메뉴 건너뛰기




Volumn 25, Issue 1, 2002, Pages 65-72

Purification and characterization of recombinant Plasmodium falciparum adenylosuccinate synthetase expressed in Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

ESCHERICHIA COLI; PLASMODIUM FALCIPARUM; PROTOZOA;

EID: 0036930693     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1006/prep.2001.1610     Document Type: Article
Times cited : (31)

References (36)
  • 1
    • 0023736379 scopus 로고
    • Purine and pyrimidine metabolism in parasitic protozoa
    • Hassan, H. F., and Coombs, G. H. (1988) Purine and pyrimidine metabolism in parasitic protozoa. FEMS Microbiol. Rev. 54, 47-84.
    • (1988) FEMS Microbiol. Rev. , vol.54 , pp. 47-84
    • Hassan, H.F.1    Coombs, G.H.2
  • 2
    • 0018633747 scopus 로고
    • Biochemistry of Plasmodium (Malarial parasites)
    • Sherman, I. W. (1979) Biochemistry of Plasmodium (Malarial parasites). Microbiol. Rev. 43, 453-495.
    • (1979) Microbiol. Rev. , vol.43 , pp. 453-495
    • Sherman, I.W.1
  • 4
    • 0030765104 scopus 로고    scopus 로고
    • Metabolic enzymes as potential drug targets in Plasmodium falciparum
    • Subbayya, I. N. S., Ray, S. S., Balaram, P., and Balaram, H. (1997) Metabolic enzymes as potential drug targets in Plasmodium falciparum. Ind. J. Med. Res. 106, 79-94.
    • (1997) Ind. J. Med. Res. , vol.106 , pp. 79-94
    • Subbayya, I.N.S.1    Ray, S.S.2    Balaram, P.3    Balaram, H.4
  • 5
    • 0030901860 scopus 로고    scopus 로고
    • Purine salvage enzymes of parasites as targets for structure-based inhibitor design
    • Craig, S. P., III, and Eakin, A. E. (1997) Purine salvage enzymes of parasites as targets for structure-based inhibitor design. Parasitol. Today 13, 238-241.
    • (1997) Parasitol. Today , vol.13 , pp. 238-241
    • Craig S.P. III1    Eakin, A.E.2
  • 6
    • 0003012497 scopus 로고    scopus 로고
    • Unusual substrate specificity of a chimeric hypoxanthine-guanine phosphoribosyltransferase containing segments from the Plasmodium falciparum and human enzymes
    • Subbayya, I. N. S., Sukumaran, S., Shivashankar, K., and Balaram, H. (2000) Unusual substrate specificity of a chimeric hypoxanthine-guanine phosphoribosyltransferase containing segments from the Plasmodium falciparum and human enzymes. Biochem. Biophys. Res. Commun. 272, 596-602.
    • (2000) Biochem. Biophys. Res. Commun. , vol.272 , pp. 596-602
    • Subbayya, I.N.S.1    Sukumaran, S.2    Shivashankar, K.3    Balaram, H.4
  • 7
    • 0034617303 scopus 로고    scopus 로고
    • Purine phosphoribosyltransferases
    • Craig, S. P., III, and Eakin, A. E. (2000) Purine phosphoribosyltransferases. J. Biol. Chem. 275, 20231-20234.
    • (2000) J. Biol. Chem. , vol.275 , pp. 20231-20234
    • Craig, S.P.1    III2    Eakin, A.E.3
  • 8
    • 0019346557 scopus 로고
    • Purine metabolism during continuous erythrocyte culture of human malaria parasites (P. falciparum)
    • Webster, H. K., and Whaun, J. M., (1981) Purine metabolism during continuous erythrocyte culture of human malaria parasites (P. falciparum). The Red Cell: Fifth Ann. Arbor. Conf. 557-570.
    • (1981) The Red Cell: Fifth Ann. Arbor. Conf. , pp. 557-570
    • Webster, H.K.1    Whaun, J.M.2
  • 9
    • 0020668139 scopus 로고
    • Regulation, genetics and properties of adenylosuccinate synthetase: A review
    • Stayton, M. M., Rudolph, F. B., and Fromm, H. J. (1983) Regulation, genetics and properties of adenylosuccinate synthetase: A review. Curr. Top. Cell Regul. 22, 103-141.
    • (1983) Curr. Top. Cell Regul. , vol.22 , pp. 103-141
    • Stayton, M.M.1    Rudolph, F.B.2    Fromm, H.J.3
  • 10
    • 0025915402 scopus 로고
    • Purification and cDNA-derived sequence of adenylosuccinate synthetase from Dictyostelium discoideum
    • Wiesmuller, L., Wittbrodt, J., Noegel, A. A., and Schleicher, M. (1991) Purification and cDNA-derived sequence of adenylosuccinate synthetase from Dictyostelium discoideum. J. Biol. Chem. 266, 2480-2485.
    • (1991) J. Biol. Chem. , vol.266 , pp. 2480-2485
    • Wiesmuller, L.1    Wittbrodt, J.2    Noegel, A.A.3    Schleicher, M.4
  • 11
    • 0020061061 scopus 로고
    • Adenylosuccinate synthetase and adenylosuccinate lyase from Trypanosoma cruzi: Specificity studies with potential chemotherapeutic agents
    • Spector, T., Berens, R. L., and Marr, J. J. (1982) Adenylosuccinate synthetase and adenylosuccinate lyase from Trypanosoma cruzi: Specificity studies with potential chemotherapeutic agents. Biochem. Pharmacol. 31, 225-229.
    • (1982) Biochem. Pharmacol. , vol.31 , pp. 225-229
    • Spector, T.1    Berens, R.L.2    Marr, J.J.3
  • 12
    • 0016289678 scopus 로고
    • Human adenylosuccinate synthetase: Partial purification, kinetic and regulatory properties of the enzyme from placenta
    • Van der Weyden, M. B., and Kelly, W. N. (1974) Human adenylosuccinate synthetase: Partial purification, kinetic and regulatory properties of the enzyme from placenta. J. Biol. Chem. 249, 7282-7289.
    • (1974) J. Biol. Chem. , vol.249 , pp. 7282-7289
    • Van der Weyden, M.B.1    Kelly, W.N.2
  • 13
    • 0017719117 scopus 로고
    • Adenylosuccinate synthetase from Azotobacter vinelandii: Purification, properties and steady-state kinetics
    • Markham, G. D., and Reed, G. H. (1977) Adenylosuccinate synthetase from Azotobacter vinelandii: Purification, properties and steady-state kinetics. Arch. Biochem. Biophys. 184, 24-35.
    • (1977) Arch. Biochem. Biophys. , vol.184 , pp. 24-35
    • Markham, G.D.1    Reed, G.H.2
  • 14
    • 0014835250 scopus 로고
    • Regulation of purine ribonucleotide synthesis by end product inhibition. 3. Effect of purine nucleotides on succino-AMP synthetase of Bacillus subtilis
    • Ishii, K., and Shiio, I. (1970) Regulation of purine ribonucleotide synthesis by end product inhibition. 3. Effect of purine nucleotides on succino-AMP synthetase of Bacillus subtilis. J. Biochem. (Tokyo) 68, 171-176.
    • (1970) J. Biochem. (Tokyo) , vol.68 , pp. 171-176
    • Ishii, K.1    Shiio, I.2
  • 15
    • 0023368634 scopus 로고
    • Overproduction, purification, and characterization of adenylosuccinate synthetase from Escherichia coli
    • Bass, M. B., Fromm, H. J., and Stayton, M. M. (1987) Overproduction, purification, and characterization of adenylosuccinate synthetase from Escherichia coli. Arch. Biochem. Biophys. 256, 335-342.
    • (1987) Arch. Biochem. Biophys. , vol.256 , pp. 335-342
    • Bass, M.B.1    Fromm, H.J.2    Stayton, M.M.3
  • 16
    • 0034681295 scopus 로고    scopus 로고
    • Structures of adenylosuccinate synthetase from Triticum aestivum and Arabidopsis thaliana
    • Prade, L, Cowan-Jacob, S. W., Chemla, P., Potter, S., Ward, E., and Fonne-Pfister, R. (2000) Structures of adenylosuccinate synthetase from Triticum aestivum and Arabidopsis thaliana. J. Mol. Biol. 296, 569-577.
    • (2000) J. Mol. Biol. , vol.296 , pp. 569-577
    • Prade, L.1    Cowan-Jacob, S.W.2    Chemla, P.3    Potter, S.4    Ward, E.5    Fonne-Pfister, R.6
  • 17
    • 0040379047 scopus 로고    scopus 로고
    • The mode of action of and the structure of a herbicide in complex with its target: Binding of activated hydantocidin to the feedback regulation site of adenylosuccinate synthetase
    • Fonne-Pfister, R., Chemls, P., Ward, E., Girardet, M., Kreuz, K. E., Honzatko, R. B., Fromm, H. J., Schar, H.-P., Grutter, M. G., and Cowan-Jacob, S. W. (1996) The mode of action of and the structure of a herbicide in complex with its target: Binding of activated hydantocidin to the feedback regulation site of adenylosuccinate synthetase. Proc. Natl. Acad. Sci. USA 93, 9431-9436.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 9431-9436
    • Fonne-Pfister, R.1    Chemls, P.2    Ward, E.3    Girardet, M.4    Kreuz, K.E.5    Honzatko, R.B.6    Fromm, H.J.7    Schar, H.-P.8    Grutter, M.G.9    Cowan-Jacob, S.W.10
  • 18
    • 19144367977 scopus 로고
    • Refined crystal structures of unligated adenylosuccinate synthetase from Escherichia coli
    • Silva, M. M., Poland, B. W., Hoffman, C. R., Fromm, H. J., and Honzatko, R. B. (1995) Refined crystal structures of unligated adenylosuccinate synthetase from Escherichia coli. J. Mol. Biol. 254, 431-446.
    • (1995) J. Mol. Biol. , vol.254 , pp. 431-446
    • Silva, M.M.1    Poland, B.W.2    Hoffman, C.R.3    Fromm, H.J.4    Honzatko, R.B.5
  • 19
    • 0023263288 scopus 로고
    • Analysis of sequences from the extremely A + T-rich genome of Plasmodium falciparum
    • Weber, J. L. (1987) Analysis of sequences from the extremely A + T-rich genome of Plasmodium falciparum. Gene 52, 103-109.
    • (1987) Gene , vol.52 , pp. 103-109
    • Weber, J.L.1
  • 20
    • 0017311840 scopus 로고
    • Human malaria parasites in continuous culture
    • Trager, W., and Jensen, J. B. (1976) Human malaria parasites in continuous culture. Science 193, 673-675.
    • (1976) Science , vol.193 , pp. 673-675
    • Trager, W.1    Jensen, J.B.2
  • 21
    • 0027428306 scopus 로고
    • Cloning of the triosephosphate isomerase gene of Plasmodium falciparum and expression in Escherichia coli
    • Ranie, J., Kumar, V. P., and Balaram, H. (1993) Cloning of the triosephosphate isomerase gene of Plasmodium falciparum and expression in Escherichia coli. Mol. Biochem. Parasitol. 61, 159-170.
    • (1993) Mol. Biochem. Parasitol. , vol.61 , pp. 159-170
    • Ranie, J.1    Kumar, V.P.2    Balaram, H.3
  • 22
    • 0012290107 scopus 로고    scopus 로고
    • Cloning and characterization of the Plasmodium falciparum adenylosuccinate synthetase gene
    • Sumathy, K., Jayalakshmi, R., Shivayogi, M. S., and Balaram, H., (2000). Cloning and characterization of the Plasmodium falciparum adenylosuccinate synthetase gene. Curr. Sci. 78, 610-615.
    • (2000) Curr. Sci. , vol.78 , pp. 610-615
    • Sumathy, K.1    Jayalakshmi, R.2    Shivayogi, M.S.3    Balaram, H.4
  • 23
    • 0023777735 scopus 로고
    • Tightly regulated tac promotor vectors useful for expression of unfused and fused proteins in Escherichia coli
    • Amann, E., Ochs, B., and Abel, K-J. (1988) Tightly regulated tac promotor vectors useful for expression of unfused and fused proteins in Escherichia coli. Gene 69, 301-315.
    • (1988) Gene , vol.69 , pp. 301-315
    • Amann, E.1    Ochs, B.2    Abel, K.-J.3
  • 24
    • 0030590262 scopus 로고    scopus 로고
    • The adenylosuccinate synthetase from the hyperthermophillic archaeon Pyrococcus species displays unusual features
    • Bouyoub, A., Barbier, G., Forterre, P., and Labedan, B. (1996) The adenylosuccinate synthetase from the hyperthermophillic archaeon Pyrococcus species displays unusual features. J. Mol. Biol. 261, 144-154.
    • (1996) J. Mol. Biol. , vol.261 , pp. 144-154
    • Bouyoub, A.1    Barbier, G.2    Forterre, P.3    Labedan, B.4
  • 25
    • 0027240254 scopus 로고
    • Expression, purification, and kinetic characterization of recombinant human adenylosuccinate lyase
    • Stone, R. L., Zalkin, H., and Dixon, J. E. (1993) Expression, purification, and kinetic characterization of recombinant human adenylosuccinate lyase. J. Biol. Chem. 268, 19710-19716.
    • (1993) J. Biol. Chem. , vol.268 , pp. 19710-19716
    • Stone, R.L.1    Zalkin, H.2    Dixon, J.E.3
  • 26
    • 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
  • 27
    • 0029034945 scopus 로고
    • Identification of an essential second metal ion in the reaction mechanism of Escherichia coli adenylosuccinate synthetase
    • Kang, C., and Fromm, H. J. (1995) Identification of an essential second metal ion in the reaction mechanism of Escherichia coli adenylosuccinate synthetase. J. Biol. Chem. 270, 15539-15544.
    • (1995) J. Biol. Chem. , vol.270 , pp. 15539-15544
    • Kang, C.1    Fromm, H.J.2
  • 28
    • 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. (1976) 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) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 29
    • 0025947362 scopus 로고
    • Escherichia coli ppGpp synthetase II activity requires spoT
    • Hernandez, J. V., and Bremer, H., (1991) Escherichia coli ppGpp synthetase II activity requires spoT. J. Biol. Chem. 266, 5991-5999.
    • (1991) J. Biol. Chem. , vol.266 , pp. 5991-5999
    • Hernandez, J.V.1    Bremer, H.2
  • 31
    • 0024801633 scopus 로고
    • Characterization of the relA1 mutation and a comparison of relA1 with new relA null alleles in Escherichia coli
    • Metzger, S., Schreiber, G., Aizenman, E., Cashel, M., and Glaser, G., (1989) Characterization of the relA1 mutation and a comparison of relA1 with new relA null alleles in Escherichia coli. J. Biol. Chem. 264, 21146-21152.
    • (1989) J. Biol. Chem. , vol.264 , pp. 21146-21152
    • Metzger, S.1    Schreiber, G.2    Aizenman, E.3    Cashel, M.4    Glaser, G.5
  • 32
    • 0018421738 scopus 로고
    • Guanosine 5′-diphosphate-3′-diphosphate inhibition of adenylosuccinate synthetase
    • Stayton, M. M., and Fromm, H. J. (1979) Guanosine 5′-diphosphate-3′-diphosphate inhibition of adenylosuccinate synthetase. J. Biol. Chem. 254, 2579-2581.
    • (1979) J. Biol. Chem. , vol.254 , pp. 2579-2581
    • Stayton, M.M.1    Fromm, H.J.2
  • 34
    • 0031153921 scopus 로고    scopus 로고
    • Adenylosuccinate synthetase from maize: Purification, properties, and mechanism of inhibition by 5′-phosphohydantocidin
    • Niderman, T., Bernasconi, P., Subramanian, M. V., and Siehl, D. L. (1997) Adenylosuccinate synthetase from maize: Purification, properties, and mechanism of inhibition by 5′-phosphohydantocidin. Plant Physiol. 114, 549-555.
    • (1997) Plant Physiol. , vol.114 , pp. 549-555
    • Niderman, T.1    Bernasconi, P.2    Subramanian, M.V.3    Siehl, D.L.4
  • 35
    • 0033178495 scopus 로고    scopus 로고
    • Adenylosuccinate synthase from Saccharomyces cerevisiae: Homologous overexpression, purification and characterization of the recombinant protein
    • Lipps, G., and Krauss, G. (1999) Adenylosuccinate synthase from Saccharomyces cerevisiae: Homologous overexpression, purification and characterization of the recombinant protein. Biochem. J. 341, 537-543.
    • (1999) Biochem. J. , vol.341 , pp. 537-543
    • Lipps, G.1    Krauss, G.2
  • 36
    • 0030904928 scopus 로고    scopus 로고
    • A study of Escherichia coli adenylosuccinate synthetase association states and the interface residues of the homodimer
    • Wang, W., Gorrell, A., Honzatko, R. B., and Fromm, H. J. (1997) A study of Escherichia coli adenylosuccinate synthetase association states and the interface residues of the homodimer. J. Biol. Chem. 272, 7078-7084.
    • (1997) J. Biol. Chem. , vol.272 , pp. 7078-7084
    • Wang, W.1    Gorrell, A.2    Honzatko, R.B.3    Fromm, H.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.