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{{ | '''Ectonucleoside triphosphate diphosphohydrolase 2''' is an [[enzyme]] that in humans is encoded by the ''ENTPD2'' [[gene]].<ref name="pmid9271669">{{cite journal | vauthors = Chadwick BP, Frischauf AM | title = Cloning and mapping of a human and mouse gene with homology to ecto-ATPase genes | journal = Mamm Genome | volume = 8 | issue = 9 | pages = 668–72 |date=Oct 1997 | pmid = 9271669 | pmc = | doi =10.1007/s003359900534 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: ENTPD2 ectonucleoside triphosphate diphosphohydrolase 2| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=954| accessdate = }}</ref> | ||
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| summary_text = The protein encoded by this gene is the type 2 enzyme of the ecto-nucleoside triphosphate diphosphohydrolase family (E-NTPDase). E-NTPDases are a family of ecto-nucleosidases that hydrolyze 5'-triphosphates. This ecto-ATPase is an integral membrane protein. Alternative splicing of this gene results in multiple transcript variants.<ref name="entrez" | | summary_text = The protein encoded by this gene is the type 2 enzyme of the ecto-nucleoside triphosphate diphosphohydrolase family (E-NTPDase). E-NTPDases are a family of ecto-nucleosidases that hydrolyze 5'-triphosphates. This ecto-ATPase is an integral membrane protein. Alternative splicing of this gene results in multiple transcript variants.<ref name="entrez" /> | ||
}} | }} | ||
It has been shown, by scientists from the [[University of Warwick]], that '''E-NTPDase2''' stimulates the growth of the [[human eye|eye]]: by testing the enzyme on tadpoles, the tadpoles were found to develop extra eyes on their body.{{Citation needed|date=May 2012}} | |||
==References== | ==References== | ||
{{reflist | {{reflist}} | ||
==Further reading== | ==Further reading== | ||
{{refbegin | 2}} | {{refbegin | 2}} | ||
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| citations = | | citations = | ||
*{{cite journal | author=Javed R | *{{cite journal | author=Javed R |title=Mutagenesis of lysine 62, asparagine 64, and conserved region 1 reduces the activity of human ecto-ATPase (NTPDase 2) |journal=Biochemistry |volume=46 |issue= 22 |pages= 6617–27 |year= 2007 |pmid= 17489562 |doi= 10.1021/bi700036e |name-list-format=vanc| author2=Yarimizu K | author3=Pelletier N | display-authors=3 | last4=Li | first4=Cheryl | last5=Knowles | first5=Aileen F. }} | ||
*{{cite journal | | *{{cite journal | vauthors=Mukasa T, Lee Y, Knowles AF |title=Either the carboxyl- or the amino-terminal region of the human ecto-ATPase (E-NTPDase 2) confers detergent and temperature sensitivity to the chicken ecto-ATP-diphosphohydrolase (E-NTPDase 8) |journal=Biochemistry |volume=44 |issue= 33 |pages= 11160–70 |year= 2005 |pmid= 16101300 |doi= 10.1021/bi050019k }} | ||
*{{cite journal | author=Jhandier MN | *{{cite journal | author=Jhandier MN |title=Portal fibroblasts regulate the proliferation of bile duct epithelia via expression of NTPDase2 |journal=J. Biol. Chem. |volume=280 |issue= 24 |pages= 22986–92 |year= 2005 |pmid= 15799977 |doi= 10.1074/jbc.M412371200 |name-list-format=vanc| author2=Kruglov EA | author3=Lavoie EG | display-authors=3 | last4=Sévigny | first4=J | last5=Dranoff | first5=JA }} | ||
*{{cite journal | author=Dranoff JA | *{{cite journal | author=Dranoff JA |title=Ectonucleotidase NTPDase2 is selectively down-regulated in biliary cirrhosis |journal=J. Investig. Med. |volume=52 |issue= 7 |pages= 475–82 |year= 2005 |pmid= 15651265 |doi=10.2310/6650.2004.00710 |name-list-format=vanc| author2=Kruglov EA | author3=Toure J | display-authors=3 | last4=Braun | first4=Norbert | last5=Zimmermann | first5=Herbert | last6=Jain | first6=Dhanpat | last7=Knowles | first7=Aileen F. | last8=Sévigny | first8=Jean }} | ||
*{{cite journal | | *{{cite journal | vauthors=Alvarado-Castillo C, Harden TK, Boyer JL |title=Regulation of P2Y1 receptor-mediated signaling by the ectonucleoside triphosphate diphosphohydrolase isozymes NTPDase1 and NTPDase2 |journal=Mol. Pharmacol. |volume=67 |issue= 1 |pages= 114–22 |year= 2005 |pmid= 15496502 |doi= 10.1124/mol.104.006908 }} | ||
*{{cite journal | author=Gerhard DS | *{{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 | | *{{cite journal | vauthors=Knowles AF, Chiang WC |title=Enzymatic and transcriptional regulation of human ecto-ATPase/E-NTPDase 2 |journal=Arch. Biochem. Biophys. |volume=418 |issue= 2 |pages= 217–27 |year= 2003 |pmid= 14522593 |doi=10.1016/j.abb.2003.08.007 }} | ||
*{{cite journal | author=Mateo J | *{{cite journal | author=Mateo J |title=Requirement of Cys399 for processing of the human ecto-ATPase (NTPDase2) and its implications for determination of the activities of splice variants of the enzyme |journal=J. Biol. Chem. |volume=278 |issue= 41 |pages= 39960–8 |year= 2003 |pmid= 12888562 |doi= 10.1074/jbc.M307854200 |name-list-format=vanc| author2=Kreda S | author3=Henry CE | display-authors=3 | last4=Harden | first4=TK | last5=Boyer | first5=JL }} | ||
*{{cite journal | author=Strausberg RL | *{{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 | | *{{cite journal | vauthors=Grinthal A, Guidotti G |title=Transmembrane domains confer different substrate specificities and adenosine diphosphate hydrolysis mechanisms on CD39, CD39L1, and chimeras |journal=Biochemistry |volume=41 |issue= 6 |pages= 1947–56 |year= 2002 |pmid= 11827541 |doi=10.1021/bi015563h }} | ||
*{{cite journal | author=Suzuki H | *{{cite journal | author=Suzuki H |title=Protein-protein interaction panel using mouse full-length cDNAs |journal=Genome Res. |volume=11 |issue= 10 |pages= 1758–65 |year= 2001 |pmid= 11591653 |doi= 10.1101/gr.180101 | pmc=311163 |name-list-format=vanc| author2=Fukunishi Y | author3=Kagawa I | display-authors=3 | last4=Saito | first4=R | last5=Oda | first5=H | last6=Endo | first6=T | last7=Kondo | first7=S | last8=Bono | first8=H | last9=Okazaki | first9=Y }} | ||
*{{cite journal | | *{{cite journal | vauthors=Mateo J, Harden TK, Boyer JL |title=Functional expression of a cDNA encoding a human ecto-ATPase |journal=Br. J. Pharmacol. |volume=128 |issue= 2 |pages= 396–402 |year= 2000 |pmid= 10510450 |doi= 10.1038/sj.bjp.0702805 | pmc=1571647 }} | ||
}} | }} | ||
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[[Category:Enzymes]] | |||
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Latest revision as of 00:31, 31 August 2017
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Ectonucleoside triphosphate diphosphohydrolase 2 is an enzyme that in humans is encoded by the ENTPD2 gene.[1][2]
The protein encoded by this gene is the type 2 enzyme of the ecto-nucleoside triphosphate diphosphohydrolase family (E-NTPDase). E-NTPDases are a family of ecto-nucleosidases that hydrolyze 5'-triphosphates. This ecto-ATPase is an integral membrane protein. Alternative splicing of this gene results in multiple transcript variants.[2]
It has been shown, by scientists from the University of Warwick, that E-NTPDase2 stimulates the growth of the eye: by testing the enzyme on tadpoles, the tadpoles were found to develop extra eyes on their body.[citation needed]
References
- ↑ Chadwick BP, Frischauf AM (Oct 1997). "Cloning and mapping of a human and mouse gene with homology to ecto-ATPase genes". Mamm Genome. 8 (9): 668–72. doi:10.1007/s003359900534. PMID 9271669.
- ↑ 2.0 2.1 "Entrez Gene: ENTPD2 ectonucleoside triphosphate diphosphohydrolase 2".
Further reading
- Javed R, Yarimizu K, Pelletier N, et al. (2007). "Mutagenesis of lysine 62, asparagine 64, and conserved region 1 reduces the activity of human ecto-ATPase (NTPDase 2)". Biochemistry. 46 (22): 6617–27. doi:10.1021/bi700036e. PMID 17489562.
- Mukasa T, Lee Y, Knowles AF (2005). "Either the carboxyl- or the amino-terminal region of the human ecto-ATPase (E-NTPDase 2) confers detergent and temperature sensitivity to the chicken ecto-ATP-diphosphohydrolase (E-NTPDase 8)". Biochemistry. 44 (33): 11160–70. doi:10.1021/bi050019k. PMID 16101300.
- Jhandier MN, Kruglov EA, Lavoie EG, et al. (2005). "Portal fibroblasts regulate the proliferation of bile duct epithelia via expression of NTPDase2". J. Biol. Chem. 280 (24): 22986–92. doi:10.1074/jbc.M412371200. PMID 15799977.
- Dranoff JA, Kruglov EA, Toure J, et al. (2005). "Ectonucleotidase NTPDase2 is selectively down-regulated in biliary cirrhosis". J. Investig. Med. 52 (7): 475–82. doi:10.2310/6650.2004.00710. PMID 15651265.
- Alvarado-Castillo C, Harden TK, Boyer JL (2005). "Regulation of P2Y1 receptor-mediated signaling by the ectonucleoside triphosphate diphosphohydrolase isozymes NTPDase1 and NTPDase2". Mol. Pharmacol. 67 (1): 114–22. doi:10.1124/mol.104.006908. PMID 15496502.
- 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.
- Knowles AF, Chiang WC (2003). "Enzymatic and transcriptional regulation of human ecto-ATPase/E-NTPDase 2". Arch. Biochem. Biophys. 418 (2): 217–27. doi:10.1016/j.abb.2003.08.007. PMID 14522593.
- Mateo J, Kreda S, Henry CE, et al. (2003). "Requirement of Cys399 for processing of the human ecto-ATPase (NTPDase2) and its implications for determination of the activities of splice variants of the enzyme". J. Biol. Chem. 278 (41): 39960–8. doi:10.1074/jbc.M307854200. PMID 12888562.
- 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.
- Grinthal A, Guidotti G (2002). "Transmembrane domains confer different substrate specificities and adenosine diphosphate hydrolysis mechanisms on CD39, CD39L1, and chimeras". Biochemistry. 41 (6): 1947–56. doi:10.1021/bi015563h. PMID 11827541.
- Suzuki H, Fukunishi Y, Kagawa I, et al. (2001). "Protein-protein interaction panel using mouse full-length cDNAs". Genome Res. 11 (10): 1758–65. doi:10.1101/gr.180101. PMC 311163. PMID 11591653.
- Mateo J, Harden TK, Boyer JL (2000). "Functional expression of a cDNA encoding a human ecto-ATPase". Br. J. Pharmacol. 128 (2): 396–402. doi:10.1038/sj.bjp.0702805. PMC 1571647. PMID 10510450.
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