메뉴 건너뛰기




Volumn 46, Issue 22, 2007, Pages 6617-6627

Mutagenesis of lysine 62, asparagine 64, and conserved region 1 reduces the activity of human ecto-ATPase (NTPDase 2)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATION ANALYSIS; CELLS; ENZYME ACTIVITY; GENE EXPRESSION; MUTAGENESIS;

EID: 34249895283     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi700036e     Document Type: Article
Times cited : (11)

References (44)
  • 1
    • 33846436678 scopus 로고    scopus 로고
    • The E-NTPDase family of ectonucleotidases: Structure function relationships and pathophysiological significance
    • Robson, S. C., Sévigny, J., and Zimmermann, H. (2006) The E-NTPDase family of ectonucleotidases: structure function relationships and pathophysiological significance, Purinergic Signaling 2, 409-430
    • (2006) Purinergic Signaling , vol.2 , pp. 409-430
    • Robson, S.C.1    Sévigny, J.2    Zimmermann, H.3
  • 2
    • 0030034867 scopus 로고    scopus 로고
    • Purification and cloning of a soluble ATP-diphosphohydrolase (apyrase) from potato tubers (Solanum tuberosum)
    • Handa, M., and Guidotti, G. (1996) Purification and cloning of a soluble ATP-diphosphohydrolase (apyrase) from potato tubers (Solanum tuberosum), Biochem. Biophys. Res. Commun. 218, 916-923.
    • (1996) Biochem. Biophys. Res. Commun , vol.218 , pp. 916-923
    • Handa, M.1    Guidotti, G.2
  • 3
    • 0029811585 scopus 로고    scopus 로고
    • Partial purification and immunohistochemical localization of ATP diphosphohydrolase from Schistosoma monsoni. Immunological cross-reactivities with potato apyrase and Toxoplasma gondii nucleoside triphosphate hydrolase
    • Vasconcelos, E. G., Ferreira, S. T., de Carvalho, T. M. U., de Souza, W., Kettlun, A. M., Mancilla, M., Valenzuela, M. A., and Verjovski-Almeida, S. (1996) Partial purification and immunohistochemical localization of ATP diphosphohydrolase from Schistosoma monsoni. Immunological cross-reactivities with potato apyrase and Toxoplasma gondii nucleoside triphosphate hydrolase, J. Biol. Chem. 271, 22139-22145.
    • (1996) J. Biol. Chem , vol.271 , pp. 22139-22145
    • Vasconcelos, E.G.1    Ferreira, S.T.2    de Carvalho, T.M.U.3    de Souza, W.4    Kettlun, A.M.5    Mancilla, M.6    Valenzuela, M.A.7    Verjovski-Almeida, S.8
  • 4
    • 33745047764 scopus 로고    scopus 로고
    • Molecular cloning and characterization of expressed human ecto-nucleoside triphosphate diphosphohydrolase 8 (E-NTPDase 8) and its soluble extracellular domain
    • Knowles, A. F., and Li, C. (2006) Molecular cloning and characterization of expressed human ecto-nucleoside triphosphate diphosphohydrolase 8 (E-NTPDase 8) and its soluble extracellular domain, Biochemists 45, 7323-7333.
    • (2006) Biochemists , vol.45 , pp. 7323-7333
    • Knowles, A.F.1    Li, C.2
  • 5
    • 0023821490 scopus 로고
    • 2+-ATPase activities in human hepatoma cells
    • 2+-ATPase activities in human hepatoma cells, Arch. Biochem. Biophys. 263, 264-271.
    • (1988) Arch. Biochem. Biophys , vol.263 , pp. 264-271
    • Knowles, A.F.1
  • 6
    • 0028173613 scopus 로고
    • Prevalence of the mercurial-sensitive ecto-ATPase in human small cell lung carcinoma: Characterization and partial purification
    • Shi, X-J., and Knowles, A. F. (1994) Prevalence of the mercurial-sensitive ecto-ATPase in human small cell lung carcinoma: characterization and partial purification, Arch. Biochem. Biophys. 315, 177-184.
    • (1994) Arch. Biochem. Biophys , vol.315 , pp. 177-184
    • Shi, X.-J.1    Knowles, A.F.2
  • 7
    • 0032862590 scopus 로고    scopus 로고
    • Functional expression of a cDNA encoding a human ecto-ATPase
    • Mateo, J., Harden, K., and Boyer, J. L. (1999) Functional expression of a cDNA encoding a human ecto-ATPase, Br. J. Pharmacol. 128, 396-402.
    • (1999) Br. J. Pharmacol , vol.128 , pp. 396-402
    • Mateo, J.1    Harden, K.2    Boyer, J.L.3
  • 8
    • 0037065699 scopus 로고    scopus 로고
    • Transmembrane domains confer different substrate specificities and adenosine diphosphate hydrolysis mechanisms on CD39, CD39L1, and chimeras
    • Grinthal, A., and Guidotti, G. (2002) Transmembrane domains confer different substrate specificities and adenosine diphosphate hydrolysis mechanisms on CD39, CD39L1, and chimeras, Biochemists 41, 1947-1956.
    • (2002) Biochemists , vol.41 , pp. 1947-1956
    • Grinthal, A.1    Guidotti, G.2
  • 9
    • 0141540462 scopus 로고    scopus 로고
    • Enzymatic and transcriptional regulation of human ecto-ATPase/E-NTPDase 2
    • Knowles, A. F., and Chiang, W.-C. (2003) Enzymatic and transcriptional regulation of human ecto-ATPase/E-NTPDase 2, Arch. Biochem. Biophys. 418, 217-227.
    • (2003) Arch. Biochem. Biophys , vol.418 , pp. 217-227
    • Knowles, A.F.1    Chiang, W.-C.2
  • 10
    • 0141994772 scopus 로고    scopus 로고
    • 399 for processing of the human ecto-ATPase (NTPDase2) and its implications for determination of the activities of splice variants of the enzyme
    • 399 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, 39960-39968.
    • (2003) J. Biol. Chem , vol.278 , pp. 39960-39968
    • Mateo, J.1    Kreda, S.2    Henry, C.E.3    Harden, T.K.4    Boyer, J.L.5
  • 11
    • 0001607723 scopus 로고
    • Distantly related sequences in the α- and β-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold
    • Walker, J. E., Saraste, M., Runswick, M. J., and Gay, N. J. (1982) Distantly related sequences in the α- and β-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold, EMBO J. 1, 945-951.
    • (1982) EMBO J , vol.1 , pp. 945-951
    • Walker, J.E.1    Saraste, M.2    Runswick, M.J.3    Gay, N.J.4
  • 12
    • 0028279385 scopus 로고
    • The functions and consensus motifs of nine types of peptide segments that form different types of nucleotide-binding sites
    • Traut, T. W. (1994) The functions and consensus motifs of nine types of peptide segments that form different types of nucleotide-binding sites, Eur. J. Biochem. 222, 9-19.
    • (1994) Eur. J. Biochem , vol.222 , pp. 9-19
    • Traut, T.W.1
  • 13
    • 0026687729 scopus 로고
    • An ATPase domain common to prokaryotic cell cycle proteins, sugar kinases, actin, and hsp70 heat shock proteins
    • Bork, P., Sander, C., and Valencia, A. (1992) An ATPase domain common to prokaryotic cell cycle proteins, sugar kinases, actin, and hsp70 heat shock proteins, Proc. Natl. Acad. Sci. U.S.A. 89, 7290-7294.
    • (1992) Proc. Natl. Acad. Sci. U.S.A , vol.89 , pp. 7290-7294
    • Bork, P.1    Sander, C.2    Valencia, A.3
  • 14
    • 0027463380 scopus 로고    scopus 로고
    • Holmes, K. C., Sander, C., and Valencia, A. (1993) A new ATP-binding fold in actin, hexokinase, and hsc 70, Trends Cell. Biol. 3, 53-59.
    • Holmes, K. C., Sander, C., and Valencia, A. (1993) A new ATP-binding fold in actin, hexokinase, and hsc 70, Trends Cell. Biol. 3, 53-59.
  • 15
    • 0033524467 scopus 로고    scopus 로고
    • Site-directed mutagenesis of a human brain ecto-apyrase: Evidence that the E-type ATPases are related to the actin/heat shock/sugar kinase superfamily
    • Smith, T. M., and Kirley, T. L. (1999) Site-directed mutagenesis of a human brain ecto-apyrase: evidence that the E-type ATPases are related to the actin/heat shock/sugar kinase superfamily, Biochemistry 38, 321-328.
    • (1999) Biochemistry , vol.38 , pp. 321-328
    • Smith, T.M.1    Kirley, T.L.2
  • 16
    • 0035799316 scopus 로고    scopus 로고
    • Site-directed mutagenesis of human nucleoside triphosphate diphosphohydrolase 3: The importance of residues in the apyrase conserved regions
    • Yang, F., Hicks-Berger, C. A., Smith, T. M., and Kirley, T. L. (2001) Site-directed mutagenesis of human nucleoside triphosphate diphosphohydrolase 3: the importance of residues in the apyrase conserved regions, Biochemists 40, 3943-3950.
    • (2001) Biochemists , vol.40 , pp. 3943-3950
    • Yang, F.1    Hicks-Berger, C.A.2    Smith, T.M.3    Kirley, T.L.4
  • 17
    • 20444412704 scopus 로고    scopus 로고
    • Conserved lysine 79 is important for activity of ecto-nucleoside triphosphate diphosphohydrolase 3 (NTPDase3)
    • Basu, S., Murphy-Piedmonte, D. M., and Kirley, T. L. (2004) Conserved lysine 79 is important for activity of ecto-nucleoside triphosphate diphosphohydrolase 3 (NTPDase3), Purinergic Signalling 1, 51-58.
    • (2004) Purinergic Signalling , vol.1 , pp. 51-58
    • Basu, S.1    Murphy-Piedmonte, D.M.2    Kirley, T.L.3
  • 18
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4, Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 19
    • 0037404803 scopus 로고    scopus 로고
    • Asparagine 81, an invariant glycosylation site near apyrase conserved region 1, is essential for full enzymatic activity of ecto-nucleoside triphospahte diphosphohydrolase 3
    • Murphy, D. M., and Kirley, T. L. (2003) Asparagine 81, an invariant glycosylation site near apyrase conserved region 1, is essential for full enzymatic activity of ecto-nucleoside triphospahte diphosphohydrolase 3, Arch. Biochem. Biophys. 413, 107-115.
    • (2003) Arch. Biochem. Biophys , vol.413 , pp. 107-115
    • Murphy, D.M.1    Kirley, T.L.2
  • 20
    • 0035499439 scopus 로고    scopus 로고
    • Site-directed mutagenesis of human nucleoside triphosphate diphosphohydrolase 3: The importance of conserved glycine residues and the identification of additional conserved protein motifs in eNTPDases
    • Kirley, T. L., Yang, F., and Ivanenkov, V. V. (2001) Site-directed mutagenesis of human nucleoside triphosphate diphosphohydrolase 3: the importance of conserved glycine residues and the identification of additional conserved protein motifs in eNTPDases, Arch. Biochem. Biophys. 395, 94-102.
    • (2001) Arch. Biochem. Biophys , vol.395 , pp. 94-102
    • Kirley, T.L.1    Yang, F.2    Ivanenkov, V.V.3
  • 22
    • 33845702620 scopus 로고    scopus 로고
    • The structure of the nucleoside triphosphate diphosphohydrolases (NTPDases) as revealed by mutagenic and computational modeling analyses
    • Kirley, T. L., Crawford, P. A., and Smith, T. M. (2006) The structure of the nucleoside triphosphate diphosphohydrolases (NTPDases) as revealed by mutagenic and computational modeling analyses, Purinergic Signalling 2, 379-389.
    • (2006) Purinergic Signalling , vol.2 , pp. 379-389
    • Kirley, T.L.1    Crawford, P.A.2    Smith, T.M.3
  • 23
    • 0034643922 scopus 로고    scopus 로고
    • Site-directed mutagenesis of human endothelial cell ecto-ADPase/soluble CD 39: Requirement of glutamate 174 and serine 218 for enzyme activity and inhibition of platelet recruitment
    • Drosopoulos, J. H. F., Broekman, M. J., Islam, N., Maliszewski, C. R., Gayle, R. B., and Marcus, A. J. (2000) Site-directed mutagenesis of human endothelial cell ecto-ADPase/soluble CD 39: requirement of glutamate 174 and serine 218 for enzyme activity and inhibition of platelet recruitment, Biochemistry 39, 6936-6943.
    • (2000) Biochemistry , vol.39 , pp. 6936-6943
    • Drosopoulos, J.H.F.1    Broekman, M.J.2    Islam, N.3    Maliszewski, C.R.4    Gayle, R.B.5    Marcus, A.J.6
  • 24
    • 0036400690 scopus 로고    scopus 로고
    • 2+ utilization by soluble human CD39/ecto-nucleotidase
    • 2+ utilization by soluble human CD39/ecto-nucleotidase, Arch. Biochem. Biophys. 406, 85-95.
    • (2002) Arch. Biochem. Biophys , vol.406 , pp. 85-95
    • Drosopoulos, J.H.F.1
  • 25
    • 0040736282 scopus 로고    scopus 로고
    • Mutagenesis of two conserved tryptophan residues of the E-type ATPases: Inactivation and conversion of an ecto-apyrase to an ecto-NTPase
    • Smith, T. M., Carl, S. A. L., and Kirley, T. L. (1999) Mutagenesis of two conserved tryptophan residues of the E-type ATPases: inactivation and conversion of an ecto-apyrase to an ecto-NTPase, Biochemists 38, 5849-5857.
    • (1999) Biochemists , vol.38 , pp. 5849-5857
    • Smith, T.M.1    Carl, S.A.L.2    Kirley, T.L.3
  • 26
    • 0027408171 scopus 로고
    • Crystal structure of the catalytic subunit of cAMP-dependent protein kinase complexed with MgATP and peptide inhibitor
    • Zheng, J., Knighton, D. R., Ten Eyck, L. F., Karlsson, R., Xuong, N.-H., Taylor, S. S., and Sowadski, J. M. (1993) Crystal structure of the catalytic subunit of cAMP-dependent protein kinase complexed with MgATP and peptide inhibitor, Biochemists 32, 2154-2161.
    • (1993) Biochemists , vol.32 , pp. 2154-2161
    • Zheng, J.1    Knighton, D.R.2    Ten Eyck, L.F.3    Karlsson, R.4    Xuong, N.-H.5    Taylor, S.S.6    Sowadski, J.M.7
  • 27
    • 0028240468 scopus 로고
    • Structural basis of the 70-kilodalton heat shock cognate protein hydrolytic activity. II. Structure of the active site with ADP or ATP bound to the wild type and mutant ATPase fragment
    • Flaherty, K. M., Wilbanks, S. M., Deluca-Flaherty, C., and McKay, D. B. (1994) Structural basis of the 70-kilodalton heat shock cognate protein hydrolytic activity. II. Structure of the active site with ADP or ATP bound to the wild type and mutant ATPase fragment, J. Biol. Chem. 269, 12899-12907.
    • (1994) J. Biol. Chem , vol.269 , pp. 12899-12907
    • Flaherty, K.M.1    Wilbanks, S.M.2    Deluca-Flaherty, C.3    McKay, D.B.4
  • 29
    • 3242888769 scopus 로고    scopus 로고
    • Crystal structure of the calcium pump with a bound ATP analogue
    • Toyoshima, C., and Mizutani, T. (2004) Crystal structure of the calcium pump with a bound ATP analogue, Nature 430, 529-535.
    • (2004) Nature , vol.430 , pp. 529-535
    • Toyoshima, C.1    Mizutani, T.2
  • 33
    • 0023036891 scopus 로고
    • Studies on the transverse tubule membrane Mg-ATPase. Lectcin-induced alterations of kinetic behavior
    • Moulton, M. P., Sabbadini, R. A., Norton, K. C., and Dahms, A. S. (1986) Studies on the transverse tubule membrane Mg-ATPase. Lectcin-induced alterations of kinetic behavior, J. Biol. Chem. 261, 12244-12251.
    • (1986) J. Biol. Chem , vol.261 , pp. 12244-12251
    • Moulton, M.P.1    Sabbadini, R.A.2    Norton, K.C.3    Dahms, A.S.4
  • 34
    • 0030018168 scopus 로고    scopus 로고
    • Control of membrane ecto-ATPase by oligomerization state: Intermolecular cross-linking modulates ATPase activity
    • Stout, J. G., and Kirley, T. L. (1996) Control of membrane ecto-ATPase by oligomerization state: intermolecular cross-linking modulates ATPase activity, Biochemists 35, 8289-8298.
    • (1996) Biochemists , vol.35 , pp. 8289-8298
    • Stout, J.G.1    Kirley, T.L.2
  • 35
    • 0141988880 scopus 로고    scopus 로고
    • Bacterial expression, characterization, and disulfide bond determination of soluble human NTPDase6 (CD39L2) nucleotidase: Implications for structure and function
    • Ivanenkov, V. V., Murphy-Piedmonte, D. M., and Kirley, T. L (2003) Bacterial expression, characterization, and disulfide bond determination of soluble human NTPDase6 (CD39L2) nucleotidase: implications for structure and function, Biochemists 42, 11726-11735.
    • (2003) Biochemists , vol.42 , pp. 11726-11735
    • Ivanenkov, V.V.1    Murphy-Piedmonte, D.M.2    Kirley, T.L.3
  • 36
    • 13444282350 scopus 로고    scopus 로고
    • Bacterial expression, folding, purification and characterization of soluble NTPDase5 (CD39L4) ecto-nucleotidase
    • Murphy-Piedmonte, D. M., Crawford, P. A., and Kirley, T. L. (2005) Bacterial expression, folding, purification and characterization of soluble NTPDase5 (CD39L4) ecto-nucleotidase, Biochim. Biophys. Acta 1747, 251-259.
    • (2005) Biochim. Biophys. Acta , vol.1747 , pp. 251-259
    • Murphy-Piedmonte, D.M.1    Crawford, P.A.2    Kirley, T.L.3
  • 37
    • 16344379358 scopus 로고    scopus 로고
    • N-linked oligosaccharides affect the enzymatic activity of CD39: Diverse interactions between seven N-linked glycosylation sites
    • Wu, J. J., Choi, L. E., and Guidotti, G. (2005) N-linked oligosaccharides affect the enzymatic activity of CD39: Diverse interactions between seven N-linked glycosylation sites, Mol. Biol. Cell 16, 1661-1672.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 1661-1672
    • Wu, J.J.1    Choi, L.E.2    Guidotti, G.3
  • 39
    • 0021891884 scopus 로고
    • Assembly of asparagine-linked oligosaccharides
    • Kornfeld, R., and Korfeld, S. (1985) Assembly of asparagine-linked oligosaccharides, Annu. Rev. Biochem. 54, 631-664.
    • (1985) Annu. Rev. Biochem , vol.54 , pp. 631-664
    • Kornfeld, R.1    Korfeld, S.2
  • 40
    • 0025048136 scopus 로고
    • The P loop - a common motif in ATP and GTP binding proteins
    • Saraste, M., Sibbald, P. R., and Wittinghofer, A. (1990) The P loop - a common motif in ATP and GTP binding proteins, Trends Biochem. Sci. 15, 430-434.
    • (1990) Trends Biochem. Sci , vol.15 , pp. 430-434
    • Saraste, M.1    Sibbald, P.R.2    Wittinghofer, A.3
  • 41
    • 0029948487 scopus 로고    scopus 로고
    • The sugar kinase/heat shock protein 70/actin superfamily: Implications of conserved structure for mechanism
    • Hurley, J. H. (1996) The sugar kinase/heat shock protein 70/actin superfamily: implications of conserved structure for mechanism, Annu. Rev. Biophys. Biomol. Struct. 25, 137-162.
    • (1996) Annu. Rev. Biophys. Biomol. Struct , vol.25 , pp. 137-162
    • Hurley, J.H.1
  • 42
    • 21744436486 scopus 로고    scopus 로고
    • Characterization of disulfide bonds in human nucleoside triphosphate diphosphohydrolase 3 (NTPDase 3): Implications for NTPDase structural modeling
    • Ivanenkov, V. V., Meller, J., and Kirley, T. L. (2005) Characterization of disulfide bonds in human nucleoside triphosphate diphosphohydrolase 3 (NTPDase 3): implications for NTPDase structural modeling, Biochemists 44, 8998-9012.
    • (2005) Biochemists , vol.44 , pp. 8998-9012
    • Ivanenkov, V.V.1    Meller, J.2    Kirley, T.L.3
  • 43
    • 3142666890 scopus 로고    scopus 로고
    • Structural characterization of the stringent response related exopolyphosphatase/guanosine pentaphosphate phosphohydrolase protein family
    • Kristensen, O., Laurberg, M., Liljas, A., Kastrup, J. S., and Gajhede, M. (2004) Structural characterization of the stringent response related exopolyphosphatase/guanosine pentaphosphate phosphohydrolase protein family, Biochemists 43, 8894-8900.
    • (2004) Biochemists , vol.43 , pp. 8894-8900
    • Kristensen, O.1    Laurberg, M.2    Liljas, A.3    Kastrup, J.S.4    Gajhede, M.5
  • 44
    • 0027159053 scopus 로고
    • Exopolyphosphatase and guanosine pentaphosphate phosphatase belong to the sugar kinase/actin/hsp 70 superfamily
    • Reizer, J., Reizer, A., Saier, M. H., Jr., Bork, P., and Sander, C. (1993) Exopolyphosphatase and guanosine pentaphosphate phosphatase belong to the sugar kinase/actin/hsp 70 superfamily, Trends Biochem. Sci. 18, 247-248.
    • (1993) Trends Biochem. Sci , vol.18 , pp. 247-248
    • Reizer, J.1    Reizer, A.2    Saier Jr., M.H.3    Bork, P.4    Sander, C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.