ACY1

Aminoacylase 1, also known as ACY1, is a human gene.cite web | title = Entrez Gene: ACY1 aminoacylase 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=95| accessdate = ]

PBB_Summary
section_title =
summary_text = 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.cite web | title = Entrez Gene: ACY1 aminoacylase 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=95| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Miller YE, Drabkin H, Jones C, Fisher JH |title=Human aminoacylase-1: cloning, regional assignment to distal chromosome 3p21.1, and identification of a cross-hybridizing sequence on chromosome 18. |journal=Genomics |volume=8 |issue= 1 |pages= 149–54 |year= 1991 |pmid= 1707030 |doi=
*cite journal | author=Miller YE, Minna JD, Gazdar AF |title=Lack of expression of aminoacylase-1 in small cell lung cancer. Evidence for inactivation of genes encoded by chromosome 3p. |journal=J. Clin. Invest. |volume=83 |issue= 6 |pages= 2120–4 |year= 1989 |pmid= 2542383 |doi=
*cite journal | author=Voss R, Lerer I, Povey S, "et al." |title=Confirmation and further regional assignment of aminoacylase 1 (acy-1) on human chromosome 3 using a simplified detection method. |journal=Ann. Hum. Genet. |volume=44 |issue= Pt 1 |pages= 1–9 |year= 1982 |pmid= 6948533 |doi=
*cite journal | author=Mitta M, Kato I, Tsunasawa S |title=The nucleotide sequence of human aminoacylase-1. |journal=Biochim. Biophys. Acta |volume=1174 |issue= 2 |pages= 201–3 |year= 1993 |pmid= 8357837 |doi=
*cite journal | author=Cook RM, Burke BJ, Buchhagen DL, "et al." |title=Human aminoacylase-1. Cloning, sequence, and expression analysis of a chromosome 3p21 gene inactivated in small cell lung cancer. |journal=J. Biol. Chem. |volume=268 |issue= 23 |pages= 17010–7 |year= 1993 |pmid= 8394326 |doi=
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899
*cite journal | author=Lindner HA, Lunin VV, Alary A, "et al." |title=Essential roles of zinc ligation and enzyme dimerization for catalysis in the aminoacylase-1/M20 family. |journal=J. Biol. Chem. |volume=278 |issue= 45 |pages= 44496–504 |year= 2004 |pmid= 12933810 |doi= 10.1074/jbc.M304233200
*cite journal | author=Gerhard DS, Wagner L, Feingold EA, "et al." |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504
*cite journal | author=Rual JF, Venkatesan K, Hao T, "et al." |title=Towards a proteome-scale map of the human protein-protein interaction network. |journal=Nature |volume=437 |issue= 7062 |pages= 1173–8 |year= 2005 |pmid= 16189514 |doi= 10.1038/nature04209
*cite journal | author=Van Coster RN, Gerlo EA, Giardina TG, "et al." |title=Aminoacylase I deficiency: a novel inborn error of metabolism. |journal=Biochem. Biophys. Res. Commun. |volume=338 |issue= 3 |pages= 1322–6 |year= 2006 |pmid= 16274666 |doi= 10.1016/j.bbrc.2005.10.126
*cite journal | author=Sass JO, Mohr V, Olbrich H, "et al." |title=Mutations in ACY1, the gene encoding aminoacylase 1, cause a novel inborn error of metabolism. |journal=Am. J. Hum. Genet. |volume=78 |issue= 3 |pages= 401–9 |year= 2006 |pmid= 16465618 |doi= 10.1086/500563
*cite journal | author=Figueiredo EL, Garcia Leão FV, De Oliveira LV, "et al." |title=The amidase activity of human tissue kallikrein is significantly lower in the urine of patients with systolic heart failure. |journal=J. Card. Fail. |volume=12 |issue= 8 |pages= 653–8 |year= 2006 |pmid= 17045186 |doi= 10.1016/j.cardfail.2006.06.004

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