Biology:ACY1
 Generic protein structure example |
Aminoacylase-1 is an enzyme that in humans is encoded by the ACY1 gene.[1][2][3]
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.[3]
References
- ↑ "Human aminoacylase-1: cloning, regional assignment to distal chromosome 3p21.1, and identification of a cross-hybridizing sequence on chromosome 18". Genomics 8 (1): 149–154. Sep 1990. doi:10.1016/0888-7543(90)90237-O. PMID 1707030.
- ↑ "Confirmation and further regional assignment of aminoacylase 1 (acy-1) on human chromosome 3 using a simplified detection method". Annals of Human Genetics 44 (Pt 1): 1–9. Jul 1980. doi:10.1111/j.1469-1809.1980.tb00940.x. PMID 6948533.
- ↑ 3.0 3.1 "Entrez Gene: ACY1 aminoacylase 1". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=95.
External links
- Human ACY1 genome location and ACY1 gene details page in the UCSC Genome Browser.
Further reading
- "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. Jun 1989. doi:10.1172/JCI114125. PMID 2542383.
- "The nucleotide sequence of human aminoacylase-1". Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression 1174 (2): 201–3. Aug 1993. doi:10.1016/0167-4781(93)90116-u. PMID 8357837.
- "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. Aug 1993. doi:10.1016/S0021-9258(19)85294-8. PMID 8394326.
- "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. Nov 2003. doi:10.1074/jbc.M304233200. PMID 12933810.
- "Towards a proteome-scale map of the human protein-protein interaction network". Nature 437 (7062): 1173–1178. Oct 2005. doi:10.1038/nature04209. PMID 16189514. Bibcode: 2005Natur.437.1173R.
- "Aminoacylase I deficiency: a novel inborn error of metabolism". Biochemical and Biophysical Research Communications 338 (3): 1322–1326. Dec 2005. doi:10.1016/j.bbrc.2005.10.126. PMID 16274666.
- "Mutations in ACY1, the gene encoding aminoacylase 1, cause a novel inborn error of metabolism". American Journal of Human Genetics 78 (3): 401–409. Mar 2006. doi:10.1086/500563. PMID 16465618.
- "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. Oct 2006. doi:10.1016/j.cardfail.2006.06.004. PMID 17045186.
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