Defective ACY1 does not hydrolyse mercapturic acids

Stable Identifier
Reaction [transition]
Homo sapiens
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Cytosolic aminocyclases 1 and 3 (ACY1,3) can hydrolyse N-acylated amino acids and N-acylcysteine-S-conjugates (Lindner et al. 2003). They are functional as dimers and utilise zinc as a cofactor. Defects in ACY1 can cause aminoacylase 1 deficiency (ACY1D; MIM:609924), leading to acute encephalopathy, seizures, impaired psychomotor development and increased urinary excretion of several N-acetylated amino acids. The missense mutation R353C is associated with recessive loss-of-function phenotype and is the most common cause of enzyme deficiency (Sass et al. 2006, Sass et al. 2007).

Literature References
PubMed ID Title Journal Year
17562838 Neurological findings in aminoacylase 1 deficiency

Sass, JO, Olbrich, H, Mohr, V, Hart, C, Woldseth, B, Krywawych, S, Bjurulf, B, Lakhani, PK, Buchdahl, RM, Omran, H

Neurology 2007
16465618 Mutations in ACY1, the gene encoding aminoacylase 1, cause a novel inborn error of metabolism

Sass, JO, Mohr, V, Olbrich, H, Engelke, U, Horvath, J, Fliegauf, M, Loges, NT, Schweitzer-Krantz, S, Moebus, R, Weiler, P, Kispert, A, Superti-Furga, A, Wevers, RA, Omran, H

Am. J. Hum. Genet. 2006

Lindner, HA, Lunin, VV, Alary, A, Hecker, R, Cygler, M, Ménard, R

J. Biol. Chem. 2003
Catalyst Activity

aminoacylase activity of ACY1 mutants:Zn2+ dimer [cytosol]

Normal reaction
Functional status

Loss of function of ACY1 mutants:Zn2+ dimer [cytosol]

Name Identifier Synonyms
toxic encephalopathy DOID:3602 Neurotoxicity (disorder), neurotoxicity, neurotoxicity syndrome, neurotoxicity
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