ACY1

Aminoacylase-1 is an enzyme that in humans is encoded by the ACY1 gene.

ACY1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1Q7L
Identifiers
Aliases	ACY1, ACY-1, ACY1D, HEL-S-5, aminoacylase 1
External IDs	OMIM: 104620; MGI: 87913; HomoloGene: 110440; GeneCards: ACY1; OMA:ACY1 - orthologs
Gene location (Human) Chr. Chromosome 3 (human) Band 3p21.2 Start 51,983,340 bp End 51,989,197 bp
Gene location (Mouse) Chr. Chromosome 9 (mouse) Band 9 F1|9 57.49 cM Start 106,310,180 bp End 106,315,518 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in duodenum right lobe of liver human kidney mucosa of transverse colon renal cortex right adrenal gland right adrenal cortex rectum muscle of thigh left adrenal gland Top expressed in right kidney proximal tubule yolk sac human kidney jejunum duodenum crypt of lieberkuhn of small intestine left lobe of liver embryo ectoderm More reference expression data BioGPS More reference expression data
Gene ontology Molecular function protein binding hydrolase activity metallopeptidase activity metal ion binding aminoacylase activity identical protein binding Cellular component cytoplasm cytosol extracellular exosome Biological process xenobiotic metabolic process cellular amino acid metabolic process metabolism proteolysis Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 95 109652 Ensembl ENSG00000243989 ENSMUSG00000023262 UniProt Q03154 Q99JW2 RefSeq (mRNA) NM_001198898 NM_000666 NM_001198895 NM_001198896 NM_001198897 NM_001276442 NM_025371 RefSeq (protein) NP_000657 NP_001185824 NP_001185825 NP_001185826 NP_001185827 NP_001263371 NP_079647 Location (UCSC) Chr 3: 51.98 – 51.99 Mb Chr 9: 106.31 – 106.32 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

Function

Aminoacylase-1 is a cytosolic, homodimeric, zinc-binding enzyme that catalyzes the hydrolysis of acylated L-amino acids to L-amino acids and acyl group, and has been postulated to function in the catabolism and salvage of acylated amino acids. ACY1 has been assigned to chromosome 3p21.1, a region reduced to homozygosity in small-cell lung cancer (SCLC), and its expression has been reported to be reduced or undetectable in SCLC cell lines and tumors. The amino acid sequence of human aminoacylase-1 is highly homologous to the porcine counterpart, and ACY1 is the first member of a new family of zinc-binding enzymes.

External links

• Human ACY1 genome location and ACY1 gene details page in the UCSC Genome Browser.

Further reading

• Miller YE, Minna JD, Gazdar AF (Jun 1989). "Lack of expression of aminoacylase-1 in small cell lung cancer. Evidence for inactivation of genes encoded by chromosome 3p". The Journal of Clinical Investigation. 83 (6): 2120–2124. doi:10.1172/JCI114125. PMC 303939. PMID 2542383.
• Mitta M, Kato I, Tsunasawa S (Aug 1993). "The nucleotide sequence of human aminoacylase-1". Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression. 1174 (2): 201–3. doi:10.1016/0167-4781(93)90116-u. PMID 8357837.
• Cook RM, Burke BJ, Buchhagen DL, Minna JD, Miller YE (Aug 1993). "Human aminoacylase-1. Cloning, sequence, and expression analysis of a chromosome 3p21 gene inactivated in small cell lung cancer". The Journal of Biological Chemistry. 268 (23): 17010–7. doi:10.1016/S0021-9258(19)85294-8. PMID 8394326.
• Lindner HA, Lunin VV, Alary A, Hecker R, Cygler M, Ménard R (Nov 2003). "Essential roles of zinc ligation and enzyme dimerization for catalysis in the aminoacylase-1/M20 family". The Journal of Biological Chemistry. 278 (45): 44496–44504. doi:10.1074/jbc.M304233200. PMID 12933810.
• Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (Oct 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–1178. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
• Van Coster RN, Gerlo EA, Giardina TG, Engelke UF, Smet JE, De Praeter CM, Meersschaut VA, De Meirleir LJ, Seneca SH, Devreese B, Leroy JG, Herga S, Perrier JP, Wevers RA, Lissens W (Dec 2005). "Aminoacylase I deficiency: a novel inborn error of metabolism". Biochemical and Biophysical Research Communications. 338 (3): 1322–1326. doi:10.1016/j.bbrc.2005.10.126. PMID 16274666.
• 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 (Mar 2006). "Mutations in ACY1, the gene encoding aminoacylase 1, cause a novel inborn error of metabolism". American Journal of Human Genetics. 78 (3): 401–409. doi:10.1086/500563. PMC 1380284. PMID 16465618.
• Figueiredo EL, Garcia Leão FV, De Oliveira LV, Moreira Mda C, De Souza Figueiredo AF (Oct 2006). "The amidase activity of human tissue kallikrein is significantly lower in the urine of patients with systolic heart failure". Journal of Cardiac Failure. 12 (8): 653–658. doi:10.1016/j.cardfail.2006.06.004. PMID 17045186.