APEH (gene)

APEH (gene)

N-acylaminoacyl-peptide hydrolase, also known as APEH, is a human gene.cite web | title = Entrez Gene: APEH N-acylaminoacyl-peptide hydrolase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=327| accessdate = ]

section_title =
summary_text = 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.cite web | title = Entrez Gene: APEH N-acylaminoacyl-peptide hydrolase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=327| accessdate = ]


Further reading

citations =
*cite journal | author=Sharma KK, Ortwerth BJ |title=Description of an acylpeptide hydrolase from lens. |journal=Exp. Eye Res. |volume=54 |issue= 6 |pages= 1005–10 |year= 1992 |pmid= 1521574 |doi=
*cite journal | author=Scaloni A, Jones WM, Barra D, "et al." |title=Acylpeptide hydrolase: inhibitors and some active site residues of the human enzyme. |journal=J. Biol. Chem. |volume=267 |issue= 6 |pages= 3811–8 |year= 1992 |pmid= 1740429 |doi=
*cite journal | author=Erlandsson R, Boldog F, Persson B, "et al." |title=The gene from the short arm of chromosome 3, at D3F15S2, frequently deleted in renal cell carcinoma, encodes acylpeptide hydrolase. |journal=Oncogene |volume=6 |issue= 7 |pages= 1293–5 |year= 1991 |pmid= 1861871 |doi=
*cite journal | author=Jones WM, Scaloni A, Bossa F, "et al." |title=Genetic relationship between acylpeptide hydrolase and acylase, two hydrolytic enzymes with similar binding but different catalytic specificities. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=88 |issue= 6 |pages= 2194–8 |year= 1991 |pmid= 2006156 |doi=
*cite journal | author=Erlandsson R, Bergerheim US, Boldog F, "et al." |title=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). |journal=Oncogene |volume=5 |issue= 8 |pages= 1207–11 |year= 1990 |pmid= 2392324 |doi=
*cite journal | author=Naylor SL, Marshall A, Hensel C, "et al." |title=The DNF15S2 locus at 3p21 is transcribed in normal lung and small cell lung cancer. |journal=Genomics |volume=4 |issue= 3 |pages= 355–61 |year= 1989 |pmid= 2565880 |doi=
*cite journal | author=Feese M, Scaloni A, Jones WM, "et al." |title=Crystallization and preliminary X-ray studies of human erythrocyte acylpeptide hydrolase. |journal=J. Mol. Biol. |volume=233 |issue= 3 |pages= 546–9 |year= 1993 |pmid= 8411161 |doi= 10.1006/jmbi.1993.1531
*cite journal | author=Mitta M, Ohnogi H, Mizutani S, "et al." |title=The nucleotide sequence of human acylamino acid-releasing enzyme. |journal=DNA Res. |volume=3 |issue= 1 |pages= 31–5 |year= 1996 |pmid= 8724851 |doi=
*cite journal | author=Scaloni A, Ingallinella P, Andolfo A, "et al." |title=Structural investigations on human erythrocyte acylpeptide hydrolase by mass spectrometric procedures. |journal=J. Protein Chem. |volume=18 |issue= 3 |pages= 349–60 |year= 1999 |pmid= 10395453 |doi=
*cite journal | author=Raphel V, Giardina T, Guevel L, "et al." |title=Cloning, sequencing and further characterization of acylpeptide hydrolase from porcine intestinal mucosa. |journal=Biochim. Biophys. Acta |volume=1432 |issue= 2 |pages= 371–81 |year= 1999 |pmid= 10407158 |doi=
*cite journal | author=Fujino T, Watanabe K, Beppu M, "et al." |title=Identification of oxidized protein hydrolase of human erythrocytes as acylpeptide hydrolase. |journal=Biochim. Biophys. Acta |volume=1478 |issue= 1 |pages= 102–12 |year= 2000 |pmid= 10719179 |doi=
*cite journal | author=Richards P, Lees J |title=Functional proteomics using microchannel plate detectors. |journal=Proteomics |volume=2 |issue= 3 |pages= 256–61 |year= 2002 |pmid= 11921441 |doi=
*cite journal | author=Perrier J, Giardina T, Durand A, Puigserver A |title=Specific enhancement of acylase I and acylpeptide hydrolase activities by the corresponding N-acetylated substrates in primary rat hepatocyte cultures. |journal=Biol. Cell |volume=94 |issue= 1 |pages= 45–54 |year= 2002 |pmid= 12000146 |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=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=Pope SN, Lee IR |title=Yeast two-hybrid identification of prostatic proteins interacting with human sex hormone-binding globulin. |journal=J. Steroid Biochem. Mol. Biol. |volume=94 |issue= 1-3 |pages= 203–8 |year= 2005 |pmid= 15862967 |doi= 10.1016/j.jsbmb.2005.01.007
*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

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