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Volumn 234, Issue 1, 2004, Pages 117-123

The pentose phosphate pathway in Trypanosoma cruzi

Author keywords

6PGDH, 6 phosphogluconate dehydrogenase; Chagas disease; G6PDH, glucose 6 phosphate dehydrogenase; Lactonase, 6 phosphogluconolactonase; Oxidative stress; Pentose phosphate pathway; PPP, pentose phosphate pathway; Subcellular localisations; Trypanosoma cruzi

Indexed keywords

CARBON DIOXIDE; ENZYME; GLUCOSE; METHYLENE BLUE; PENTOSE;

EID: 1942502299     PISSN: 03781097     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.femsle.2004.03.018     Document Type: Article
Times cited : (58)

References (25)
  • 1
    • 0028258946 scopus 로고
    • Intermediate metabolism in Trypanosoma cruzi
    • Cazzulo J.J. Intermediate metabolism in Trypanosoma cruzi. J. Bioenerg. Biomemb. 26:1994;157-165.
    • (1994) J. Bioenerg. Biomemb. , vol.26 , pp. 157-165
    • Cazzulo, J.J.1
  • 2
    • 0032986133 scopus 로고    scopus 로고
    • Purification and properties of phosphoglucose isomerases of Trypanosoma cruzi
    • Concepción J.L., Chataing B., Dubourdieu M. Purification and properties of phosphoglucose isomerases of Trypanosoma cruzi. Comp. Biochem. Physiol. Part B. 122:1999;211-222.
    • (1999) Comp. Biochem. Physiol. Part B , vol.122 , pp. 211-222
    • Concepción, J.L.1    Chataing, B.2    Dubourdieu, M.3
  • 3
    • 0031032145 scopus 로고    scopus 로고
    • The pentose phosphate pathway and Parasitic Protozoa
    • Barrett M.P. The pentose phosphate pathway and Parasitic Protozoa. Parasitol. Today. 13:1997;11-16.
    • (1997) Parasitol. Today , vol.13 , pp. 11-16
    • Barrett, M.P.1
  • 4
    • 85047686510 scopus 로고    scopus 로고
    • The plastidic pentose phosphate translocator represents a link between the cytosolic and plastidic pentose phosphate pathway in plants
    • Eicks M., Maurino V., Knappe S., Flugge U., Fischer K. The plastidic pentose phosphate translocator represents a link between the cytosolic and plastidic pentose phosphate pathway in plants. Plant Physiol. 128:2002;512-522.
    • (2002) Plant Physiol. , vol.128 , pp. 512-522
    • Eicks, M.1    Maurino, V.2    Knappe, S.3    Flugge, U.4    Fischer, K.5
  • 5
    • 0023722279 scopus 로고
    • The pentose phosphate pathway in the endoplasmic reticulum
    • Bublitz C., Steavenson S. The pentose phosphate pathway in the endoplasmic reticulum. J. Biol. Chem. 263(26):1988;12849-12853.
    • (1988) J. Biol. Chem. , vol.263 , Issue.26 , pp. 12849-12853
    • Bublitz, C.1    Steavenson, S.2
  • 6
    • 0024336546 scopus 로고
    • Dehydrogenases of the pentose phosphate pathway in rat liver peroxisomes
    • Antonenkov V.D. Dehydrogenases of the pentose phosphate pathway in rat liver peroxisomes. Eur. J. Biochem. 183:1989;75-82.
    • (1989) Eur. J. Biochem. , vol.183 , pp. 75-82
    • Antonenkov, V.D.1
  • 7
    • 0024497978 scopus 로고
    • The enzymes of the classical pentose phosphate pathway display differential activities in procyclic and bloodstream forms of Trypanosoma brucei
    • Cronin C.N., Nolan D.P., Voorheis H.P. The enzymes of the classical pentose phosphate pathway display differential activities in procyclic and bloodstream forms of Trypanosoma brucei. FEBS Lett. 244:1989;26-30.
    • (1989) FEBS Lett. , vol.244 , pp. 26-30
    • Cronin, C.N.1    Nolan, D.P.2    Voorheis, H.P.3
  • 8
    • 0032566440 scopus 로고    scopus 로고
    • A 2.8 Å resolution structure of 6-phosphogluconate dehydrogenase from the Protozoan parasite Trypanosoma brucei: Comparison with the sheep enzyme accounts for differences in activity with coenzyme and substrate analogues
    • Phillips C., Dohnalek J., Gover S., Barrett M.P., Adams M.J. A 2.8 Å resolution structure of 6-phosphogluconate dehydrogenase from the Protozoan parasite Trypanosoma brucei: comparison with the sheep enzyme accounts for differences in activity with coenzyme and substrate analogues. J. Mol. Biol. 282:1998;667-681.
    • (1998) J. Mol. Biol. , vol.282 , pp. 667-681
    • Phillips, C.1    Dohnalek, J.2    Gover, S.3    Barrett, M.P.4    Adams, M.J.5
  • 9
    • 0034623222 scopus 로고    scopus 로고
    • Molecular characterization of the first two enzymes of the pentose phosphate pathway of Trypanosoma brucei. Glucose-6-phosphate dehydrogenase and 6-phophogluconolactonase
    • Duffieux F., Van Roy J., Michels P.A.M., Opperdoes F.R. Molecular characterization of the first two enzymes of the pentose phosphate pathway of Trypanosoma brucei. Glucose-6-phosphate dehydrogenase and 6- phophogluconolactonase. J. Biol. Chem. 275:2000;27559-27565.
    • (2000) J. Biol. Chem. , vol.275 , pp. 27559-27565
    • Duffieux, F.1    Van Roy, J.2    Michels, P.A.M.3    Opperdoes, F.R.4
  • 11
    • 0342831592 scopus 로고
    • Some aspects of carbohydrate metabolism of cultural forms of Trypanosoma cruzi
    • Raw I. Some aspects of carbohydrate metabolism of cultural forms of Trypanosoma cruzi. Rev. Inst. Med. Trop. Sao Paulo. 1:1959;192-194.
    • (1959) Rev. Inst. Med. Trop. Sao Paulo , vol.1 , pp. 192-194
    • Raw, I.1
  • 12
    • 0017568352 scopus 로고
    • Trypanosoma cruzi: Kinetic properties of glucose-6-phosphate dehydrogenase
    • Funayama Sh., Funayama Si., Ito I.Y., Veiga L.A. Trypanosoma cruzi: kinetic properties of glucose-6-phosphate dehydrogenase. Exp. Parasitol. 43:1977;376-381.
    • (1977) Exp. Parasitol. , vol.43 , pp. 376-381
    • Funayama, Sh.1    Funayama, Si.2    Ito, I.Y.3    Veiga, L.A.4
  • 13
    • 0346157320 scopus 로고    scopus 로고
    • The 6-phosphogluconate dehydrogenase from Trypanosoma cruzi: The absence of two inter-subunit salt bridges as a reason for enzyme instability
    • Igoillo Esteve M., Cazzulo J.J. The 6-phosphogluconate dehydrogenase from Trypanosoma cruzi: the absence of two inter-subunit salt bridges as a reason for enzyme instability. Mol. Biochem. Parasitol. 133:2004;197-207.
    • (2004) Mol. Biochem. Parasitol. , vol.133 , pp. 197-207
    • Igoillo Esteve, M.1    Cazzulo, J.J.2
  • 15
    • 0343702077 scopus 로고
    • 14-glucose in two strains of Trypanosoma cruzi
    • 14-glucose in two strains of Trypanosoma cruzi. J. Protozool. 11:1964;509-513.
    • (1964) J. Protozool. , vol.11 , pp. 509-513
    • Mancilla, R.1    Náquira, C.2
  • 19
    • 0000311344 scopus 로고
    • 14 for the evaluation of the pathways of glucose metabolism
    • 14 for the evaluation of the pathways of glucose metabolism. J. Biol. Chem. 238:1963;517-523.
    • (1963) J. Biol. Chem. , vol.238 , pp. 517-523
    • Katz, J.1    Wood, H.G.2
  • 20
    • 0021287730 scopus 로고
    • Glycosomal and mitochondrial malate dehydrogenase in epimastigotes of Trypanosoma cruzi
    • Cannata J.J.B., Cazzulo J.J. Glycosomal and mitochondrial malate dehydrogenase in epimastigotes of Trypanosoma cruzi. Mol. Biochem. Parasitol. 11:1984;37-49.
    • (1984) Mol. Biochem. Parasitol. , vol.11 , pp. 37-49
    • Cannata, J.J.B.1    Cazzulo, J.J.2
  • 21
    • 0024674189 scopus 로고
    • On the regulatory properties of the pyruvate kinase from Trypanosoma cruzi epimastigotes
    • Cazzulo J.J., Cazzulo Franke M.C., Franke de Cazzulo B.M. On the regulatory properties of the pyruvate kinase from Trypanosoma cruzi epimastigotes. FEMS Microbiol. Lett. 59:1989;259-264.
    • (1989) FEMS Microbiol. Lett. , vol.59 , pp. 259-264
    • Cazzulo, J.J.1    Cazzulo Franke, M.C.2    Franke De Cazzulo, B.M.3
  • 22
    • 0028822037 scopus 로고
    • Phosphoenolpyruvate carboxykinase from Trypanosoma cruzi. Purification and physicochemical and kinetic properties
    • Cymeryng C., Cazzulo J.J., Cannata J.J.B. Phosphoenolpyruvate carboxykinase from Trypanosoma cruzi. Purification and physicochemical and kinetic properties. Mol. Biochem. Parasitol. 73:1995;91-101.
    • (1995) Mol. Biochem. Parasitol. , vol.73 , pp. 91-101
    • Cymeryng, C.1    Cazzulo, J.J.2    Cannata, J.J.B.3
  • 23
    • 0028041047 scopus 로고
    • Hexosemonophosphate shunt activity in intact Plasmodium falciparum - Infected erythrocytes and in free parasites
    • Atamna H., Pascarmona G., Guinsburg H. Hexosemonophosphate shunt activity in intact Plasmodium falciparum - infected erythrocytes and in free parasites. Mol. Biochem. Parasitol. 67:1994;78-89.
    • (1994) Mol. Biochem. Parasitol. , vol.67 , pp. 78-89
    • Atamna, H.1    Pascarmona, G.2    Guinsburg, H.3
  • 24
    • 0034934234 scopus 로고    scopus 로고
    • Trypanothione as a target in the design of antitrypanosomal and antileishmanial agents
    • Augustyns K., Amssoms K., Yamani A., Rajan P.K., Haemers A. Trypanothione as a target in the design of antitrypanosomal and antileishmanial agents. Curr. Pharm. Des. 7:2001;1117-1141.
    • (2001) Curr. Pharm. Des. , vol.7 , pp. 1117-1141
    • Augustyns, K.1    Amssoms, K.2    Yamani, A.3    Rajan, P.K.4    Haemers, A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.