Acylamino-acid-releasing enzyme is an enzyme that in humans is encoded by the APEHgene.[1][2]
This gene encodes the enzyme acylpeptide hydrolase, which catalyzes the hydrolysis of the terminal acetylatedamino 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.[2]
References
↑Erlandsson R, Bergerheim US, Boldog F, Marcsek Z, Kunimi K, Lin BY, Ingvarsson S, Castresana JS, Lee WH (Oct 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. PMID2392324.
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. PMID1740429.
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. PMID1861871.
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. doi:10.1016/0888-7543(89)90342-X. PMID2565880.
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. PMID8411161.
Mitta M, Ohnogi H, Mizutani S, et al. (1996). "The nucleotide sequence of human acylamino acid-releasing enzyme". DNA Res. 3 (1): 31–5. doi:10.1093/dnares/3.1.31. PMID8724851.
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. doi:10.1023/A:1021047730831. PMID10395453.
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. doi:10.1016/S0167-4838(99)00087-4. PMID10407158.
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. doi:10.1016/S0167-4838(00)00004-2. PMID10719179.
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. doi:10.1016/S0248-4900(01)01177-7. PMID12000146.
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. PMID15862967.
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. PMID16189514.