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Volumn 149, Issue 2, 2006, Pages 223-230

Adenosine kinase from Cryptosporidium parvum

Author keywords

Adenosine kinase; Cryptosporidium parvum; Parasite; Protozoa; Purine salvage

Indexed keywords

ADENOSINE KINASE; ADENOSINE TRIPHOSPHATE; CYTIDINE TRIPHOSPHATE; GUANOSINE TRIPHOSPHATE; URIDINE TRIPHOSPHATE;

EID: 33747811518     PISSN: 01666851     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molbiopara.2006.06.001     Document Type: Article
Times cited : (17)

References (33)
  • 1
    • 0030623684 scopus 로고    scopus 로고
    • Cryptosporidiosis: an emerging, highly infectious threat
    • Guerrant R.L. Cryptosporidiosis: an emerging, highly infectious threat. Emerg Infect Dis 3 (1997) 51-57
    • (1997) Emerg Infect Dis , vol.3 , pp. 51-57
    • Guerrant, R.L.1
  • 2
    • 0023964522 scopus 로고
    • Occurrence and significance of Cryptosporidium in water
    • Rose J.B. Occurrence and significance of Cryptosporidium in water. J Am Water Works Assoc 80 (1988) 53-58
    • (1988) J Am Water Works Assoc , vol.80 , pp. 53-58
    • Rose, J.B.1
  • 3
    • 0026358601 scopus 로고
    • Survey of potable water supplies for Cryptosporidium and Giardia
    • Rose J.B., Gerba C.P., and Jakubowski W. Survey of potable water supplies for Cryptosporidium and Giardia. Environ Sci Technol 25 (1991) 1393-1400
    • (1991) Environ Sci Technol , vol.25 , pp. 1393-1400
    • Rose, J.B.1    Gerba, C.P.2    Jakubowski, W.3
  • 4
    • 0025919022 scopus 로고
    • Occurrence of Giardia and Cryptosporidium spp. in surface water supplies
    • LeChevallier M.W., Norton W.D., and Lee R.G. Occurrence of Giardia and Cryptosporidium spp. in surface water supplies. Appl Environ Microbiol 57 (1991) 2610-2616
    • (1991) Appl Environ Microbiol , vol.57 , pp. 2610-2616
    • LeChevallier, M.W.1    Norton, W.D.2    Lee, R.G.3
  • 5
    • 0024320432 scopus 로고
    • Occurrence of Cryptosporidium in home daycare centers in west-central Colorado
    • Diers J., and McCallister G.L. Occurrence of Cryptosporidium in home daycare centers in west-central Colorado. J Parasitol 75 (1989) 637-638
    • (1989) J Parasitol , vol.75 , pp. 637-638
    • Diers, J.1    McCallister, G.L.2
  • 6
    • 0042853713 scopus 로고    scopus 로고
    • Purine and pyrimidine transport and metabolism
    • Marr J.J., Nilsen T.W., and Komuniecki R.W. (Eds), Elsevier Science Ltd., London
    • Carter N.S., Rager N., and Ullman B. Purine and pyrimidine transport and metabolism. In: Marr J.J., Nilsen T.W., and Komuniecki R.W. (Eds). Molecular medical parasitology vol. 1 (2003), Elsevier Science Ltd., London 197-223
    • (2003) Molecular medical parasitology , vol.1 , pp. 197-223
    • Carter, N.S.1    Rager, N.2    Ullman, B.3
  • 8
    • 0023037698 scopus 로고
    • Cryptosporidium spp. and cryptosporidiosis
    • Fayer R., and Ungar B.L. Cryptosporidium spp. and cryptosporidiosis. Microbiol Rev 50 (1986) 458-483
    • (1986) Microbiol Rev , vol.50 , pp. 458-483
    • Fayer, R.1    Ungar, B.L.2
  • 9
    • 0029078714 scopus 로고
    • Massive outbreak of waterborne cryptosporidium infection in Milwaukee, Wisconsin: recurrence of illness and risk of secondary transmission
    • MacKenzie W.R., Schell W.L., Blair K.A., et al. Massive outbreak of waterborne cryptosporidium infection in Milwaukee, Wisconsin: recurrence of illness and risk of secondary transmission. Clin Infect Dis 21 (1995) 57-62
    • (1995) Clin Infect Dis , vol.21 , pp. 57-62
    • MacKenzie, W.R.1    Schell, W.L.2    Blair, K.A.3
  • 10
    • 0031442426 scopus 로고    scopus 로고
    • Cryptosporidiosis-associated mortality following a massive waterborne outbreak in Milwaukee, Wisconsin
    • Hoxie N.J., Davis J.P., Vergeront J.M., Nashold R.D., and Blair K.A. Cryptosporidiosis-associated mortality following a massive waterborne outbreak in Milwaukee, Wisconsin. Am J Public Health 87 (1997) 2032-2035
    • (1997) Am J Public Health , vol.87 , pp. 2032-2035
    • Hoxie, N.J.1    Davis, J.P.2    Vergeront, J.M.3    Nashold, R.D.4    Blair, K.A.5
  • 11
    • 2442468577 scopus 로고    scopus 로고
    • A review of chemotherapeutic approaches to the treatment of cryptosporidiosis
    • Armson A., Thompson R.C., and Reynoldson J.A. A review of chemotherapeutic approaches to the treatment of cryptosporidiosis. Expert Rev Anti Infect Ther 1 (2003) 297-305
    • (2003) Expert Rev Anti Infect Ther , vol.1 , pp. 297-305
    • Armson, A.1    Thompson, R.C.2    Reynoldson, J.A.3
  • 12
    • 11144353587 scopus 로고    scopus 로고
    • Complete genome sequence of the apicomplexan, Cryptosporidium parvum
    • Abrahamsen M.S., Templeton T.J., Enomoto S., et al. Complete genome sequence of the apicomplexan, Cryptosporidium parvum. Science 304 (2004) 441-445
    • (2004) Science , vol.304 , pp. 441-445
    • Abrahamsen, M.S.1    Templeton, T.J.2    Enomoto, S.3
  • 13
    • 1542267798 scopus 로고    scopus 로고
    • Gene transfer in the evolution of parasite nucleotide biosynthesis
    • Striepen B., Pruijssers A.J., Huang J., et al. Gene transfer in the evolution of parasite nucleotide biosynthesis. Proc Natl Acad Sci USA 101 (2004) 3154-3159
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 3154-3159
    • Striepen, B.1    Pruijssers, A.J.2    Huang, J.3
  • 14
    • 0001529564 scopus 로고
    • Enzymatic phosphorylation of adenosine and 2,6-diaminopurine riboside
    • Kornberg A., and Pricer Jr. W.E. Enzymatic phosphorylation of adenosine and 2,6-diaminopurine riboside. J Biol Chem 193 (1951) 481-495
    • (1951) J Biol Chem , vol.193 , pp. 481-495
    • Kornberg, A.1    Pricer Jr., W.E.2
  • 15
    • 0001653501 scopus 로고
    • The enzymatic synthesis of adenylic acid, adenosine kinase
    • Caputto R. The enzymatic synthesis of adenylic acid, adenosine kinase. J Biol Chem 189 (1951) 801-814
    • (1951) J Biol Chem , vol.189 , pp. 801-814
    • Caputto, R.1
  • 16
    • 0014197765 scopus 로고
    • Some properties of partially purified mammalian adenosine kinase
    • Lindberg B., Klenow H., and Hansen K. Some properties of partially purified mammalian adenosine kinase. J Biol Chem 242 (1967) 350-356
    • (1967) J Biol Chem , vol.242 , pp. 350-356
    • Lindberg, B.1    Klenow, H.2    Hansen, K.3
  • 17
    • 0027968068 scopus 로고
    • CLUSTALW: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson J.D., Higgins D.G., and Gibson T.J. CLUSTALW: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucl Acids Res 22 (1994) 4673-4680
    • (1994) Nucl Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 18
    • 0342614926 scopus 로고    scopus 로고
    • Codon usage tabulated from international DNA sequence databases: status for the year
    • Nakamura Y., Gojobori T., and Ikemura T. Codon usage tabulated from international DNA sequence databases: status for the year. Nucl Acids Res 28 (2000) 292
    • (2000) Nucl Acids Res , vol.28 , pp. 292
    • Nakamura, Y.1    Gojobori, T.2    Ikemura, T.3
  • 19
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72 (1976) 248-254
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 20
    • 0019324594 scopus 로고
    • Further purification of adenosine kinase from rat heart using affinity and ion-exchange chromatography
    • de Jong J.W., Keijzer E., Uitendaal M.P., and Harmsen E. Further purification of adenosine kinase from rat heart using affinity and ion-exchange chromatography. Anal Biochem 101 (1980) 407-412
    • (1980) Anal Biochem , vol.101 , pp. 407-412
    • de Jong, J.W.1    Keijzer, E.2    Uitendaal, M.P.3    Harmsen, E.4
  • 21
    • 19944428454 scopus 로고    scopus 로고
    • The crystal structure of human adenylate kinase 6: an adenylate kinase localized to the cell nucleus
    • Ren H., Wang L., Bennett M., et al. The crystal structure of human adenylate kinase 6: an adenylate kinase localized to the cell nucleus. Proc Natl Acad Sci USA 102 (2005) 303-308
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 303-308
    • Ren, H.1    Wang, L.2    Bennett, M.3
  • 22
    • 0000292524 scopus 로고
    • A note on the kinetics of enzyme action
    • Briggs G.E., and Haldane J.B.S. A note on the kinetics of enzyme action. Biochem J 19 (1925) 338-339
    • (1925) Biochem J , vol.19 , pp. 338-339
    • Briggs, G.E.1    Haldane, J.B.S.2
  • 23
    • 0025828793 scopus 로고
    • Nucleotide sequence of the Rhodobacter capsulatus fruK gene, which encodes fructose-1-phosphate kinase: evidence for a kinase superfamily including both phosphofructokinases of Escherichia coli
    • Wu L.F., Reizer A., Reizer J., Cai B., Tomich J.M., and Saier Jr. M.H. Nucleotide sequence of the Rhodobacter capsulatus fruK gene, which encodes fructose-1-phosphate kinase: evidence for a kinase superfamily including both phosphofructokinases of Escherichia coli. J Bacteriol 173 (1991) 3117-3127
    • (1991) J Bacteriol , vol.173 , pp. 3117-3127
    • Wu, L.F.1    Reizer, A.2    Reizer, J.3    Cai, B.4    Tomich, J.M.5    Saier Jr., M.H.6
  • 24
    • 0027404023 scopus 로고
    • Convergent evolution of similar enzymatic function on different protein folds: the hexokinase, ribokinase, and galactokinase families of sugar kinases
    • Bork P., Sander C., and Valencia A. Convergent evolution of similar enzymatic function on different protein folds: the hexokinase, ribokinase, and galactokinase families of sugar kinases. Protein Sci 2 (1993) 31-40
    • (1993) Protein Sci , vol.2 , pp. 31-40
    • Bork, P.1    Sander, C.2    Valencia, A.3
  • 25
    • 0034685603 scopus 로고    scopus 로고
    • Crystal structures of Toxoplasma gondii adenosine kinase reveal a novel catalytic mechanism and prodrug binding
    • Schumacher M.A., Scott D.M., Mathews I.I., et al. Crystal structures of Toxoplasma gondii adenosine kinase reveal a novel catalytic mechanism and prodrug binding. J Mol Biol 298 (2000) 875-893
    • (2000) J Mol Biol , vol.298 , pp. 875-893
    • Schumacher, M.A.1    Scott, D.M.2    Mathews, I.I.3
  • 26
    • 0032506161 scopus 로고    scopus 로고
    • Structure of human adenosine kinase at 1.5 A resolution
    • Mathews I.I., Erion M.D., and Ealick S.E. Structure of human adenosine kinase at 1.5 A resolution. Biochemistry 37 (1998) 15607-15620
    • (1998) Biochemistry , vol.37 , pp. 15607-15620
    • Mathews, I.I.1    Erion, M.D.2    Ealick, S.E.3
  • 27
    • 22444433045 scopus 로고    scopus 로고
    • Functional characterization of an evolutionarily distinct phosphopantetheinyl transferase in the apicomplexan Cryptosporidium parvum
    • Cai X., Herschap D., and Zhu G. Functional characterization of an evolutionarily distinct phosphopantetheinyl transferase in the apicomplexan Cryptosporidium parvum. Eukaryot Cell 4 (2005) 1211-1220
    • (2005) Eukaryot Cell , vol.4 , pp. 1211-1220
    • Cai, X.1    Herschap, D.2    Zhu, G.3
  • 28
    • 0032868347 scopus 로고    scopus 로고
    • Recombinant expression, purification, and characterization of Toxoplasma gondii adenosine kinase
    • Darling J.A., Sullivan Jr. W.J., Carter D., Ullman B., and Roos D.S. Recombinant expression, purification, and characterization of Toxoplasma gondii adenosine kinase. Mol Biochem Parasitol 103 (1999) 15-23
    • (1999) Mol Biochem Parasitol , vol.103 , pp. 15-23
    • Darling, J.A.1    Sullivan Jr., W.J.2    Carter, D.3    Ullman, B.4    Roos, D.S.5
  • 29
    • 0019321165 scopus 로고
    • Human placental adenosine kinase. Kinetic mechanism and inhibition
    • Palella T.D., Andres C.M., and Fox I.H. Human placental adenosine kinase. Kinetic mechanism and inhibition. J Biol Chem 255 (1980) 5264-5269
    • (1980) J Biol Chem , vol.255 , pp. 5264-5269
    • Palella, T.D.1    Andres, C.M.2    Fox, I.H.3
  • 31
    • 18044369302 scopus 로고    scopus 로고
    • 6-Benzylthioinosine analogues as subversive substrate of Toxoplasma gondii adenosine kinase: activities and selective toxicities
    • Rais R.H., Al Safarjalani O.N., Yadav V., et al. 6-Benzylthioinosine analogues as subversive substrate of Toxoplasma gondii adenosine kinase: activities and selective toxicities. Biochem Pharmacol 69 (2005) 1409-1419
    • (2005) Biochem Pharmacol , vol.69 , pp. 1409-1419
    • Rais, R.H.1    Al Safarjalani, O.N.2    Yadav, V.3
  • 32
    • 1842555109 scopus 로고    scopus 로고
    • Synthesis, biological activity and molecular modeling of 6-benzylthioinosine analogues as subversive substrates of Toxoplasma gondii adenosine kinase
    • Yadav V., Chu C.K., Rais R.H., et al. Synthesis, biological activity and molecular modeling of 6-benzylthioinosine analogues as subversive substrates of Toxoplasma gondii adenosine kinase. J Med Chem 47 (2004) 1987-1996
    • (2004) J Med Chem , vol.47 , pp. 1987-1996
    • Yadav, V.1    Chu, C.K.2    Rais, R.H.3
  • 33
    • 0029066380 scopus 로고
    • Structure-activity relationship for the binding of nucleoside ligands to adenosine kinase from Toxoplasma gondii
    • Iltzsch M.H., Uber S.S., Tankersley K.O., and el Kouni M.H. Structure-activity relationship for the binding of nucleoside ligands to adenosine kinase from Toxoplasma gondii. Biochem Pharmacol 49 (1995) 1501-1512
    • (1995) Biochem Pharmacol , vol.49 , pp. 1501-1512
    • Iltzsch, M.H.1    Uber, S.S.2    Tankersley, K.O.3    el Kouni, M.H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.