fish, frog, mouse, and human and is expressed in the central nervous system (CNS) in human, a role in CNS function or development is conceivable but has yet to be demonstrated. Thus, at this point, we cannot state whether ACY1 deficiency has pathogenic significance with pleiotropic clinical expression or is simply a biochemical variant. Awareness of this new genetic entity may help both in delineating its clinical significance and in avoiding erroneous diagnoses.
Related Concept Videos
Inborn Errors of Metabolism
Overview of Protein Metabolism
Amino acids play various roles in the body once they are absorbed into cells. They are restructured...
Lethal Alleles
Lucien Cuénot discovered lethal alleles in 1905 while studying the inheritance of coat color in mice. The agouti gene is responsible for the color of the coat in mice. This gene codes for an agouti-signaling protein, which is responsible for melanin distribution in mammals. The wild-type allele gives rise to gray-brown coat color in mice, while the mutant allele gives rise to yellow coat color. In addition to coat color, the agouti gene is associated with the yellow...
Lysosomal Hydrolases
Translation
Translation is the process of synthesizing proteins from the genetic information carried by messenger RNA (mRNA). Following transcription, it constitutes the final step in the expression of genes. This process is carried out by ribosomes, complexes of protein and specialized RNA molecules. Ribosomes, transfer RNA (tRNA), and other proteins produce a chain of amino acids—the polypeptide—as the end product of translation.
Translation Produces the Building Blocks of Life
Translation
Translation is the process of synthesizing proteins from the genetic information carried by messenger RNA (mRNA). Following transcription, it constitutes the final step in the expression of genes. This process is carried out by ribosomes, complexes of protein and specialized RNA molecules. Ribosomes, transfer RNA (tRNA), and other proteins produce a chain of amino acids—the polypeptide—as the end product of translation.
Translation Produces the Building Blocks of Life

