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Volumn 142, Issue 12, 1996, Pages 3337-3345

Metabolic adaptation of Trichomonas vaginalis to growth rate and glucose availability

Author keywords

Chemostat; Energy metabolism; Glucose; Metabolic control analysis; Trichomonas vaginalis

Indexed keywords

ACETIC ACID; ALANINE; COENZYME A TRANSFERASE; FRUCTOKINASE; FRUCTOSE BISPHOSPHATE ALDOLASE; GLUCOSE; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; GLYCEROL; GLYCEROL 3 PHOSPHATE DEHYDROGENASE; ISOMERASE; LACTATE DEHYDROGENASE; LACTIC ACID; MALATE DEHYDROGENASE (DECARBOXYLATING); PYRUVATE KINASE;

EID: 0030462786     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/13500872-142-12-3337     Document Type: Article
Times cited : (16)

References (41)
  • 1
    • 0345611317 scopus 로고
    • Glycolysis and pentose phosphate cycle in Trichomonas vaginalis. I. Enzyme activity pattern and the constant proportion quintet
    • Arese, P. & Cappuccinelli, P. (1974). Glycolysis and pentose phosphate cycle in Trichomonas vaginalis. I. Enzyme activity pattern and the constant proportion quintet. Int J Biochem 5, 859-865.
    • (1974) Int J Biochem , vol.5 , pp. 859-865
    • Arese, P.1    Cappuccinelli, P.2
  • 2
    • 0028247085 scopus 로고
    • Hysteresis of cytosolic NADP-malic enzyme II from Trypanosoma cruzi
    • Avilan, L. & Garcia, P. (1994). Hysteresis of cytosolic NADP-malic enzyme II from Trypanosoma cruzi. Mol Biochem Parasitol 65, 225-232.
    • (1994) Mol Biochem Parasitol , vol.65 , pp. 225-232
    • Avilan, L.1    Garcia, P.2
  • 3
    • 0000717689 scopus 로고
    • Enzymes as biochemical reagents: Hexokinase
    • Edited by H. U. Bergmeyer. New York: Academic Press
    • Bergmeyer, H. U. (1974). Enzymes as biochemical reagents: hexokinase. In Methods of Enzymatic Analysis, pp. 473. Edited by H. U. Bergmeyer. New York: Academic Press.
    • (1974) Methods of Enzymatic Analysis , pp. 473
    • Bergmeyer, H.U.1
  • 4
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the qualification of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976). A rapid and sensitive method for the qualification 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
  • 6
    • 0022270676 scopus 로고
    • 13C-NMR reveals glycerol as an unexpected major metabolite of the protozoan parasite Trichomonas vaginalis
    • Chapman, A., Linstead, D. J., Lloyd, D. & Williams, J. (1985). 13C-NMR reveals glycerol as an unexpected major metabolite of the protozoan parasite Trichomonas vaginalis. FEBS Lett 191, 287-292.
    • (1985) FEBS Lett , vol.191 , pp. 287-292
    • Chapman, A.1    Linstead, D.J.2    Lloyd, D.3    Williams, J.4
  • 7
    • 0002439035 scopus 로고
    • Energy metabolism in anaerobic protozoa
    • Edited by J. J. Marr & M. Müller. New York: Academic Press
    • Coombs, G. H. & Müller, M. (1995). Energy metabolism in anaerobic protozoa. In Biochemistry and Molecular Biology of Parasites, pp. 33-47. Edited by J. J. Marr & M. Müller. New York: Academic Press.
    • (1995) Biochemistry and Molecular Biology of Parasites , pp. 33-47
    • Coombs, G.H.1    Müller, M.2
  • 8
    • 0026653206 scopus 로고
    • Effects of overexpression of phosphofructokinase on glycolysis in the yeast Saccharomyces cerevisiae
    • Davies, S. E. & Brindle, K. M. (1992). Effects of overexpression of phosphofructokinase on glycolysis in the yeast Saccharomyces cerevisiae. Biochemistry 31, 4729-4735.
    • (1992) Biochemistry , vol.31 , pp. 4729-4735
    • Davies, S.E.1    Brindle, K.M.2
  • 9
    • 0001419545 scopus 로고
    • The establishment of various trichomonads of animals and man in axenic cultures
    • Diamond, L. S. (1957). The establishment of various trichomonads of animals and man in axenic cultures. J Parasitol 43, 488-490.
    • (1957) J Parasitol , vol.43 , pp. 488-490
    • Diamond, L.S.1
  • 10
    • 0000944767 scopus 로고
    • Triglycerides and glycerol: Determination after alkaline hydrolysis
    • Edited by H. U. Bergmeyer. Weinheim: Verlag Chemie
    • Eggstein, M. & Kuhlmann, E. (1974). Triglycerides and glycerol: determination after alkaline hydrolysis. In Methods of Enzymatic Analysis, pp. 1825-1835. Edited by H. U. Bergmeyer. Weinheim: Verlag Chemie.
    • (1974) Methods of Enzymatic Analysis , pp. 1825-1835
    • Eggstein, M.1    Kuhlmann, E.2
  • 11
    • 0018885152 scopus 로고
    • Trichomonas vaginalis: Reevaluation of its clinical presentation and laboratory diagnosis
    • Fouts, A. C. & Kraus, S. J. (1980). Trichomonas vaginalis: reevaluation of its clinical presentation and laboratory diagnosis. J Infect Dis 141, 137-143.
    • (1980) J Infect Dis , vol.141 , pp. 137-143
    • Fouts, A.C.1    Kraus, S.J.2
  • 12
    • 0000831018 scopus 로고
    • L-(+)-Lactate: Determination with lactate dehydrogenase and NAD
    • Edited by H. U. Bergmeyer. Weinheim: Verlag Chemie
    • Gutmann, I. & Wahlefeld, A. W. (1974). L-(+)-Lactate: determination with lactate dehydrogenase and NAD. In Methods of Enzymatic Analysis, pp. 1464-1475. Edited by H. U. Bergmeyer. Weinheim: Verlag Chemie.
    • (1974) Methods of Enzymatic Analysis , pp. 1464-1475
    • Gutmann, I.1    Wahlefeld, A.W.2
  • 14
    • 0027393935 scopus 로고
    • Identification, purification and separation of different isozymes of NADP-specific malic enzyme from Tritrichomonas foetus
    • Hrdy, I., Mertens, E. & Van Schaftingen, E. (1993). Identification, purification and separation of different isozymes of NADP-specific malic enzyme from Tritrichomonas foetus. Mol Biochem Parasitol 57, 253-260.
    • (1993) Mol Biochem Parasitol , vol.57 , pp. 253-260
    • Hrdy, I.1    Mertens, E.2    Van Schaftingen, E.3
  • 16
    • 0025309496 scopus 로고
    • Properties of Trichomonas vaginalis grown under chemostat controlled growth conditions
    • Lenker, M. W. & Alderete, J. F. (1990). Properties of Trichomonas vaginalis grown under chemostat controlled growth conditions. Genitourin Med 66, 193-199.
    • (1990) Genitourin Med , vol.66 , pp. 193-199
    • Lenker, M.W.1    Alderete, J.F.2
  • 17
    • 0021796772 scopus 로고
    • Metronidazole inhibition of hydrogen production in vivo in drug-sensitive and resistant strains of Trichomonas vaginalis
    • Lloyd, D. & Kristensen, B. (1985). Metronidazole inhibition of hydrogen production in vivo in drug-sensitive and resistant strains of Trichomonas vaginalis. J Gen Microbiol 131, 849-853.
    • (1985) J Gen Microbiol , vol.131 , pp. 849-853
    • Lloyd, D.1    Kristensen, B.2
  • 18
    • 1842642613 scopus 로고
    • The effects of environmental factors on the metabolism of Giardia and Trichomonas
    • Edited by G. H. Coombs & M. J. North. London: Taylor & Francis
    • Lloyd, D. & Paget, T. A. (1991). The effects of environmental factors on the metabolism of Giardia and Trichomonas. In Biochemical Protozoology, pp. 92-101. Edited by G. H. Coombs & M. J. North. London: Taylor & Francis.
    • (1991) Biochemical Protozoology , pp. 92-101
    • Lloyd, D.1    Paget, T.A.2
  • 19
    • 0018069328 scopus 로고
    • Effect of oxygen and carbon dioxide on the growth of Trichomonas vaginalis and Tritrichomonas foetus
    • Mack, S. R. & Müller, M. (1978). Effect of oxygen and carbon dioxide on the growth of Trichomonas vaginalis and Tritrichomonas foetus. J Parasitol 64, 927-929.
    • (1978) J Parasitol , vol.64 , pp. 927-929
    • Mack, S.R.1    Müller, M.2
  • 20
    • 0019215536 scopus 로고
    • End products of carbohydrate metabolism in Trichomonas vaginalis
    • Mack, S. R. & Müller, M. (1980). End products of carbohydrate metabolism in Trichomonas vaginalis. Comp Biochem Physiol 67B, 213-216.
    • (1980) Comp Biochem Physiol , vol.67 B , pp. 213-216
    • Mack, S.R.1    Müller, M.2
  • 21
    • 0027423316 scopus 로고
    • A glyceraldehyde-3-phosphate dehydrogenase with eubacterial features in the amitochondriate eukaryote, Trichomonas vaginalis
    • Markos, A., Miretsky, A. & Müller, M. (1993). A glyceraldehyde-3-phosphate dehydrogenase with eubacterial features in the amitochondriate eukaryote, Trichomonas vaginalis. J Mol Evol 37, 631-643.
    • (1993) J Mol Evol , vol.37 , pp. 631-643
    • Markos, A.1    Miretsky, A.2    Müller, M.3
  • 22
    • 0025856178 scopus 로고
    • Pyrophosphate-dependent phosphofructokinase, an anaerobic glycolytic enzyme?
    • Mertens, E. (1991). Pyrophosphate-dependent phosphofructokinase, an anaerobic glycolytic enzyme? FEBS Lett 285, 1-5.
    • (1991) FEBS Lett , vol.285 , pp. 1-5
    • Mertens, E.1
  • 23
    • 0027412292 scopus 로고
    • ATP versus pyrophosphate: Glycolysis revisited in parasitic protists
    • Mertens, E. (1993). ATP versus pyrophosphate: glycolysis revisited in parasitic protists. Parasitol Today 9, 122-126.
    • (1993) Parasitol Today , vol.9 , pp. 122-126
    • Mertens, E.1
  • 24
    • 0025047810 scopus 로고
    • Glucokinase and fructokinase of Trichomonas vaginalis and Tritrichomonas foetus
    • Mertens, E. & Müller, M. (1990). Glucokinase and fructokinase of Trichomonas vaginalis and Tritrichomonas foetus. J Protozool 37, 384-388.
    • (1990) J Protozool , vol.37 , pp. 384-388
    • Mertens, E.1    Müller, M.2
  • 25
    • 0024445334 scopus 로고
    • Presence of a fructose-2,6-bisphosphate-insensitive pyrophosphate: Fructose-6-phosphate phosphotransferase in the anaerobic protozoa Tritrichomonas foetus, Trichomonas vaginalis and Isotricha prostoma
    • Mertens, E., Van Schaftingen, E. & Müller, M. (1989). Presence of a fructose-2,6-bisphosphate-insensitive pyrophosphate: fructose-6-phosphate phosphotransferase in the anaerobic protozoa Tritrichomonas foetus, Trichomonas vaginalis and Isotricha prostoma. Mol Biochem Parasitol 31, 183-190.
    • (1989) Mol Biochem Parasitol , vol.31 , pp. 183-190
    • Mertens, E.1    Van Schaftingen, E.2    Müller, M.3
  • 26
    • 0021753882 scopus 로고
    • Simultaneous purification of hexokinase, class-I fructose-bisphosphate aldolase, triosephosphate isomerase and phosphoglycerate kinase from Trypanosoma brucei
    • Misset, O. & Opperdoes, F. R. (1984). Simultaneous purification of hexokinase, class-I fructose-bisphosphate aldolase, triosephosphate isomerase and phosphoglycerate kinase from Trypanosoma brucei. Eur J Biochem 144, 475-483.
    • (1984) Eur J Biochem , vol.144 , pp. 475-483
    • Misset, O.1    Opperdoes, F.R.2
  • 27
    • 0023095941 scopus 로고
    • Glyceraldehyde-phosphate dehydrogenase from Trypanosoma brucei. Comparison of the glycosomal and cytosolic isoenzymes
    • Misset, O., Van Beeumen, J., Lambeir, A. M., Van der Meer, R. & Opperdoes, F. R. (1987). Glyceraldehyde-phosphate dehydrogenase from Trypanosoma brucei. Comparison of the glycosomal and cytosolic isoenzymes. Eur J Biochem 162, 501-507.
    • (1987) Eur J Biochem , vol.162 , pp. 501-507
    • Misset, O.1    Van Beeumen, J.2    Lambeir, A.M.3    Van Der Meer, R.4    Opperdoes, F.R.5
  • 28
    • 0024151128 scopus 로고
    • Energy metabolism of protozoa without mitochondria
    • Müller, M. (1988). Energy metabolism of protozoa without mitochondria. Annu Rev Microbiol 42, 465-488.
    • (1988) Annu Rev Microbiol , vol.42 , pp. 465-488
    • Müller, M.1
  • 29
    • 0001910082 scopus 로고
    • Biochemistry of Trichomonas vaginalis
    • Edited by B. M. Honigberg. New York: Springer
    • Müller, M. (1989). Biochemistry of Trichomonas vaginalis. In Trichomonads Parasitic in Humans, pp. 53-83. Edited by B. M. Honigberg. New York: Springer.
    • (1989) Trichomonads Parasitic in Humans , pp. 53-83
    • Müller, M.1
  • 30
    • 0040692338 scopus 로고
    • Energy metabolism of anaerobic parasitic protists
    • Edited by G. H. Coombs & M. J. North. London: Taylor & Francis
    • Müller, M. (1991). Energy metabolism of anaerobic parasitic protists. In Biochemical Protozoology, pp. 80-91. Edited by G. H. Coombs & M. J. North. London: Taylor & Francis.
    • (1991) Biochemical Protozoology , pp. 80-91
    • Müller, M.1
  • 31
    • 0029084376 scopus 로고
    • Different internal metabolites trigger the induction of glycolytic gene expression in Saccharomyces cerevisiae
    • Müller, S., Boles, E., May, M. & Zimmermann, F. K. (1995). Different internal metabolites trigger the induction of glycolytic gene expression in Saccharomyces cerevisiae. J Bacteriol 177, 4517-4519.
    • (1995) J Bacteriol , vol.177 , pp. 4517-4519
    • Müller, S.1    Boles, E.2    May, M.3    Zimmermann, F.K.4
  • 32
    • 0025369916 scopus 로고
    • Trichomonas vaginalis requires traces of oxygen and high concentrations of carbon dioxide for optimal growth
    • Paget, T. A. & Lloyd, D. (1990). Trichomonas vaginalis requires traces of oxygen and high concentrations of carbon dioxide for optimal growth. Mol Biochem Parasitol 41, 65-72.
    • (1990) Mol Biochem Parasitol , vol.41 , pp. 65-72
    • Paget, T.A.1    Lloyd, D.2
  • 33
    • 0024694679 scopus 로고
    • Overproduction of glycolytic enzymes in yeast
    • Schaaff, I., Heinisch, J. & Zimmermann, F. K. (1989). Overproduction of glycolytic enzymes in yeast. Yeast 5, 285-290.
    • (1989) Yeast , vol.5 , pp. 285-290
    • Schaaff, I.1    Heinisch, J.2    Zimmermann, F.K.3
  • 34
    • 0028324169 scopus 로고
    • A nitrogen-limited, glucose-repressed, continuous culture of Saccharomyces cerevisiae
    • Sierkstra, L. N., ter Schure, E. G., Verbakel, J. M. A. & Verrips, C. T. (1994). A nitrogen-limited, glucose-repressed, continuous culture of Saccharomyces cerevisiae. Microbiology 140, 593-599.
    • (1994) Microbiology , vol.140 , pp. 593-599
    • Sierkstra, L.N.1    Ter Schure, E.G.2    Verbakel, J.M.A.3    Verrips, C.T.4
  • 35
    • 0022744840 scopus 로고
    • Anaerobic pyruvate metabolism of Tritrichomonas foetus and Trichomonas vaginalis hydrogenosomes
    • Steinbuchel, A. & Müller, M. (1986a). Anaerobic pyruvate metabolism of Tritrichomonas foetus and Trichomonas vaginalis hydrogenosomes. Mol Biochem Parasitol 20, 57-65.
    • (1986) Mol Biochem Parasitol , vol.20 , pp. 57-65
    • Steinbuchel, A.1    Müller, M.2
  • 36
    • 0022747671 scopus 로고
    • Glycerol, a metabolic end product of Trichomonas vaginalis and Tritrichomonas foetus
    • Steinbüchel, A. & Müller, M. (1986b). Glycerol, a metabolic end product of Trichomonas vaginalis and Tritrichomonas foetus. Mol Biochem Parasitol 20, 45-55.
    • (1986) Mol Biochem Parasitol , vol.20 , pp. 45-55
    • Steinbüchel, A.1    Müller, M.2
  • 37
    • 0028030877 scopus 로고
    • Carbohydrate metabolism and physiology of the parasitic protist Trichomonas vaginalis studied in chemostats
    • Ter Kuile, B. H. (1994a). Carbohydrate metabolism and physiology of the parasitic protist Trichomonas vaginalis studied in chemostats. Microbiology 140, 2495-2502.
    • (1994) Microbiology , vol.140 , pp. 2495-2502
    • Ter Kuile, B.H.1
  • 38
    • 0028169442 scopus 로고
    • Adaptation of the carbon metabolism of Trichomonas vaginalis to the nature and availability of the carbon source
    • Ter Kuile, B. H. (1994b). Adaptation of the carbon metabolism of Trichomonas vaginalis to the nature and availability of the carbon source. Microbiology 140, 2503-2510.
    • (1994) Microbiology , vol.140 , pp. 2503-2510
    • Ter Kuile, B.H.1
  • 39
    • 0026086143 scopus 로고
    • Chemostat cultures of Leishmania donovani promastigotes and Trypanosoma brucei procyclic trypomastigotes
    • Ter Kuile, B. H. & Opperdoes, F. R. (1991). Chemostat cultures of Leishmania donovani promastigotes and Trypanosoma brucei procyclic trypomastigotes. Mol Biochem Parasitol 45, 171-173.
    • (1991) Mol Biochem Parasitol , vol.45 , pp. 171-173
    • Ter Kuile, B.H.1    Opperdoes, F.R.2
  • 40
    • 0017343370 scopus 로고
    • Energy conservation in chemotrophic anaerobic bacteria
    • Thauer, R. K., Jungermann, K. & Decker, K. (1977). Energy conservation in chemotrophic anaerobic bacteria. Bacteriol Reviews 41, 100-180.
    • (1977) Bacteriol Reviews , vol.41 , pp. 100-180
    • Thauer, R.K.1    Jungermann, K.2    Decker, K.3
  • 41
    • 0001657527 scopus 로고
    • L-Alanine: Determination with alanine dehydrogenase
    • Edited by H. U. Bergmeyer. New York: Academic Press
    • Williamson, D. H. (1974). L-Alanine: determination with alanine dehydrogenase. In Methods of Enzymatic Analysis, pp. 1679-1682. Edited by H. U. Bergmeyer. New York: Academic Press.
    • (1974) Methods of Enzymatic Analysis , pp. 1679-1682
    • Williamson, D.H.1


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