APEH (gene)

N-acylaminoacyl-peptide hydrolase
Identifiers
Symbols	APEH ; ACPH; APH; D3F15S2; D3S48E; DNF15S2; MGC2178; OPH
External IDs	Template:OMIM5 Template:MGI HomoloGene: 1240
Gene ontology Molecular function Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Biological process Template:GNF GO
RNA expression pattern
More reference expression data
Orthologs
Template:GNF Ortholog box
Species	Human	Mouse
Entrez	n/a	n/a
Ensembl	n/a	n/a
UniProt	n/a	n/a
RefSeq (mRNA)	n/a	n/a
RefSeq (protein)	n/a	n/a
Location (UCSC)	n/a	n/a
PubMed search	n/a	n/a

N-acylaminoacyl-peptide hydrolase, also known as APEH, is a human gene.

This gene encodes the enzyme acylpeptide hydrolase, which catalyzes the hydrolysis of the terminal acetylated amino acid preferentially from small acetylated peptides. The acetyl amino acid formed by this hydrolase is further processed to acetate and a free amino acid by an aminoacylase. This gene is located within the same region of chromosome 3 (3p21) as the aminoacylase gene, and deletions at this locus are also associated with a decrease in aminoacylase activity. The acylpeptide hydrolase is a homotetrameric protein of 300 kDa with each subunit consisting of 732 amino acid residues. It can play an important role in destroying oxidatively damaged proteins in living cells. Deletions of this gene locus are found in various types of carcinomas, including small cell lung carcinoma and renal cell carcinoma.

Further reading

• Sharma KK, Ortwerth BJ (1992). "Description of an acylpeptide hydrolase from lens". Exp. Eye Res. 54 (6): 1005–10. PMID 1521574.
• Scaloni A, Jones WM, Barra D; et al. (1992). "Acylpeptide hydrolase: inhibitors and some active site residues of the human enzyme". J. Biol. Chem. 267 (6): 3811–8. PMID 1740429.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Erlandsson R, Boldog F, Persson B; et al. (1991). "The gene from the short arm of chromosome 3, at D3F15S2, frequently deleted in renal cell carcinoma, encodes acylpeptide hydrolase". Oncogene. 6 (7): 1293–5. PMID 1861871.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Jones WM, Scaloni A, Bossa F; et al. (1991). "Genetic relationship between acylpeptide hydrolase and acylase, two hydrolytic enzymes with similar binding but different catalytic specificities". Proc. Natl. Acad. Sci. U.S.A. 88 (6): 2194–8. PMID 2006156.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Erlandsson R, Bergerheim US, Boldog F; et al. (1990). "A gene near the D3F15S2 site on 3p is expressed in normal human kidney but not or only at a severely reduced level in 11 of 15 primary renal cell carcinomas (RCC)". Oncogene. 5 (8): 1207–11. PMID 2392324.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Naylor SL, Marshall A, Hensel C; et al. (1989). "The DNF15S2 locus at 3p21 is transcribed in normal lung and small cell lung cancer". Genomics. 4 (3): 355–61. PMID 2565880.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Feese M, Scaloni A, Jones WM; et al. (1993). "Crystallization and preliminary X-ray studies of human erythrocyte acylpeptide hydrolase". J. Mol. Biol. 233 (3): 546–9. doi:10.1006/jmbi.1993.1531. PMID 8411161.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Mitta M, Ohnogi H, Mizutani S; et al. (1996). "The nucleotide sequence of human acylamino acid-releasing enzyme". DNA Res. 3 (1): 31–5. PMID 8724851.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Scaloni A, Ingallinella P, Andolfo A; et al. (1999). "Structural investigations on human erythrocyte acylpeptide hydrolase by mass spectrometric procedures". J. Protein Chem. 18 (3): 349–60. PMID 10395453.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Raphel V, Giardina T, Guevel L; et al. (1999). "Cloning, sequencing and further characterization of acylpeptide hydrolase from porcine intestinal mucosa". Biochim. Biophys. Acta. 1432 (2): 371–81. PMID 10407158.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Fujino T, Watanabe K, Beppu M; et al. (2000). "Identification of oxidized protein hydrolase of human erythrocytes as acylpeptide hydrolase". Biochim. Biophys. Acta. 1478 (1): 102–12. PMID 10719179.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Richards P, Lees J (2002). "Functional proteomics using microchannel plate detectors". Proteomics. 2 (3): 256–61. PMID 11921441.
• Perrier J, Giardina T, Durand A, Puigserver A (2002). "Specific enhancement of acylase I and acylpeptide hydrolase activities by the corresponding N-acetylated substrates in primary rat hepatocyte cultures". Biol. Cell. 94 (1): 45–54. PMID 12000146.CS1 maint: Multiple names: authors list (link)
• 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:10.1073/pnas.242603899. PMID 12477932.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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:10.1101/gr.2596504. PMID 15489334.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Pope SN, Lee IR (2005). "Yeast two-hybrid identification of prostatic proteins interacting with human sex hormone-binding globulin". J. Steroid Biochem. Mol. Biol. 94 (1–3): 203–8. doi:10.1016/j.jsbmb.2005.01.007. PMID 15862967.
• 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:10.1038/nature04209. PMID 16189514.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)