ACY1
From Wikipedia, the free encyclopedia
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Aminoacylase 1
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| PDB rendering based on 1q7l. | ||||||||||||||
| Available structures: 1q7l | ||||||||||||||
| Identifiers | ||||||||||||||
| Symbol(s) | ACY1; ACY1D; ACYLASE | |||||||||||||
| External IDs | OMIM: 104620 MGI: 87913 HomoloGene: 37330 | |||||||||||||
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| RNA expression pattern | ||||||||||||||
| Orthologs | ||||||||||||||
| Human | Mouse | |||||||||||||
| Entrez | 95 | 109652 | ||||||||||||
| Ensembl | ENSG00000114786 | ENSMUSG00000023262 | ||||||||||||
| Uniprot | Q03154 | Q99JW2 | ||||||||||||
| Refseq | NM_000666 (mRNA) NP_000657 (protein) |
NM_025371 (mRNA) NP_079647 (protein) |
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| Location | Chr 3: 51.99 - 52 Mb | Chr 9: 106.29 - 106.3 Mb | ||||||||||||
| Pubmed search | [1] | [2] | ||||||||||||
Aminoacylase 1, also known as ACY1, is a human gene.[1]
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.[1]
[edit] References
[edit] Further reading
- Miller YE, Drabkin H, Jones C, Fisher JH (1991). "Human aminoacylase-1: cloning, regional assignment to distal chromosome 3p21.1, and identification of a cross-hybridizing sequence on chromosome 18.". Genomics 8 (1): 149–54. PMID 1707030.
- Miller YE, Minna JD, Gazdar AF (1989). "Lack of expression of aminoacylase-1 in small cell lung cancer. Evidence for inactivation of genes encoded by chromosome 3p.". J. Clin. Invest. 83 (6): 2120–4. PMID 2542383.
- Voss R, Lerer I, Povey S, et al. (1982). "Confirmation and further regional assignment of aminoacylase 1 (acy-1) on human chromosome 3 using a simplified detection method.". Ann. Hum. Genet. 44 (Pt 1): 1–9. PMID 6948533.
- Mitta M, Kato I, Tsunasawa S (1993). "The nucleotide sequence of human aminoacylase-1.". Biochim. Biophys. Acta 1174 (2): 201–3. PMID 8357837.
- Cook RM, Burke BJ, Buchhagen DL, et al. (1993). "Human aminoacylase-1. Cloning, sequence, and expression analysis of a chromosome 3p21 gene inactivated in small cell lung cancer.". J. Biol. Chem. 268 (23): 17010–7. PMID 8394326.
- Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:. PMID 12477932.
- Lindner HA, Lunin VV, Alary A, et al. (2004). "Essential roles of zinc ligation and enzyme dimerization for catalysis in the aminoacylase-1/M20 family.". J. Biol. Chem. 278 (45): 44496–504. doi:. PMID 12933810.
- Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:. PMID 15489334.
- Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network.". Nature 437 (7062): 1173–8. doi:. PMID 16189514.
- Van Coster RN, Gerlo EA, Giardina TG, et al. (2006). "Aminoacylase I deficiency: a novel inborn error of metabolism.". Biochem. Biophys. Res. Commun. 338 (3): 1322–6. doi:. PMID 16274666.
- Sass JO, Mohr V, Olbrich H, et al. (2006). "Mutations in ACY1, the gene encoding aminoacylase 1, cause a novel inborn error of metabolism.". Am. J. Hum. Genet. 78 (3): 401–9. doi:. PMID 16465618.
- Figueiredo EL, Garcia Leão FV, De Oliveira LV, et al. (2006). "The amidase activity of human tissue kallikrein is significantly lower in the urine of patients with systolic heart failure.". J. Card. Fail. 12 (8): 653–8. doi:. PMID 17045186.

