메뉴 건너뛰기




Volumn 35, Issue 7, 2012, Pages 1191-1196

Molecular characterization and mutational analysis of recombinant diadenosine 5′,5″-P1,P4-tetraphosphate hydrolase from Plasmodium falciparum

Author keywords

Ap4A hydrolase; Chemotherapeutic; Diadenosine tetraphosphate; Malaria; Mutational analysis; Plasmodium

Indexed keywords

ADENOSINE PHOSPHATE; ADENOSINE TRIPHOSPHATE; ALANINE; MAGNESIUM ION; PHENYLALANINE; PROLINE; RECOMBINANT DIADENOSINE 5',5'' P1,P4 TETRAPHOSPHATE HYDROLASE; RECOMBINANT ENZYME; UNCLASSIFIED DRUG;

EID: 84863551433     PISSN: 09186158     EISSN: 13475215     Source Type: Journal    
DOI: 10.1248/bpb.b12-00165     Document Type: Article
Times cited : (4)

References (25)
  • 1
    • 79952193925 scopus 로고    scopus 로고
    • cited 14 December, 2010
    • World Health Organization. "World Malaria Report 2010.": 〈http://www.who.int/malaria/world-malaria-report-2010/ worldmalariareport2010.pdf〉, cited 14 December, 2010.
    • World Malaria Report 2010
  • 2
    • 0033796867 scopus 로고    scopus 로고
    • Synthesis of dinucleoside polyphosphates catalyzed by firefly luciferase and several ligases
    • Sillero A, Sillero MA. Synthesis of dinucleoside polyphosphates catalyzed by firefly luciferase and several ligases. Pharmacol. Ther., 87, 91-102 (2000).
    • (2000) Pharmacol. Ther. , vol.87 , pp. 91-102
    • Sillero, A.1    Sillero, M.A.2
  • 3
    • 2442582635 scopus 로고    scopus 로고
    • Analogs of diadenosine tetraphosphate (Ap4A)
    • Guranowski A. Analogs of diadenosine tetraphosphate (Ap4A). Acta Biochim. Pol., 50, 947-972 (2003).
    • (2003) Acta Biochim. Pol. , vol.50 , pp. 947-972
    • Guranowski, A.1
  • 5
    • 1342287127 scopus 로고    scopus 로고
    • 4A as signaling regulators of MITF activity in FcepsilonRI-activated mast cells
    • 4A as signaling regulators of MITF activity in FcepsilonRI-activated mast cells. Immunity, 20, 145-151 (2004).
    • (2004) Immunity , vol.20 , pp. 145-151
    • Lee, Y.N.1    Nechushtan, H.2    Figov, N.3    Razin, E.4
  • 6
    • 0020285201 scopus 로고
    • Abundant amounts of diadenosine 5′,5‴-P1,P4-tetraphosphate are present and releasable, but metabolically inactive, in human platelets
    • Flodgaard H, Klenow H. Abundant amounts of diadenosine 5′,5‴-P1,P4-tetraphosphate are present and releasable, but metabolically inactive, in human platelets. Biochem. J., 208, 737-742 (1982).
    • (1982) Biochem. J. , vol.208 , pp. 737-742
    • Flodgaard, H.1    Klenow, H.2
  • 8
    • 0010540009 scopus 로고
    • Alteration of adenyl dinucleotide metabolism by environmental stress
    • Baker JC, Jacobson MK. Alteration of adenyl dinucleotide metabolism by environmental stress. Proc. Natl. Acad. Sci. U.S.A., 83, 2350-2352 (1986).
    • (1986) Proc. Natl. Acad. Sci. U.S.A. , vol.83 , pp. 2350-2352
    • Baker, J.C.1    Jacobson, M.K.2
  • 10
    • 0037437792 scopus 로고    scopus 로고
    • The involvement of diadenosine 5′,5‴-P1,P4-tetraphosphate in cell cycle arrest and regulation of apoptosis
    • Vartanian AA, Suzuki H, Poletaev AI. The involvement of diadenosine 5′,5‴-P1,P4-tetraphosphate in cell cycle arrest and regulation of apoptosis. Biochem. Pharmacol., 65, 227-235 (2003).
    • (2003) Biochem. Pharmacol. , vol.65 , pp. 227-235
    • Vartanian, A.A.1    Suzuki, H.2    Poletaev, A.I.3
  • 11
    • 0037162392 scopus 로고    scopus 로고
    • Hint, Fhit, and GalT: Function, structure, evolution, and mechanism of three branches of the histidine triad superfamily of nucleotide hydrolases and transferases
    • Brenner C. Hint, Fhit, and GalT: function, structure, evolution, and mechanism of three branches of the histidine triad superfamily of nucleotide hydrolases and transferases. Biochemistry, 41, 9003-9014 (2002).
    • (2002) Biochemistry , vol.41 , pp. 9003-9014
    • Brenner, C.1
  • 12
    • 0042357538 scopus 로고    scopus 로고
    • Regulation of dinucleoside polyphosphate pools by the YgdP and ApaH hydrolases is essential for the ability of Salmonella enterica serovar typhimurium to invade cultured mammalian cells
    • Ismail TM, Hart CA, McLennan AG. Regulation of dinucleoside polyphosphate pools by the YgdP and ApaH hydrolases is essential for the ability of Salmonella enterica serovar typhimurium to invade cultured mammalian cells. J. Biol. Chem., 278, 32602-32607 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 32602-32607
    • Ismail, T.M.1    Hart, C.A.2    McLennan, A.G.3
  • 13
    • 0033796851 scopus 로고    scopus 로고
    • Dinucleoside polyphosphates-friend or foe?
    • McLennan AG. Dinucleoside polyphosphates-friend or foe? Pharmacol. Ther., 87, 73-89 (2000).
    • (2000) Pharmacol. Ther. , vol.87 , pp. 73-89
    • McLennan, A.G.1
  • 14
    • 0029835350 scopus 로고    scopus 로고
    • The MutT proteins or "Nudix" hydrolases, a family of versatile, widely distributed, "housecleaning" enzymes
    • Bessman MJ, Frick DN, O'Handley SF. The MutT proteins or "Nudix" hydrolases, a family of versatile, widely distributed, "housecleaning" enzymes. J. Biol. Chem., 271, 25059-25062 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 25059-25062
    • Bessman, M.J.1    Frick, D.N.2    O'Handley, S.F.3
  • 15
    • 0033796736 scopus 로고    scopus 로고
    • Specific and nonspecific enzymes involved in the catabolism of mononucleoside and dinucleoside polyphosphates
    • Guranowski A. Specific and nonspecific enzymes involved in the catabolism of mononucleoside and dinucleoside polyphosphates. Pharmacol. Ther., 87, 117-139 (2000).
    • (2000) Pharmacol. Ther. , vol.87 , pp. 117-139
    • Guranowski, A.1
  • 16
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem., 72, 248-254 (1976).
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 19
    • 41649083951 scopus 로고    scopus 로고
    • Synthesis of 2-modified aristeromycins and their analogs as potent inhibitors against Plasmodium falciparum S-adenosyl-L-homocysteine hydrolase
    • Ando T, Iwata M, Zulfiqar F, Miyamoto T, Nakanishi M, Kitade Y. Synthesis of 2-modified aristeromycins and their analogs as potent inhibitors against Plasmodium falciparum S-adenosyl-L-homocysteine hydrolase. Bioorg. Med. Chem., 16, 3809-3815 (2008).
    • (2008) Bioorg. Med. Chem. , vol.16 , pp. 3809-3815
    • Ando, T.1    Iwata, M.2    Zulfiqar, F.3    Miyamoto, T.4    Nakanishi, M.5    Kitade, Y.6
  • 20
    • 0035956260 scopus 로고    scopus 로고
    • Cloning, characterisation and crystallisation of a diadenosine 5′,5‴-P(1),P(4)-tetraphosphate pyrophosphohydrolase from Caenorhabditis elegans
    • Abdelghany HM, Gasmi L, Cartwright JL, Bailey S, Rafferty JB, McLennan AG. Cloning, characterisation and crystallisation of a diadenosine 5′,5‴-P(1),P(4)-tetraphosphate pyrophosphohydrolase from Caenorhabditis elegans. Biochim. Biophys. Acta, 1550, 27-36 (2001).
    • (2001) Biochim. Biophys. Acta , vol.1550 , pp. 27-36
    • Abdelghany, H.M.1    Gasmi, L.2    Cartwright, J.L.3    Bailey, S.4    Rafferty, J.B.5    McLennan, A.G.6
  • 21
    • 0021112845 scopus 로고
    • Catabolism of diadenosine 5′,5‴-P1,P4-tetraphosphate in procaryotes. Purification and properties of diadenosine 5′,5‴-P1, P4-tetraphosphate (symmetrical) pyrophosphohydrolase from Escherichia coli K12
    • Guranowski A, Jakubowski H, Holler E. Catabolism of diadenosine 5′,5‴-P1,P4-tetraphosphate in procaryotes. Purification and properties of diadenosine 5′,5‴-P1,P4-tetraphosphate (symmetrical) pyrophosphohydrolase from Escherichia coli K12. J. Biol. Chem., 258, 14784-14789 (1983).
    • (1983) J. Biol. Chem. , vol.258 , pp. 14784-14789
    • Guranowski, A.1    Jakubowski, H.2    Holler, E.3
  • 22
    • 0027548883 scopus 로고
    • Human placental (asymmetrical) diadenosine 5′,5‴-P1,P4- tetraphosphate hydrolase: Purification to homogeneity and some properties
    • Lazewska D, Starzyńska E, Guranowski A. Human placental (asymmetrical) diadenosine 5′,5‴-P1,P4-tetraphosphate hydrolase: purification to homogeneity and some properties. Protein Expr. Purif., 4, 45-51 (1993).
    • (1993) Protein Expr. Purif. , vol.4 , pp. 45-51
    • Lazewska, D.1    Starzyńska, E.2    Guranowski, A.3
  • 23
    • 0014010408 scopus 로고
    • Kinetic and magnetic resonance studies of the pyruvate kinase reaction. II. Complexes of enzyme, metal, and substrates
    • Mildvan AS, Cohn M. Kinetic and magnetic resonance studies of the pyruvate kinase reaction. II. Complexes of enzyme, metal, and substrates. J. Biol. Chem., 241, 1178-1193 (1966).
    • (1966) J. Biol. Chem. , vol.241 , pp. 1178-1193
    • Mildvan, A.S.1    Cohn, M.2
  • 24
    • 0028930105 scopus 로고
    • Diadenosine 5′,5‴-P1,P4-tetraphosphate hydrolase is present in human erythrocytes, leukocytes and platelets
    • Hankin S, Matthew N, Thorne H, McLennan AG. Diadenosine 5′,5‴-P1,P4-tetraphosphate hydrolase is present in human erythrocytes, leukocytes and platelets. Int. J. Biochem. Cell Biol., 27, 201-206 (1995).
    • (1995) Int. J. Biochem. Cell Biol. , vol.27 , pp. 201-206
    • Hankin, S.1    Matthew, N.2    Thorne, H.3    McLennan, A.G.4
  • 25
    • 0038813696 scopus 로고    scopus 로고
    • Analysis of the catalytic and binding residues of the diadenosine tetraphosphate pyrophosphohydrolase from Caenorhabditis elegans by site-directed mutagenesis
    • Abdelghany HM, Bailey S, Blackburn GM, Rafferty JB, McLennan AG. Analysis of the catalytic and binding residues of the diadenosine tetraphosphate pyrophosphohydrolase from Caenorhabditis elegans by site-directed mutagenesis. J. Biol. Chem., 278, 4435-4439 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 4435-4439
    • Abdelghany, H.M.1    Bailey, S.2    Blackburn, G.M.3    Rafferty, J.B.4    McLennan, A.G.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.