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Gene Review

ACY1  -  aminoacylase 1

Homo sapiens

Synonyms: ACY-1, ACY1D, Aminoacylase-1, HEL-S-5, N-acyl-L-amino-acid amidohydrolase
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Disease relevance of ACY1

  • ACY1 has been assigned to chromosome 3p21.1, a region reduced to homozygosity in small cell lung cancer (SCLC), and has been reported to exhibit reduced or absent expression in SCLC cell lines and tumors [1].
  • Structural studies of lipooligosaccharides from Haemophilus ducreyi ITM 5535, ITM 3147, and a fresh clinical isolate, ACY1: evidence for intrastrain heterogeneity with the production of mutually exclusive sialylated or elongated glycoforms [2].
  • We have focused our efforts on an analysis of chromosomal band 3p21.1 since aminoacylase-1 (ACY1), which is localized to this band, has been shown to have lower levels of expression in several small cell and non-small cell lung cancer cell lines [3].
  • In EBV transformed lymphoblasts, aminoacylase I activity was deficient [4].
  • A Zn(2+)-dependent aminoacylase mediating this cleavage was purified from Corynebacterium striatum Ax20, and the corresponding gene agaA was cloned and heterologously expressed in Escherichia coli [5].

High impact information on ACY1

  • The four currently known Ntn hydrolases (glutamine PRPP amidotransferase, penicillin acylase, the 20S proteasome and aspartylglucosaminidase) are encoded as inactive precursors, and are activated by cleavage of the peptide bond preceding the catalytic residue [6].
  • The nucleophile is cysteine in GAT, serine in penicillin acylase, and threonine in the proteasome [7].
  • The crystal structures of three amidohydrolases have been determined recently: glutamine PRPP amidotransferase (GAT), penicillin acylase, and the proteasome [7].
  • We have examined the expression of aminoacylase-1 (ACY-1), encoded by chromosome 3p21, using both an electrophoretic activity assay and a monoclonal antibody-based ELISA [8].
  • ACY-1 was undetectable in a significant number of SCLC cell lines (4/29) and tumors (1/8), but not in non-small cell lung cancer (NSCLC) cell lines (0/19) or tumors (0/9), nor in a variety of other human cell lines (0/15) or colon tumors (0/8) [8].

Chemical compound and disease context of ACY1


Biological context of ACY1

  • The genes for human aminoacylase-1 (ACY1, N-acylamino acid aminohydrolase, E.C., an enzyme in amino acid metabolism, and beta-galactosidase-A (GLB1, E.C., deficient in GM1-gangliosidosis, have been assigned to human chromosome 3 [13].
  • Aminoacylase 1 (ACY1; EC 3.5.14) is the most abundant of the aminoacylases, a class of enzymes involved in hydrolysis of N-acetylated proteins [14].
  • Two human cDNA libraries and one human genomic DNA library were screened with a previously isolated partial ACY1 cDNA to isolate a full-length transcript [1].
  • Sequence analysis of clones from each of these libraries resulted in an ACY1 cDNA of 1438 base pairs with an open reading frame of 1224-base pairs coding for a putative protein of 408 amino acids with a predicted molecular mass of 45,882 Da [1].
  • The evolutionary conservation of this gene cluster includes three adjacent human shortest regions of overlap (SROs): 3p21.1 (ACY1), 3p21.3-->p21.2 (CACNA1D), and 3p21.3 (ZNF64) [15].

Anatomical context of ACY1

  • Because ACY1 is evolutionarily conserved in fish, frog, mouse, and human and is expressed in the central nervous system (CNS) in human, a role in CNS function or development is conceivable but has yet to be demonstrated [14].
  • Southern and northern analyses of ACY1 in SCLC cell lines failed to demonstrate any gross abnormalities of the ACY1 structural gene or instances of absent or aberrantly sized mRNA, respectively [1].
  • Both ACY1 activity and this restriction fragment have been further demonstrated to be syntenic to distal 3p21.1 through the use of a panel of human-rodent somatic cell hybrids containing fragments of chromosome 3 [16].
  • A variety of human tissues, including lung, brain, liver, kidney, heart, adrenal medulla, and erythrocytes have previously been tested for ACY-1 activity and antigen; all but erythrocytes are positive [8].
  • A specific bacterial aminoacylase cleaves odorant precursors secreted in the human axilla [5].

Associations of ACY1 with chemical compounds


Other interactions of ACY1

  • 1. PCR analysis of somatic cell and radiation hybrids localized ALAS1 to the same distal region of 3p21.1 as the aminoacylase-1 gene [22].
  • They differ also from other N-acylamino acid amidohydrolases: aminoacylase (EC and aspartoacylase (EC [23].
  • Antioxidant and antimutagenic activity of mannan neoglycoconjugates: mannan-human serum albumin and mannan-penicillin G acylase [24].
  • The amino-acid sequence of a peptide resulting from limited proteolysis of the polypeptide chain with proteinase K, which was determined by microsequencing (RHEFHALRAGFALDEGLA), was found to be very similar to the corresponding sequence of porcine kidney acylase I [25].
  • Present experiments were performed on unusually tryptophan-rich protein, bacterial penicillin acylase (28 Trp per dimer of 82 kDa) and were aimed to extend these observations [26].

Analytical, diagnostic and therapeutic context of ACY1


  1. Human aminoacylase-1. Cloning, sequence, and expression analysis of a chromosome 3p21 gene inactivated in small cell lung cancer. Cook, R.M., Burke, B.J., Buchhagen, D.L., Minna, J.D., Miller, Y.E. J. Biol. Chem. (1993) [Pubmed]
  2. Structural studies of lipooligosaccharides from Haemophilus ducreyi ITM 5535, ITM 3147, and a fresh clinical isolate, ACY1: evidence for intrastrain heterogeneity with the production of mutually exclusive sialylated or elongated glycoforms. Schweda, E.K., Jonasson, J.A., Jansson, P.E. J. Bacteriol. (1995) [Pubmed]
  3. Isolation of two contigs of overlapping cosmids derived from human chromosomal band 3p21.1 and identification of 5 new 3p21.1 genes. Shridhar, V., Golembieski, W., Kamat, A., Smith, S.E., Phillips, N., Miller, O.J., Miller, Y., Smith, D.I. Somat. Cell Mol. Genet. (1994) [Pubmed]
  4. Aminoacylase I deficiency: a novel inborn error of metabolism. Van Coster, R.N., Gerlo, E.A., Giardina, T.G., Engelke, U.F., Smet, J.E., De Praeter, C.M., Meersschaut, V.A., De Meirleir, L.J., Seneca, S.H., Devreese, B., Leroy, J.G., Herga, S., Perrier, J.P., Wevers, R.A., Lissens, W. Biochem. Biophys. Res. Commun. (2005) [Pubmed]
  5. A specific bacterial aminoacylase cleaves odorant precursors secreted in the human axilla. Natsch, A., Gfeller, H., Gygax, P., Schmid, J., Acuna, G. J. Biol. Chem. (2003) [Pubmed]
  6. Autocatalytic processing of the 20S proteasome. Seemuller, E., Lupas, A., Baumeister, W. Nature (1996) [Pubmed]
  7. A protein catalytic framework with an N-terminal nucleophile is capable of self-activation. Brannigan, J.A., Dodson, G., Duggleby, H.J., Moody, P.C., Smith, J.L., Tomchick, D.R., Murzin, A.G. Nature (1995) [Pubmed]
  8. Lack of expression of aminoacylase-1 in small cell lung cancer. Evidence for inactivation of genes encoded by chromosome 3p. Miller, Y.E., Minna, J.D., Gazdar, A.F. J. Clin. Invest. (1989) [Pubmed]
  9. Chemical modification of serine at the active site of penicillin acylase from Kluyvera citrophila. Martín, J., Slade, A., Aitken, A., Arche, R., Virden, R. Biochem. J. (1991) [Pubmed]
  10. Abnormal expression of sphingomyelin acylase in atopic dermatitis: an etiologic factor for ceramide deficiency? Murata, Y., Ogata, J., Higaki, Y., Kawashima, M., Yada, Y., Higuchi, K., Tsuchiya, T., Kawainami, S., Imokawa, G. J. Invest. Dermatol. (1996) [Pubmed]
  11. Mutations of penicillin acylase residue B71 extend substrate specificity by decreasing steric constraints for substrate binding. Morillas, M., McVey, C.E., Brannigan, J.A., Ladurner, A.G., Forney, L.J., Virden, R. Biochem. J. (2003) [Pubmed]
  12. Evolution of an acylase active on cephalosporin C. Pollegioni, L., Lorenzi, S., Rosini, E., Marcone, G.L., Molla, G., Verga, R., Cabri, W., Pilone, M.S. Protein Sci. (2005) [Pubmed]
  13. Mapping of aminoacylase-1 and beta-galactosidase-A to homologous regions of human chromosome 3 and mouse chromosome 9 suggests location of additional genes. Naylor, S.L., Elliott, R.W., Brown, J.A., Shows, T.B. Am. J. Hum. Genet. (1982) [Pubmed]
  14. Mutations in ACY1, the gene encoding aminoacylase 1, cause a novel inborn error of metabolism. Sass, J.O., Mohr, V., Olbrich, H., Engelke, U., Horvath, J., Fliegauf, M., Loges, N.T., Schweitzer-Krantz, S., Moebus, R., Weiler, P., Kispert, A., Superti-Furga, A., Wevers, R.A., Omran, H. Am. J. Hum. Genet. (2006) [Pubmed]
  15. The human chromosome 3 gene cluster ACY1-CACNA1D-ZNF64-ATP2B2 is evolutionarily conserved in Ateles paniscus chamek (Platyrrhini, Primates). Seuánez, H.N., Lachtermacher, M., Canavez, F., Moreira, M.A. Cytogenet. Cell Genet. (1997) [Pubmed]
  16. Human aminoacylase-1: cloning, regional assignment to distal chromosome 3p21.1, and identification of a cross-hybridizing sequence on chromosome 18. Miller, Y.E., Drabkin, H., Jones, C., Fisher, J.H. Genomics (1990) [Pubmed]
  17. Proteins identified as targets of the acyl glucuronide metabolite of mycophenolic acid in kidney tissue from mycophenolate mofetil treated rats. Asif, A.R., Armstrong, V.W., Voland, A., Wieland, E., Oellerich, M., Shipkova, M. Biochimie (2007) [Pubmed]
  18. Confirmation and further regional assignment of aminoacylase 1 (acy-1) on human chromosome 3 using a simplified detection method. Voss, R., Lerer, I., Povey, S., Solomon, E., Bobrow, M. Ann. Hum. Genet. (1980) [Pubmed]
  19. The nucleotide sequence of human aminoacylase-1. Mitta, M., Kato, I., Tsunasawa, S. Biochim. Biophys. Acta (1993) [Pubmed]
  20. The use of immobilized enzymes in the food industry: a review. Kilara, A., Shahani, K.M. CRC critical reviews in food science and nutrition. (1979) [Pubmed]
  21. Genetic relationship between acylpeptide hydrolase and acylase, two hydrolytic enzymes with similar binding but different catalytic specificities. Jones, W.M., Scaloni, A., Bossa, F., Popowicz, A.M., Schneewind, O., Manning, J.M. Proc. Natl. Acad. Sci. U.S.A. (1991) [Pubmed]
  22. Assignment of the human housekeeping delta-aminolevulinate synthase gene (ALAS1) to chromosome band 3p21.1 by PCR analysis of somatic cell hybrids. Cotter, P.D., Drabkin, H.A., Varkony, T., Smith, D.I., Bishop, D.F. Cytogenet. Cell Genet. (1995) [Pubmed]
  23. Polymorphism of the cobalt-activated acylase in human tissues. Ziomek, E., Szewczuk, A. Acta Biochim. Pol. (1978) [Pubmed]
  24. Antioxidant and antimutagenic activity of mannan neoglycoconjugates: mannan-human serum albumin and mannan-penicillin G acylase. Krizková, L., Zitnanová, I., Mislovicová, D., Masárová, J., Sasinková, V., Duracková, Z., Krajcovic, J. Mutat. Res. (2006) [Pubmed]
  25. The rat kidney acylase I, characterization and molecular cloning. Differences with other acylases I. Giardina, T., Perrier, J., Puigserver, A. Eur. J. Biochem. (2000) [Pubmed]
  26. On the excited-state energy transfer between tryptophan residues in proteins: the case of penicillin acylase. Ercelen, S., Kazan, D., Erarslan, A., Demchenko, A.P. Biophys. Chem. (2001) [Pubmed]
  27. The pig aminoacylase 1 (ACY1) and ribosomal protein L29 (RPL29)/heparin/heparan sulfate interacting protein (HIP) genes are located together at 13q21-->q22, corresponding to human 3p21.1. Sawazaki, T., Minezawa, M. Cytogenet. Cell Genet. (1999) [Pubmed]
  28. Essential roles of zinc ligation and enzyme dimerization for catalysis in the aminoacylase-1/M20 family. Lindner, H.A., Lunin, V.V., Alary, A., Hecker, R., Cygler, M., Ménard, R. J. Biol. Chem. (2003) [Pubmed]
  29. Roles of dimerization domain residues in binding and catalysis by aminoacylase-1. Lindner, H.A., Alary, A., Boju, L.I., Sulea, T., Ménard, R. Biochemistry (2005) [Pubmed]
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