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Volumn 436, Issue 3, 2011, Pages 641-650

Glucose-6-phosphate dehydrogenase-6-phosphogluconolactonase: A unique bifunctional enzyme from Plasmodium falciparum

Author keywords

6 phosphogluconolactonase; Glucose 6 phosphate dehydrogenase; Malaria; Pentose phosphate pathway; Plasmodium; Redox

Indexed keywords

6 PHOSPHOGLUCONOLACTONASE; GLUCONOLACTONASE; GLUCOSE 6 PHOSPHATE DEHYDROGENASE; GLUTATHIONE DERIVATIVE; UNCLASSIFIED DRUG;

EID: 79957693495     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20110170     Document Type: Article
Times cited : (50)

References (34)
  • 1
    • 0031875836 scopus 로고    scopus 로고
    • Glucose-6-phosphate dehydrogenase deficiency and malaria
    • Ruwende, C. and Hill, A. (1998) Glucose-6-phosphate dehydrogenase deficiency and malaria. J. Mol. Med. 76, 581-588
    • (1998) J. Mol. Med. , vol.76 , pp. 581-588
    • Ruwende, C.1    Hill, A.2
  • 5
    • 19644378660 scopus 로고    scopus 로고
    • Erythrocyte variants and the nature of their malaria protective effect
    • DOI 10.1111/j.1462-5822.2005.00524.x
    • Min-Oo, G. and Gros, P. (2005) Erythrocyte variants and the nature of their malaria protective effect. Cell Microbiol. 7, 753-763 (Pubitemid 40740372)
    • (2005) Cellular Microbiology , vol.7 , Issue.6 , pp. 753-763
    • Min-Oo, G.1    Gros, P.2
  • 6
    • 0028041047 scopus 로고
    • Hexose-monophosphate shunt activity in intact Plasmodium falciparum-infected erythrocytes and in free parasites
    • Atamna, H., Pascarmona, G. and Ginsburg, H. (1994) Hexose-monophosphate shunt activity in intact Plasmodium falciparum-infected erythrocytes and in free parasites. Mol. Biochem. Parasitol. 67, 79-89
    • (1994) Mol. Biochem. Parasitol. , vol.67 , pp. 79-89
    • Atamna, H.1    Pascarmona, G.2    Ginsburg, H.3
  • 7
    • 0023259238 scopus 로고
    • Glucose-6-phosphate dehydrogenase of malaria parasite Plasmodium falciparum
    • Yoshida, A. and Roth, Jr, E. F. (1987) Glucose-6-phosphate dehydrogenase of malaria parasite Plasmodium falciparum. Blood 69, 1528-1530 (Pubitemid 17085318)
    • (1987) Blood , vol.69 , Issue.5 , pp. 1528-1530
    • Yoshida, A.1    Roth Jr., E.F.2
  • 8
    • 0025309238 scopus 로고
    • Expression and characterization of glucose-6-phosphate dehydrogenase of Plasmodium falciparum
    • Kurdi-Haidar, B. and Luzzatto, L. (1990) Expression and characterization of glucose-6-phosphate dehydrogenase of Plasmodium falciparum. Mol. Biochem. Parasitol. 41, 83-91
    • (1990) Mol. Biochem. Parasitol. , vol.41 , pp. 83-91
    • Kurdi-Haidar, B.1    Luzzatto, L.2
  • 10
    • 0034844693 scopus 로고    scopus 로고
    • Glucose-6-phosphate dehydrogenase-6-phosphogluconolactonase. A novel bifunctional enzyme in malaria parasites
    • Clarke, J. L., Scopes, D. A., Sodeinde, O. and Mason, P. J. (2001) Glucose-6-phosphate dehydrogenase-6-phosphogluconolactonase. A novel bifunctional enzyme in malaria parasites. Eur. J. Biochem. 268, 2013-2019
    • (2001) Eur. J. Biochem. , vol.268 , pp. 2013-2019
    • Clarke, J.L.1    Scopes, D.A.2    Sodeinde, O.3    Mason, P.J.4
  • 11
    • 0031016103 scopus 로고    scopus 로고
    • Plasmodium falciparum glucose-6-phosphate dehydrogenase (G6PD): The N-terminal portion is homologous to a predicted protein encoded near to G6PD in Haemophilus influenzae
    • Scopes, D. A., Bautista, J. M., Vulliamy, T. J. and Mason, P. J. (1997) Plasmodium falciparum glucose-6-phosphate dehydrogenase (G6PD): the N-terminal portion is homologous to a predicted protein encoded near to G6PD in Haemophilus influenzae. Mol. Microbiol. 23, 847-848
    • (1997) Mol. Microbiol. , vol.23 , pp. 847-848
    • Scopes, D.A.1    Bautista, J.M.2    Vulliamy, T.J.3    Mason, P.J.4
  • 12
    • 0037373688 scopus 로고    scopus 로고
    • A unique insertion in Plasmodium berghei glucose-6-phosphate dehydrogenase-6-phosphogluconolactonase: Evolutionary and functional studies
    • Clarke, J. L., Sodeinde, O. and Mason, P. J. (2003) A unique insertion in Plasmodium berghei glucose-6-phosphate dehydrogenase-6-phosphogluconolactonase: evolutionary and functional studies. Mol. Biochem. Parasitol. 127, 1-8
    • (2003) Mol. Biochem. Parasitol. , vol.127 , pp. 1-8
    • Clarke, J.L.1    Sodeinde, O.2    Mason, P.J.3
  • 13
    • 33745158974 scopus 로고    scopus 로고
    • Transient silencing of Plasmodium falciparum bifunctional glucose-6-phosphate dehydrogenase - 6-phosphogluconolactonase
    • Crooke, A., Diez, A., Mason, P. J. and Bautista, J. M. (2006) Transient silencing of Plasmodium falciparum bifunctional glucose-6-phosphate dehydrogenase - 6-phosphogluconolactonase. FEBS J. 273, 1537-1546
    • (2006) FEBS J. , vol.273 , pp. 1537-1546
    • Crooke, A.1    Diez, A.2    Mason, P.J.3    Bautista, J.M.4
  • 14
    • 33745951984 scopus 로고    scopus 로고
    • On the origin and functions of RNA-mediated silencing: From protists to man
    • Cerutti, H. and Casas-Mollano, J. A. (2006) On the origin and functions of RNA-mediated silencing: from protists to man. Curr. Genet. 50, 81-99
    • (2006) Curr. Genet. , vol.50 , pp. 81-99
    • Cerutti, H.1    Casas-Mollano, J.A.2
  • 15
    • 42549094690 scopus 로고    scopus 로고
    • No miRNA were found in Plasmodium and the ones identified in erythrocytes could not be correlated with infection
    • Xue, X., Zhang, Q., Huang, Y., Feng, L. and Pan, W. (2008) No miRNA were found in Plasmodium and the ones identified in erythrocytes could not be correlated with infection. Malar. J. 7, 47
    • (2008) Malar. J. , vol.7 , pp. 47
    • Xue, X.1    Zhang, Q.2    Huang, Y.3    Feng, L.4    Pan, W.5
  • 16
    • 33646035486 scopus 로고    scopus 로고
    • Interference with redox-active enzymes as a basis for the design of antimalarial drugs
    • Rahlfs, S. and Becker, K. (2006) Interference with redox-active enzymes as a basis for the design of antimalarial drugs. Mini Rev. Med. Chem. 6, 163-176
    • (2006) Mini Rev. Med. Chem. , vol.6 , pp. 163-176
    • Rahlfs, S.1    Becker, K.2
  • 19
    • 0001594119 scopus 로고
    • Initial steady state velocities in the evaluation of enzyme-coenzyme- substrate reaction mechanisms
    • Dalziel, K. (1957) Initial steady state velocities in the evaluation of enzyme-coenzyme-substrate reaction mechanisms. Acta Chem. Scand. 11, 1706-1723
    • (1957) Acta Chem. Scand. , vol.11 , pp. 1706-1723
    • Dalziel, K.1
  • 20
    • 0022607599 scopus 로고
    • Blood cell phosphogluconolactonase: Assay and properties
    • Beutler, E., Kuhl, W. and Gelbart, T. (1986) Blood cell phosphogluconolactonase: assay and properties. Br. J. Haematol. 62, 577-586
    • (1986) Br. J. Haematol. , vol.62 , pp. 577-586
    • Beutler, E.1    Kuhl, W.2    Gelbart, T.3
  • 21
    • 0023753283 scopus 로고
    • Glucose-6-phosphate dehydrogenase activity of the malaria parasite Plasmodium falciparum
    • Ling, I. T. and Wilson, R. J. (1988) Glucose-6-phosphate dehydrogenase activity of the malaria parasite Plasmodium falciparum. Mol. Biochem. Parasitol. 31, 47-56
    • (1988) Mol. Biochem. Parasitol. , vol.31 , pp. 47-56
    • Ling, I.T.1    Wilson, R.J.2
  • 22
    • 0015527226 scopus 로고
    • Human erythrocyte glucose 6-phosphate dehydrogenase: Electron microscope studies on structure and interconversion of tetramers, dimers and monomers
    • Wrigley, N. G., Heather, J. V., Bonsignore, A. and De Flora, A. (1972) Human erythrocyte glucose 6-phosphate dehydrogenase: electron microscope studies on structure and interconversion of tetramers, dimers and monomers. J. Mol. Biol. 68, 483-499
    • (1972) J. Mol. Biol. , vol.68 , pp. 483-499
    • Wrigley, N.G.1    Heather, J.V.2    Bonsignore, A.3    De Flora, A.4
  • 24
    • 48249100845 scopus 로고    scopus 로고
    • What is the role of the second 'structural' NADP+-binding site in human glucose 6-phosphate dehydrogenase?
    • Wang, X. T., Chan, T. F., Lam, V. M. and Engel, P. C. (2008) What is the role of the second 'structural' NADP+-binding site in human glucose 6-phosphate dehydrogenase? Protein Sci. 17, 1403-1411
    • (2008) Protein Sci. , vol.17 , pp. 1403-1411
    • Wang, X.T.1    Chan, T.F.2    Lam, V.M.3    Engel, P.C.4
  • 25
    • 0034654509 scopus 로고    scopus 로고
    • Human glucose-6-phosphate dehydrogenase: The crystal structure reveals a structural NADP(+) molecule and provides insights into enzyme deficiency
    • Au, S. W., Gover, S., Lam, V. M. and Adams, M. J. (2000) Human glucose-6-phosphate dehydrogenase: the crystal structure reveals a structural NADP(+) molecule and provides insights into enzyme deficiency. Structure 8, 293-303
    • (2000) Structure , vol.8 , pp. 293-303
    • Au, S.W.1    Gover, S.2    Lam, V.M.3    Adams, M.J.4
  • 26
    • 0035860710 scopus 로고    scopus 로고
    • NMR spectroscopic analysis of the first two steps of the pentose-phosphate pathway elucidates the role of 6-phosphogluconolactonase
    • Miclet, E., Stoven, V., Michels, P. A., Opperdoes, F. R., Lallemand, J. Y. and Duffieux, F. (2001) NMR spectroscopic analysis of the first two steps of the pentose-phosphate pathway elucidates the role of 6-phosphogluconolactonase. J. Biol. Chem. 276, 34840-34846
    • (2001) J. Biol. Chem. , vol.276 , pp. 34840-34846
    • Miclet, E.1    Stoven, V.2    Michels, P.A.3    Opperdoes, F.R.4    Lallemand, J.Y.5    Duffieux, F.6
  • 27
    • 0036375584 scopus 로고    scopus 로고
    • Recombinant human glucose-6-phosphate dehydrogenase. Evidence for a rapid-equilibrium random-order mechanism
    • Wang, X. T., Au, S. W., Lam, V. M. and Engel, P. C. (2002) Recombinant human glucose-6-phosphate dehydrogenase. Evidence for a rapid-equilibrium random-order mechanism. Eur. J. Biochem. 269, 3417-3424
    • (2002) Eur. J. Biochem. , vol.269 , pp. 3417-3424
    • Wang, X.T.1    Au, S.W.2    Lam, V.M.3    Engel, P.C.4
  • 28
    • 0026094986 scopus 로고
    • Kinetic properties of normal human erythrocyte glucose-6-phosphate dehydrogenase dimers
    • Adediran, S. A. (1991) Kinetic properties of normal human erythrocyte glucose-6-phosphate dehydrogenase dimers. Biochimie 73, 1211-1218
    • (1991) Biochimie , vol.73 , pp. 1211-1218
    • Adediran, S.A.1
  • 29
    • 0020773962 scopus 로고
    • 6-Phosphogluconolactonase purification, properties and activities in various tissues
    • Bauer, H. P., Srihari, T., Jochims, J. C. and Hofer, H. W. (1983) 6-Phosphogluconolactonase purification, properties and activities in various tissues. Eur. J. Biochem. 133, 163-168
    • (1983) Eur. J. Biochem. , vol.133 , pp. 163-168
    • Bauer, H.P.1    Srihari, T.2    Jochims, J.C.3    Hofer, H.W.4
  • 30
    • 0014487357 scopus 로고
    • Subunit interactions of glucose-6-phosphate dehydrogenase from human erythrocytes
    • Cohen, P. and Rosemeyer, M. A. (1969) Subunit interactions of glucose-6-phosphate dehydrogenase from human erythrocytes. Eur. J. Biochem. 8, 8-15
    • (1969) Eur. J. Biochem. , vol.8 , pp. 8-15
    • Cohen, P.1    Rosemeyer, M.A.2
  • 31
    • 51349088530 scopus 로고    scopus 로고
    • Molecular mechanisms and clinical implications of reversible protein S-glutathionylation
    • Mieyal, J. J., Gallogly, M. M., Qanungo, S., Sabens, E. A. and Shelton, M. D. (2008) Molecular mechanisms and clinical implications of reversible protein S-glutathionylation. Antioxid. Redox Signaling 10, 1941-1988
    • (2008) Antioxid. Redox Signaling , vol.10 , pp. 1941-1988
    • Mieyal, J.J.1    Gallogly, M.M.2    Qanungo, S.3    Sabens, E.A.4    Shelton, M.D.5
  • 33
    • 0028834278 scopus 로고
    • Targeted disruption of the housekeeping gene encoding glucose 6-phosphate dehydrogenase (G6PD): G6PD is dispensable for pentose synthesis but essential for defense against oxidative stress
    • Pandolfi, P. P., Sonati, F., Rivi, R., Mason, P., Grosveld, F. and Luzzatto, L. (1995) Targeted disruption of the housekeeping gene encoding glucose 6-phosphate dehydrogenase (G6PD): G6PD is dispensable for pentose synthesis but essential for defense against oxidative stress. EMBO J. 14, 5209-5215
    • (1995) EMBO J. , vol.14 , pp. 5209-5215
    • Pandolfi, P.P.1    Sonati, F.2    Rivi, R.3    Mason, P.4    Grosveld, F.5    Luzzatto, L.6
  • 34
    • 62149135922 scopus 로고    scopus 로고
    • Inhibition of Trypanosoma brucei glucose-6-phosphate dehydrogenase by human steroids and their effects on the viability of cultured parasites
    • Cordeiro, A. T., Thiemann, O. H. and Michels, P. A. (2009) Inhibition of Trypanosoma brucei glucose-6-phosphate dehydrogenase by human steroids and their effects on the viability of cultured parasites. Bioorg. Med. Chem. 17, 2483-2489
    • (2009) Bioorg. Med. Chem. , vol.17 , pp. 2483-2489
    • Cordeiro, A.T.1    Thiemann, O.H.2    Michels, P.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.