N-terminal acetylation of proteins is a widespread and highly conserved process. Aminoacylase 1 is the most abundant of the aminoacylases, a class of enzymes involved in hydrolysis of N-acetylated proteins.
Aminoacylase-1 is a homodimeric zinc-binding metalloenzyme. A cytosolic enzyme with a wide range of tissue expression, it cleaves acylated L-amino acids (except L-aspartate) into L-amino acids and an acyl group. L-aspartate derivatives are cleaved by aminoacylase-2 (aspartoacylase) (MIM.608034).
References
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. Mutations in ACY1, the Gene Encoding Aminoacylase 1, Cause a Novel Inborn Error of Metabolism. Am J Hum Genet. 2006 Mar;78(3):401-9. PMID: 16465618