메뉴 건너뛰기




Volumn 382, Issue 2, 2004, Pages 759-767

Transketolase from Leishmania mexicana has a dual subcellular localization

Author keywords

Glycosome; Leishmania mexicana; Pentose phosphate pathway; Transketolase

Indexed keywords

CYTOLOGY; ENZYME INHIBITION; ESCHERICHIA COLI; PROTEINS; X RAY CRYSTALLOGRAPHY;

EID: 4544269846     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20040459     Document Type: Article
Times cited : (46)

References (46)
  • 1
    • 0023464501 scopus 로고
    • Compartmentation of carbohydrate metabolism in trypanosomes
    • Opperdoes, F. R. (1987) Compartmentation of carbohydrate metabolism in trypanosomes. Annu. Rev. Microbiol. 41, 127-151
    • (1987) Annu. Rev. Microbiol. , vol.41 , pp. 127-151
    • Opperdoes, F.R.1
  • 2
    • 0031032145 scopus 로고    scopus 로고
    • The pentose phosphate pathway and parasitic protozoa
    • Barrett, M. P. (1997) The pentose phosphate pathway and parasitic protozoa. Parasitol. Today 13, 11-16
    • (1997) Parasitol. Today , vol.13 , pp. 11-16
    • Barrett, M.P.1
  • 4
    • 0032423288 scopus 로고    scopus 로고
    • Properties and functions of the thiamin diphosphate dependent enzyme transketolase
    • Schenk, G., Duggleby, R. G. and Nixon, P. F. (1998) Properties and functions of the thiamin diphosphate dependent enzyme transketolase. Int. J. Biochem. Cell Biol. 30, 1297-1318
    • (1998) Int. J. Biochem. Cell Biol. , vol.30 , pp. 1297-1318
    • Schenk, G.1    Duggleby, R.G.2    Nixon, P.F.3
  • 5
    • 0031001809 scopus 로고    scopus 로고
    • Molecular evolutionary analysis of the thiamine-diphosphate-dependent enzyme transketolase
    • Schenk, G., Layfield, R., Candy, J. M., Duggleby, R. G. and Nixon, P. F. (1997) Molecular evolutionary analysis of the thiamine-diphosphate-dependent enzyme transketolase. J. Mol. Evol. 44, 552-572
    • (1997) J. Mol. Evol. , vol.44 , pp. 552-572
    • Schenk, G.1    Layfield, R.2    Candy, J.M.3    Duggleby, R.G.4    Nixon, P.F.5
  • 6
    • 0032537478 scopus 로고    scopus 로고
    • Crystallography and mutagenesis of transketolase: Mechanistic implications for enzymatic thiamine catalysis
    • Schneider, G. and Linqvist, Y. (1998) Crystallography and mutagenesis of transketolase: mechanistic implications for enzymatic thiamine catalysis. Biochim. Biophys. Acta 1385, 387-398
    • (1998) Biochim. Biophys. Acta , vol.1385 , pp. 387-398
    • Schneider, G.1    Linqvist, Y.2
  • 7
    • 0017023665 scopus 로고
    • Enzymes of carbohydrate metabolism in four human species of Leishmania: A comparative study
    • Martin, E., Simon, M. W., Schaefer, F. W. and Mukkada, A. J. (1976) Enzymes of carbohydrate metabolism in four human species of Leishmania: a comparative study. J. Protozool. 23, 600-607
    • (1976) J. Protozool. , vol.23 , pp. 600-607
    • Martin, E.1    Simon, M.W.2    Schaefer, F.W.3    Mukkada, A.J.4
  • 8
    • 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. and Voorheis, H. P. (1989) The enzymes of the classical pentose phosphate pathway display differential activities in procyclic and bloodstream forms of Trypanosoma brucei. FEBS Lett. 244, 26-30
    • (1989) FEBS Lett. , vol.244 , pp. 26-30
    • Cronin, C.N.1    Nolan, D.P.2    Voorheis, H.P.3
  • 9
    • 0032030782 scopus 로고    scopus 로고
    • Purification, properties and in situ localisation of the amphibolic enzymes D-ribulose 5-phosphate 3-epimerase and transketolase from spinach chloroplasts
    • Teige, M., Melzer, M. and Süss, K. H. (1998) Purification, properties and in situ localisation of the amphibolic enzymes D-ribulose 5-phosphate 3-epimerase and transketolase from spinach chloroplasts. Eur. J. Biochem. 252, 237-244
    • (1998) Eur. J. Biochem. , vol.252 , pp. 237-244
    • Teige, M.1    Melzer, M.2    Süss, K.H.3
  • 10
    • 0023722279 scopus 로고
    • The pentose phosphate pathway in the endoplasmic reticulum
    • Bublitz, C. and Steavenson, S. (1988) The pentose phosphate pathway in the endoplasmic reticulum. J. Biol. Chem. 263, 12849-12853
    • (1988) J. Biol. Chem. , vol.263 , pp. 12849-12853
    • Bublitz, C.1    Steavenson, S.2
  • 11
    • 0024336546 scopus 로고
    • Dehydrogenases of the pentose phosphate pathway in rat liver peroxisomes
    • Antonenkov, V. D. (1989) Dehydrogenases of the pentose phosphate pathway in rat liver peroxisomes. Eur. J. Biochem. 183, 75-82
    • (1989) Eur. J. Biochem. , vol.183 , pp. 75-82
    • Antonenkov, V.D.1
  • 13
    • 0035161710 scopus 로고    scopus 로고
    • Localization of glucose-6-phosphate dehydrogenase activity on ribosomes of granular endoplasmic reticulum, in peroxisomes and peripheral cytoplasm of rat liver parenchymal cells
    • Frederiks, W. M. and Vreeling-Sindelárová, H. (2001) Localization of glucose-6-phosphate dehydrogenase activity on ribosomes of granular endoplasmic reticulum, in peroxisomes and peripheral cytoplasm of rat liver parenchymal cells. Histochem. J. 33, 345-353
    • (2001) Histochem. J. , vol.33 , pp. 345-353
    • Frederiks, W.M.1    Vreeling-Sindelárová, H.2
  • 14
    • 0034623222 scopus 로고    scopus 로고
    • Molecular characterisation of the first two enzymes of the pentose-phosphate pathway of Trypanosoma brucei
    • Duffieux, F., Roy, J. V., Michels, P. A. M. and Opperdoes, F. R. (2000) Molecular characterisation of the first two enzymes of the pentose-phosphate pathway of Trypanosoma brucei. J. Biol. Chem. 275, 27559-27565
    • (2000) J. Biol. Chem. , vol.275 , pp. 27559-27565
    • Duffieux, F.1    Roy, J.V.2    Michels, P.A.M.3    Opperdoes, F.R.4
  • 15
    • 0033525539 scopus 로고    scopus 로고
    • Purification, localisation and characterisation of glucose-6-phosphate dehydrogenase of Trypanosoma brucei
    • Heise, N. and Opperdoes, F. R. (1999) Purification, localisation and characterisation of glucose-6-phosphate dehydrogenase of Trypanosoma brucei. Mol. Biochem. Parasitol. 99, 21-32
    • (1999) Mol. Biochem. Parasitol. , vol.99 , pp. 21-32
    • Heise, N.1    Opperdoes, F.R.2
  • 17
    • 0017195170 scopus 로고
    • A simple monophasic medium for axenic culture of hemoflagellates
    • Berens, R. L., Brun, R. and Krassner, S. M. (1976) A simple monophasic medium for axenic culture of hemoflagellates. J. Parasitol. 62, 360-365
    • (1976) J. Parasitol. , vol.62 , pp. 360-365
    • Berens, R.L.1    Brun, R.2    Krassner, S.M.3
  • 18
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilising the principle of protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilising the principle of protein-dye binding. Anal. Biochem. 72, 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 19
    • 0027262263 scopus 로고
    • Rapid isolation of DNA from trypanosomatid protozoa using a simple 'mini-prep' procedure
    • Medina-Acosta, E. and Cross, G. A. M. (1993) Rapid isolation of DNA from trypanosomatid protozoa using a simple 'mini-prep' procedure. Mol. Biochem. Parasitol. 59, 327-330
    • (1993) Mol. Biochem. Parasitol. , vol.59 , pp. 327-330
    • Medina-Acosta, E.1    Cross, G.A.M.2
  • 20
    • 0003076963 scopus 로고
    • Recent changes to the MOSFLM package for processing film and image plate data
    • Leslie, A. G. W. (1992) Recent changes to the MOSFLM package for processing film and image plate data. Jt. CCP4 + ESF-EAMCB Newslett. Prot. Crystallogr. 26
    • (1992) Jt. CCP4 + ESF-EAMCB Newslett. Prot. Crystallogr. , vol.26
    • Leslie, A.G.W.1
  • 22
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4
    • Collaborative Computational Project, Number 4. (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr. Sect. D. Biol. Crystallogr. 50, 760-763
    • (1994) Acta Crystallogr. Sect. D. Biol. Crystallogr. , vol.50 , pp. 760-763
  • 25
  • 27
    • 0033119938 scopus 로고    scopus 로고
    • Further additions to MolScript version 1.4, including reading and contouring of electron-density maps
    • Esnouf, R. M. (1999) Further additions to MolScript version 1.4, including reading and contouring of electron-density maps. Acta Crystallogr. D. Biol. Crystallogr. 55, 938-940
    • (1999) Acta Crystallogr. D. Biol. Crystallogr. , vol.55 , pp. 938-940
    • Esnouf, R.M.1
  • 28
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D: Photorealistic molecular graphics
    • Merritt, E. A. and Bacon, D. J. (1997) Raster3D: photorealistic molecular graphics. Methods Enzymol. 277, 505-524
    • (1997) Methods Enzymol. , vol.277 , pp. 505-524
    • Merritt, E.A.1    Bacon, D.J.2
  • 29
    • 0014632067 scopus 로고
    • Transketolase mutants of Escherichia coli
    • Josephson, B. L. and Fraenkel, D. G. (1969) Transketolase mutants of Escherichia coli. J. Bacteriol. 100, 1289-1295
    • (1969) J. Bacteriol. , vol.100 , pp. 1289-1295
    • Josephson, B.L.1    Fraenkel, D.G.2
  • 30
    • 0018238954 scopus 로고
    • An improved assay for hexokinase activity in human tissue homogenates
    • Scheer, W. D., Lehman, H. P. and Beeler, M. F. (1978) An improved assay for hexokinase activity in human tissue homogenates. Anal. Biochem. 91, 451-463
    • (1978) Anal. Biochem. , vol.91 , pp. 451-463
    • Scheer, W.D.1    Lehman, H.P.2    Beeler, M.F.3
  • 31
    • 0024674189 scopus 로고
    • On the regulatory properties of the pyruvate kinase from Trypanosoma cruzi epimastigotes
    • Cazzulo, J. J., Cazzulo Franke, M. C. and Franke de Cazzulo, B. M. (1989) On the regulatory properties of the pyruvate kinase from Trypanosoma cruzi epimastigotes. FEMS Microbiol. Lett. 59, 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
  • 32
    • 0030221826 scopus 로고    scopus 로고
    • Purification and partial structural and kinetic characterization of an alanine aminotransferase from epimastigotes of Trypanosoma cruzi
    • Zelada, C., Montemartini, M., Cazzulo, J. J. and Nowicki, C. (1996) Purification and partial structural and kinetic characterization of an alanine aminotransferase from epimastigotes of Trypanosoma cruzi. Mol. Biochem. Parasitol. 79, 225-228
    • (1996) Mol. Biochem. Parasitol. , vol.79 , pp. 225-228
    • Zelada, C.1    Montemartini, M.2    Cazzulo, J.J.3    Nowicki, C.4
  • 33
    • 0028822037 scopus 로고
    • Phosphoenolpyruvate carboxykinase from Trypanosoma cruzi. Purification and physicochemical and kinetic properties
    • Cymeryng, C., Cazzulo, J. J. and Cannata, J. J. B. (1995) Phosphoenolpyruvate carboxykinase from Trypanosoma cruzi. Purification and physicochemical and kinetic properties. Mol. Biochem. Parasitol. 73, 91-101
    • (1995) Mol. Biochem. Parasitol. , vol.73 , pp. 91-101
    • Cymeryng, C.1    Cazzulo, J.J.2    Cannata, J.J.B.3
  • 34
    • 0028305456 scopus 로고
    • Refined structure of transketolase from Saccharomyces cerevisiae at 2.0 Å resolution
    • Nikkola, M., Lindqvist, Y. and Schneider, G. (1994) Refined structure of transketolase from Saccharomyces cerevisiae at 2.0 Å resolution. J. Mol. Biol. 238, 387-404
    • (1994) J. Mol. Biol. , vol.238 , pp. 387-404
    • Nikkola, M.1    Lindqvist, Y.2    Schneider, G.3
  • 38
    • 0026699609 scopus 로고
    • Aerobic fermentation of glucose by trypanosomatids
    • Cazzulo, J. J. (1992) Aerobic fermentation of glucose by trypanosomatids. FASEB J. 6, 3153-3161
    • (1992) FASEB J. , vol.6 , pp. 3153-3161
    • Cazzulo, J.J.1
  • 39
    • 0022260611 scopus 로고
    • Leishmania mexicana: Subcellular distribution of enzymes in amastigotes and promastigotes
    • Mottram, J. C. and Coombs, G. H. (1985) Leishmania mexicana: subcellular distribution of enzymes in amastigotes and promastigotes. Exp. Parasitol. 59, 265-274
    • (1985) Exp. Parasitol. , vol.59 , pp. 265-274
    • Mottram, J.C.1    Coombs, G.H.2
  • 40
    • 0024432768 scopus 로고
    • A common structural motif in thiamin pyrophosphate-binding enzymes
    • Hawkins, C. F., Borges, A. and Perham, R. N. (1989) A common structural motif in thiamin pyrophosphate-binding enzymes. FEBS Lett. 255, 77-82
    • (1989) FEBS Lett. , vol.255 , pp. 77-82
    • Hawkins, C.F.1    Borges, A.2    Perham, R.N.3
  • 41
    • 0031039575 scopus 로고    scopus 로고
    • Examination of the thiamin binding site in yeast transketolase by site-directed mutagenesis
    • Meshalkina, L., Nilsson, U., Wikner, C., Kostikowa, T. and Schneider, G. (1997) Examination of the thiamin binding site in yeast transketolase by site-directed mutagenesis. Eur. J. Biochem. 244, 646-652
    • (1997) Eur. J. Biochem. , vol.244 , pp. 646-652
    • Meshalkina, L.1    Nilsson, U.2    Wikner, C.3    Kostikowa, T.4    Schneider, G.5
  • 42
    • 0030853640 scopus 로고    scopus 로고
    • Aspartate 155 of human transketolase is essential for thiamine diphospnate-magnesium binding, and cofactor binding is required for dimer formation
    • Wang, J. J. L., Martin, P. R. and Singleton, C. K. (1997) Aspartate 155 of human transketolase is essential for thiamine diphospnate-magnesium binding, and cofactor binding is required for dimer formation. Biochim. Biophys. Acta 1341, 165-172
    • (1997) Biochim. Biophys. Acta , vol.1341 , pp. 165-172
    • Wang, J.J.L.1    Martin, P.R.2    Singleton, C.K.3
  • 43
    • 0031029945 scopus 로고    scopus 로고
    • Examination of substrate binding in thiamin diphosphate-dependent transketolase by protein crystallography and site-directed mutagenesis
    • Nilsson, U., Meshalikina, L., Lindqvist, Y. and Schneider, G. (1997) Examination of substrate binding in thiamin diphosphate-dependent transketolase by protein crystallography and site-directed mutagenesis. J. Biol. Chem. 272, 1864-1869
    • (1997) J. Biol. Chem. , vol.272 , pp. 1864-1869
    • Nilsson, U.1    Meshalikina, L.2    Lindqvist, Y.3    Schneider, G.4
  • 44
    • 0027054829 scopus 로고
    • In vivo import of firefly luciferase into the glycosomes of Trypanosoma brucei and mutational analysis of the C-terminal targeting signal
    • Sommer, J. M., Cheng, Q., Keiler, G. and Wang, C. C. (1992) In vivo import of firefly luciferase into the glycosomes of Trypanosoma brucei and mutational analysis of the C-terminal targeting signal. Mol. Biol. Cell. 3, 749-759
    • (1992) Mol. Biol. Cell. , vol.3 , pp. 749-759
    • Sommer, J.M.1    Cheng, Q.2    Keiler, G.3    Wang, C.C.4
  • 45
    • 0028080428 scopus 로고
    • Subcellular distribution and characterization of glucosephosphate isomerase in Leishmania mexicana mexicana
    • Nyame, K., Do-Thi, C. D., Opperdoes, F. R. and Michels, P. A. (1994) Subcellular distribution and characterization of glucosephosphate isomerase in Leishmania mexicana mexicana. Mol. Biochem. Parasitol. 67, 269-279
    • (1994) Mol. Biochem. Parasitol. , vol.67 , pp. 269-279
    • Nyame, K.1    Do-Thi, C.D.2    Opperdoes, F.R.3    Michels, P.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.