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{{ | '''Acylamino-acid-releasing enzyme''' is an [[enzyme]] that in humans is encoded by the ''APEH'' [[gene]].<ref name="pmid2392324">{{cite journal | author = Erlandsson R | 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 |date=Oct 1990 | pmid = 2392324 | pmc = | doi = |name-list-format=vanc| author2 = Bergerheim US | author3 = Boldog F | author4 = Marcsek Z | author5 = Kunimi K | author6 = Lin BY | author7 = Ingvarsson S | author8 = Castresana JS | author9 = Lee WH }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: APEH N-acylaminoacyl-peptide hydrolase| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=327| accessdate = }}</ref> | ||
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| 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 | | summary_text = This gene encodes the enzyme [[acylpeptide hydrolase]], which catalyzes the [[hydrolysis]] of the terminal [[acetylation|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 (genetics)|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 [[oxidation|oxidatively]]-damaged proteins in living cells. Deletions of this gene locus are found in various types of [[carcinoma]]s, including [[small-cell lung carcinoma]] and [[renal cell carcinoma]].<ref name="entrez" /> | ||
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==References== | ==References== | ||
{{reflist| | {{reflist}} | ||
==External links== | |||
* {{UCSC gene info|APEH}} | |||
==Further reading== | ==Further reading== | ||
{{refbegin | 2}} | {{refbegin | 2}} | ||
{{PBB_Further_reading | {{PBB_Further_reading | ||
| citations = | | citations = | ||
*{{cite journal | | *{{cite journal |vauthors=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=10.1016/0014-4835(92)90165-O }} | ||
*{{cite journal | author=Scaloni A | *{{cite journal | author=Scaloni A |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= |name-list-format=vanc| author2=Jones WM | author3=Barra D | display-authors=3 | last4=Pospischil | first4=M | last5=Sassa | first5=S | last6=Popowicz | first6=A | last7=Manning | first7=LR | last8=Schneewind | first8=O | last9=Manning | first9=JM }} | ||
*{{cite journal | author=Erlandsson R |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= |name-list-format=vanc| author2=Boldog F | author3=Persson B | display-authors=3 | last4=Zabarovsky | first4=ER | last5=Allikmets | first5=RL | last6=Sümegi | first6=J | last7=Klein | first7=G | last8=Jörnvall | first8=H }} | |||
*{{cite journal | author= | *{{cite journal | author=Jones WM |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=10.1073/pnas.88.6.2194 | pmc=51196 |name-list-format=vanc| author2=Scaloni A | author3=Bossa F | display-authors=3 | last4=Popowicz | first4=AM | last5=Schneewind | first5=O | last6=Manning | first6=JM }} | ||
*{{cite journal | author=Naylor SL |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=10.1016/0888-7543(89)90342-X |name-list-format=vanc| author2=Marshall A | author3=Hensel C | display-authors=3 | last4=Martinez | first4=P.F. | last5=Holley | first5=B. | last6=Sakaguchi | first6=A.Y. }} | |||
*{{cite journal | author= | *{{cite journal | author=Feese M |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 |name-list-format=vanc| author2=Scaloni A | author3=Jones WM | display-authors=3 | last4=Manning | first4=JM | last5=Remington | first5=SJ }} | ||
*{{cite journal | author=Mitta M |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=10.1093/dnares/3.1.31 |name-list-format=vanc| author2=Ohnogi H | author3=Mizutani S | display-authors=3 | last4=Sakiyama | first4=F | last5=Kato | first5=I | last6=Tsunasawa | first6=S }} | |||
*{{cite journal | author= | *{{cite journal | author=Scaloni A |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=10.1023/A:1021047730831 |name-list-format=vanc| author2=Ingallinella P | author3=Andolfo A | display-authors=3 | last4=Jones | first4=Wanda | last5=Marino | first5=Gennaro | last6=Manning | first6=James M. }} | ||
*{{cite journal | author=Raphel V |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=10.1016/S0167-4838(99)00087-4 |name-list-format=vanc| author2=Giardina T | author3=Guevel L | display-authors=3 | last4=Perrier | first4=J | last5=Dupuis | first5=L | last6=Guo | first6=XJ | last7=Puigserver | first7=A }} | |||
*{{cite journal | author= | *{{cite journal | author=Fujino T |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=10.1016/S0167-4838(00)00004-2 |name-list-format=vanc| author2=Watanabe K | author3=Beppu M | display-authors=3 | last4=Kikugawa | first4=K | last5=Yasuda | first5=H }} | ||
*{{cite journal |vauthors=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=10.1002/1615-9861(200203)2:3<256::AID-PROT256>3.0.CO;2-K }} | |||
*{{cite journal | author= | *{{cite journal |vauthors=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=10.1016/S0248-4900(01)01177-7 }} | ||
*{{cite journal | author=Strausberg RL |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 | pmc=139241 |name-list-format=vanc| author2=Feingold EA | author3=Grouse LH | display-authors=3 | last4=Derge | first4=JG | last5=Klausner | first5=RD | last6=Collins | first6=FS | last7=Wagner | first7=L | last8=Shenmen | first8=CM | last9=Schuler | first9=GD }} | |||
*{{cite journal | author= | *{{cite journal | author=Gerhard DS |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 | pmc=528928 |name-list-format=vanc| author2=Wagner L | author3=Feingold EA | display-authors=3 | last4=Shenmen | first4=CM | last5=Grouse | first5=LH | last6=Schuler | first6=G | last7=Klein | first7=SL | last8=Old | first8=S | last9=Rasooly | first9=R }} | ||
*{{cite journal |vauthors=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= | *{{cite journal | author=Rual JF |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 |name-list-format=vanc| author2=Venkatesan K | author3=Hao T | display-authors=3 | last4=Hirozane-Kishikawa | first4=Tomoko | last5=Dricot | first5=Amélie | last6=Li | first6=Ning | last7=Berriz | first7=Gabriel F. | last8=Gibbons | first8=Francis D. | last9=Dreze | first9=Matija }} | ||
}} | }} | ||
{{refend}} | {{refend}} | ||
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Latest revision as of 18:07, 29 August 2017
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| External IDs | GeneCards: [1] | ||||||
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| Species | Human | Mouse | |||||
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| Location (UCSC) | n/a | n/a | |||||
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Acylamino-acid-releasing enzyme is an enzyme that in humans is encoded by the APEH gene.[1][2]
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.[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. PMID 2392324.
- ↑ 2.0 2.1 "Entrez Gene: APEH N-acylaminoacyl-peptide hydrolase".
External links
- Human APEH genome location and APEH gene details page in the UCSC Genome Browser.
Further reading
- Sharma KK, Ortwerth BJ (1992). "Description of an acylpeptide hydrolase from lens". Exp. Eye Res. 54 (6): 1005–10. doi:10.1016/0014-4835(92)90165-O. 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.
- 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.
- 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. doi:10.1073/pnas.88.6.2194. PMC 51196. PMID 2006156.
- 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. PMID 2565880.
- 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.
- 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. PMID 8724851.
- 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. PMID 10395453.
- 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. PMID 10407158.
- 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. PMID 10719179.
- Richards P, Lees J (2002). "Functional proteomics using microchannel plate detectors". Proteomics. 2 (3): 256–61. doi:10.1002/1615-9861(200203)2:3<256::AID-PROT256>3.0.CO;2-K. 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. doi:10.1016/S0248-4900(01)01177-7. PMID 12000146.
- 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. PMC 139241. PMID 12477932.
- 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. PMC 528928. PMID 15489334.
- 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.
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