메뉴 건너뛰기




Volumn 1606, Issue 1-3, 2003, Pages 83-93

Uncoupling of the glucose growth defect and the deregulation of glycolysis in Saccharomyces cerevisiae tps1 mutants expressing trehalose-6-phosphate-insensitive hexokinase from Schizosaccharomyces pombe

Author keywords

Fermentation; Glycolysis; Hexokinase; TPS1 gene; Trehalose 6 phosphate synthase

Indexed keywords

FUNGAL ENZYME; FUNGAL PROTEIN; GLUCOKINASE; GLUCOSE; GLUCOSE 6 PHOSPHATE; TREHALOSE 6 PHOSPHATE; TREHALOSE 6 PHOSPHATE INSENSITIVE HEXOKINASE; TREHALOSE 6 PHOSPHATE SYNTHETASE; UNCLASSIFIED DRUG;

EID: 0142042964     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0005-2728(03)00086-0     Document Type: Article
Times cited : (33)

References (52)
  • 1
    • 0026451211 scopus 로고
    • Characterization of the 56 kDa subunit of the yeast trehalose-6-phosphate synthase and cloning of its gene reveal its identity with the product of CIF1, a regulator of carbon catabolite inactivation
    • Bell W., Klaassen P., Ohnacker M., Boller T., Herweijer M., Schoppink P., van der Zee P., Wiemken A. Characterization of the 56 kDa subunit of the yeast trehalose-6-phosphate synthase and cloning of its gene reveal its identity with the product of CIF1, a regulator of carbon catabolite inactivation. Eur. J. Biochem. 209:1992;951-959.
    • (1992) Eur. J. Biochem. , vol.209 , pp. 951-959
    • Bell, W.1    Klaassen, P.2    Ohnacker, M.3    Boller, T.4    Herweijer, M.5    Schoppink, P.6    Van Der Zee, P.7    Wiemken, A.8
  • 2
    • 0027446935 scopus 로고
    • Disruption of TPS2, the gene encoding the 100-kDa subunit of the trehalose-6-phosphate synthase/phosphatase complex in Saccharomyces cerevisiae, causes accumulation of trehalose-6-phosphate and loss of trehalose-6-phosphate phosphatase activity
    • De Virgilio C., Buerckert N., Bell W., Jeno P., Boller T., Wiemken A. Disruption of TPS2, the gene encoding the 100-kDa subunit of the trehalose-6-phosphate synthase/phosphatase complex in Saccharomyces cerevisiae, causes accumulation of trehalose-6-phosphate and loss of trehalose-6-phosphate phosphatase activity. Eur. J. Biochem. 212:1993;315-323.
    • (1993) Eur. J. Biochem. , vol.212 , pp. 315-323
    • De Virgilio, C.1    Buerckert, N.2    Bell, W.3    Jeno, P.4    Boller, T.5    Wiemken, A.6
  • 3
    • 0028985536 scopus 로고
    • Trehalose synthase: Guard to the gate of glycolysis in yeast?
    • Thevelein J.M., Hohmann S. Trehalose synthase: guard to the gate of glycolysis in yeast? Trends Biochem. Sci. 20:1995;3-10.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 3-10
    • Thevelein, J.M.1    Hohmann, S.2
  • 5
    • 0015972675 scopus 로고
    • Isolation of a regulatory mutant of fructose-1,6-diphosphatase in Saccharomyces carlsbergensis
    • van de Poll K.W., Kerkenaar A., Schamhart D.H.J. Isolation of a regulatory mutant of fructose-1,6-diphosphatase in Saccharomyces carlsbergensis. J. Bacteriol. 117:1974;965-970.
    • (1974) J. Bacteriol. , vol.117 , pp. 965-970
    • Van De Poll, K.W.1    Kerkenaar, A.2    Schamhart, D.H.J.3
  • 6
    • 0017404565 scopus 로고
    • Characterization of a regulatory mutant of fructose 1,6-bisphosphatase in Saccharomyces carlsbergensis
    • van de Poll K.W., Schamhart D.H. Characterization of a regulatory mutant of fructose 1,6-bisphosphatase in Saccharomyces carlsbergensis. Mol. Gen. Genet. 154:1977;61-66.
    • (1977) Mol. Gen. Genet. , vol.154 , pp. 61-66
    • Van De Poll, K.W.1    Schamhart, D.H.2
  • 7
    • 0026521266 scopus 로고
    • Molecular cloning of CIF1, a yeast gene necessary for growth on glucose
    • Gonzalez M.I., Stucka R., Blazquez M.A., Feldmann H., Gancedo C. Molecular cloning of CIF1, a yeast gene necessary for growth on glucose. Yeast. 8:1992;183-192.
    • (1992) Yeast , vol.8 , pp. 183-192
    • Gonzalez, M.I.1    Stucka, R.2    Blazquez, M.A.3    Feldmann, H.4    Gancedo, C.5
  • 8
    • 0027534678 scopus 로고
    • The growth and signalling defects of the ggs1 (fdp1/byp1) deletion mutant on glucose are suppressed by a deletion of the gene encoding hexokinase PII
    • Hohmann S., Neves M.J., de Koning W., Alijo R., Ramos J., Thevelein J.M. The growth and signalling defects of the ggs1 (fdp1/byp1) deletion mutant on glucose are suppressed by a deletion of the gene encoding hexokinase PII. Curr. Genet. 23:1993;281-289.
    • (1993) Curr. Genet. , vol.23 , pp. 281-289
    • Hohmann, S.1    Neves, M.J.2    De Koning, W.3    Alijo, R.4    Ramos, J.5    Thevelein, J.M.6
  • 9
    • 0027305174 scopus 로고
    • Trehalose-6-phosphate, a new regulator of yeast glycolysis that inhibits hexokinases
    • Blazquez M.A., Lagunas R., Gancedo C., Gancedo J.M. Trehalose-6-phosphate, a new regulator of yeast glycolysis that inhibits hexokinases. FEBS Lett. 329:1993;51-54.
    • (1993) FEBS Lett. , vol.329 , pp. 51-54
    • Blazquez, M.A.1    Lagunas, R.2    Gancedo, C.3    Gancedo, J.M.4
  • 10
    • 0039295216 scopus 로고
    • The Pasteur effect in the allosteric era
    • A.E.A. Kornberg. Oxford: Pergamon
    • Sols A. The Pasteur effect in the allosteric era. Kornberg A.E.A. Reflections in Biochemistry. 1976;199-206 Pergamon, Oxford.
    • (1976) Reflections in Biochemistry , pp. 199-206
    • Sols, A.1
  • 11
    • 0025772978 scopus 로고
    • A yeast homologue of the bovine lens fibre MIP gene family complements the growth defect of a Saccharomyces cerevisiae mutant on fermentable sugars but not its defect in glucose-induced RAS-mediated cAMP signaling
    • Van Aelst L., Hohmann S., Zimmermann F.K., Jans A.W.H., Thevelein J.M. A yeast homologue of the bovine lens fibre MIP gene family complements the growth defect of a Saccharomyces cerevisiae mutant on fermentable sugars but not its defect in glucose-induced RAS-mediated cAMP signaling. EMBO J. 10:1991;2095-2104.
    • (1991) EMBO J. , vol.10 , pp. 2095-2104
    • Van Aelst, L.1    Hohmann, S.2    Zimmermann, F.K.3    Jans, A.W.H.4    Thevelein, J.M.5
  • 12
    • 0028947362 scopus 로고
    • Fps1, a yeast member of the MIP family of channel proteins, is a facilitator for glycerol uptake and efflux and is inactive under osmotic stress
    • Luyten K., Albertyn J., Skibbe W.F., Prior B.A., Ramos J., Thevelein J.M., Hohmann S. Fps1, a yeast member of the MIP family of channel proteins, is a facilitator for glycerol uptake and efflux and is inactive under osmotic stress. EMBO J. 14:1995;1360-1371.
    • (1995) EMBO J. , vol.14 , pp. 1360-1371
    • Luyten, K.1    Albertyn, J.2    Skibbe, W.F.3    Prior, B.A.4    Ramos, J.5    Thevelein, J.M.6    Hohmann, S.7
  • 13
    • 0029598442 scopus 로고
    • Mode of action of the qcr9 and cat3 mutations in restoring the ability of Saccharomyces cerevisiae tps1 mutants to grow on glucose
    • Blazquez M.A., Gancedo C. Mode of action of the qcr9 and cat3 mutations in restoring the ability of Saccharomyces cerevisiae tps1 mutants to grow on glucose. Mol. Gen. Genet. 249:1995;655-664.
    • (1995) Mol. Gen. Genet. , vol.249 , pp. 655-664
    • Blazquez, M.A.1    Gancedo, C.2
  • 14
    • 0029948606 scopus 로고    scopus 로고
    • Evidence for trehalose-6-phosphate-dependent and -independent mechanisms in the control of sugar influx into yeast glycolysis
    • Hohmann S., Bell W., Neves M.J., Valckx D., Thevelein J.M. Evidence for trehalose-6-phosphate-dependent and -independent mechanisms in the control of sugar influx into yeast glycolysis. Mol. Microbiol. 20:1996;981-991.
    • (1996) Mol. Microbiol. , vol.20 , pp. 981-991
    • Hohmann, S.1    Bell, W.2    Neves, M.J.3    Valckx, D.4    Thevelein, J.M.5
  • 15
    • 0031891707 scopus 로고    scopus 로고
    • During the initiation of fermentation overexpression of hexokinase PII in yeast transiently causes a similar deregulation of glycolysis as deletion of Tps1
    • Ernandes J.R., De Meirsman C., Rolland F., Winderickx J., de Winde J., Brandão R.L., Thevelein J.M. During the initiation of fermentation overexpression of hexokinase PII in yeast transiently causes a similar deregulation of glycolysis as deletion of Tps1. Yeast. 14:1998;255-269.
    • (1998) Yeast , vol.14 , pp. 255-269
    • Ernandes, J.R.1    De Meirsman, C.2    Rolland, F.3    Winderickx, J.4    De Winde, J.5    Brandão, R.L.6    Thevelein, J.M.7
  • 16
    • 0033927803 scopus 로고    scopus 로고
    • Reconstitution of ethanolic fermentation in permeabilized spheroplasts of wild-type and trehalose-6-phosphate synthase mutants of the yeast Saccharomyces cerevisiae
    • Noubhani A., Bunoust O., Rigoulet M., Thevelein J.M. Reconstitution of ethanolic fermentation in permeabilized spheroplasts of wild-type and trehalose-6-phosphate synthase mutants of the yeast Saccharomyces cerevisiae. Eur. J. Biochem. 267:2000;4566-4576.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 4566-4576
    • Noubhani, A.1    Bunoust, O.2    Rigoulet, M.3    Thevelein, J.M.4
  • 17
    • 0035155847 scopus 로고    scopus 로고
    • Analysis and modification of trehalose-6-phosphate levels in the yeast Saccharomyces cerevisiae using Bacillus subtilis phosphotrehalase
    • Van Vaeck C., Wera S., Van Dijck P., Thevelein J.M. Analysis and modification of trehalose-6-phosphate levels in the yeast Saccharomyces cerevisiae using Bacillus subtilis phosphotrehalase. Biochem. J. 353:2001;157-162.
    • (2001) Biochem. J. , vol.353 , pp. 157-162
    • Van Vaeck, C.1    Wera, S.2    Van Dijck, P.3    Thevelein, J.M.4
  • 18
    • 0034663598 scopus 로고    scopus 로고
    • Expression of Escherichia coli otsA in a Saccharomyces cerevisiae tps1 mutant restores trehalose-6-phosphate levels and partly restores growth and fermentation with glucose and control of glucose influx into glycolysis
    • Bonini B.M., Van Vaeck C., Larsson C., Gustafsson L., Ma P., Winderickx J., Van Dijck P., Thevelein J.M. Expression of Escherichia coli otsA in a Saccharomyces cerevisiae tps1 mutant restores trehalose-6-phosphate levels and partly restores growth and fermentation with glucose and control of glucose influx into glycolysis. Biochem. J. 350:2000;261-268.
    • (2000) Biochem. J. , vol.350 , pp. 261-268
    • Bonini, B.M.1    Van Vaeck, C.2    Larsson, C.3    Gustafsson, L.4    Ma, P.5    Winderickx, J.6    Van Dijck, P.7    Thevelein, J.M.8
  • 20
    • 0027493391 scopus 로고
    • Disruption of the Kluyveromyces lactis GGS1 gene causes inability to grow on glucose and fructose and is suppressed by mutations that reduce sugar uptake
    • Luyten K., de Koning W., Tesseur I., Ruiz M.C., Ramos J., Cobbaert P., Thevelein J.M., Hohmann S. Disruption of the Kluyveromyces lactis GGS1 gene causes inability to grow on glucose and fructose and is suppressed by mutations that reduce sugar uptake. Eur. J. Biochem. 217:1993;701-713.
    • (1993) Eur. J. Biochem. , vol.217 , pp. 701-713
    • Luyten, K.1    De Koning, W.2    Tesseur, I.3    Ruiz, M.C.4    Ramos, J.5    Cobbaert, P.6    Thevelein, J.M.7    Hohmann, S.8
  • 21
    • 0028270766 scopus 로고
    • Trehalose-6-P synthase is dispensable for growth on glucose but not for spore germination in Schizosaccharomyces pombe
    • Blazquez M.A., Stucka R., Feldmann H., Gancedo C. Trehalose-6-P synthase is dispensable for growth on glucose but not for spore germination in Schizosaccharomyces pombe. J. Bacteriol. 176:1994;3895-3902.
    • (1994) J. Bacteriol. , vol.176 , pp. 3895-3902
    • Blazquez, M.A.1    Stucka, R.2    Feldmann, H.3    Gancedo, C.4
  • 22
    • 0031025298 scopus 로고    scopus 로고
    • The filamentous fungus Aspergillus niger contains two "differentially regulated" trehalose-6-phosphate synthase-encoding genes, tpsA and tpsB
    • Wolschek M.F., Kubicek C.P. The filamentous fungus Aspergillus niger contains two "differentially regulated" trehalose-6-phosphate synthase-encoding genes, tpsA and tpsB. J. Biol. Chem. 272:1997;2729-2735.
    • (1997) J. Biol. Chem. , vol.272 , pp. 2729-2735
    • Wolschek, M.F.1    Kubicek, C.P.2
  • 23
    • 0029766086 scopus 로고    scopus 로고
    • Cloning and biochemical characterisation of an Aspergillus niger glucokinase. Evidence for the presence of separate glucokinase and hexokinase enzymes
    • Panneman H., Ruijter G.J., van den Broeck H.C., Driever E.T., Visser J. Cloning and biochemical characterisation of an Aspergillus niger glucokinase. Evidence for the presence of separate glucokinase and hexokinase enzymes. Eur. J. Biochem. 240:1996;518-525.
    • (1996) Eur. J. Biochem. , vol.240 , pp. 518-525
    • Panneman, H.1    Ruijter, G.J.2    Van Den Broeck, H.C.3    Driever, E.T.4    Visser, J.5
  • 24
    • 0032033441 scopus 로고    scopus 로고
    • Isolation and molecular characterization of the Arabidopsis TPS1 gene, encoding trehalose-6-phosphate synthase
    • Blazquez M.A., Santos E., Flores C.L., Martinez Zapater J.M., Salinas J., Gancedo C. Isolation and molecular characterization of the Arabidopsis TPS1 gene, encoding trehalose-6-phosphate synthase. Plant J. 13:1998;685-689.
    • (1998) Plant J. , vol.13 , pp. 685-689
    • Blazquez, M.A.1    Santos, E.2    Flores, C.L.3    Martinez Zapater, J.M.4    Salinas, J.5    Gancedo, C.6
  • 25
    • 0029187847 scopus 로고
    • Trehalose and trehalase in plants: Recent developments
    • Müller J., Boller T., Wiemken A. Trehalose and trehalase in plants: recent developments. Plant Sci. 112:1995;1-9.
    • (1995) Plant Sci. , vol.112 , pp. 1-9
    • Müller, J.1    Boller, T.2    Wiemken, A.3
  • 26
    • 0032053108 scopus 로고    scopus 로고
    • Sensing trehalose biosynthesis in plants
    • Goddijn O., Smeekens S. Sensing trehalose biosynthesis in plants. Plant J. 14:1998;143-146.
    • (1998) Plant J. , vol.14 , pp. 143-146
    • Goddijn, O.1    Smeekens, S.2
  • 28
    • 0035205611 scopus 로고    scopus 로고
    • An unexpected plethora of trehalose biosynthesis genes in Arabidopsis thaliana
    • Leyman B., Van Dijck P., Thevelein J.M. An unexpected plethora of trehalose biosynthesis genes in Arabidopsis thaliana. Trends Plant Sci. 6:2001;510-513.
    • (2001) Trends Plant Sci. , vol.6 , pp. 510-513
    • Leyman, B.1    Van Dijck, P.2    Thevelein, J.M.3
  • 29
    • 0030956438 scopus 로고    scopus 로고
    • Expression of the yeast trehalose-6-phosphate synthase gene in transgenic tobacco plants: Pleiotropic phenotypes include drought tolerance
    • Romero C., Belles J.M., Vaya J.L., Serrano R., CulianezMacia F.A. Expression of the yeast trehalose-6-phosphate synthase gene in transgenic tobacco plants: pleiotropic phenotypes include drought tolerance. Planta. 201:1997;293-297.
    • (1997) Planta , vol.201 , pp. 293-297
    • Romero, C.1    Belles, J.M.2    Vaya, J.L.3    Serrano, R.4    CulianezMacia, F.A.5
  • 31
    • 0035209371 scopus 로고    scopus 로고
    • Enhancing photosynthesis with sugar signals
    • Paul M., Pellny T., Goddijn O. Enhancing photosynthesis with sugar signals. Trends Plant Sci. 6:2001;197-200.
    • (2001) Trends Plant Sci. , vol.6 , pp. 197-200
    • Paul, M.1    Pellny, T.2    Goddijn, O.3
  • 32
    • 0344500842 scopus 로고    scopus 로고
    • Trehalose metabolism in sugar sensing and plant development
    • Müller J., Wiemken A., Aeschbacher R. Trehalose metabolism in sugar sensing and plant development. Plant Sci. 147:1999;37-47.
    • (1999) Plant Sci. , vol.147 , pp. 37-47
    • Müller, J.1    Wiemken, A.2    Aeschbacher, R.3
  • 34
    • 0037103791 scopus 로고    scopus 로고
    • Truncation of Arabidopsis thaliana and Selaginella lepidophylla trehalose-6-phosphate synthase unlocks high catalytic activity and supports high trehalose levels on expression in yeast
    • Van Dijck P., Mascorro-Gallardo J.O., De Bus M., Royackers K., Iturriaga G., Thevelein J.M. Truncation of Arabidopsis thaliana and Selaginella lepidophylla trehalose-6-phosphate synthase unlocks high catalytic activity and supports high trehalose levels on expression in yeast. Biochem. J. 366:2002;63-71.
    • (2002) Biochem. J. , vol.366 , pp. 63-71
    • Van Dijck, P.1    Mascorro-Gallardo, J.O.2    De Bus, M.3    Royackers, K.4    Iturriaga, G.5    Thevelein, J.M.6
  • 35
    • 0024977417 scopus 로고
    • Elevated recombination rates in transcriptionally active DNA
    • Thomas B.J., Rothstein R.J. Elevated recombination rates in transcriptionally active DNA. Cell. 56:1989;619-630.
    • (1989) Cell , vol.56 , pp. 619-630
    • Thomas, B.J.1    Rothstein, R.J.2
  • 36
    • 0026864596 scopus 로고
    • Complementation of Saccharomyces cerevisiae auxotrophic mutants by Arabidopsis thaliana cDNAs
    • Minet M., Dufour M.E., Lacroute F. Complementation of Saccharomyces cerevisiae auxotrophic mutants by Arabidopsis thaliana cDNAs. Plant J. 2:1992;417-422.
    • (1992) Plant J. , vol.2 , pp. 417-422
    • Minet, M.1    Dufour, M.E.2    Lacroute, F.3
  • 37
    • 0026670522 scopus 로고
    • Fission yeast and a plant have functional homologues of the Sar1 and Sec12 proteins involved in ER to Golgi traffic in budding yeast
    • d'Enfert C., Gensse M., Gaillardin C. Fission yeast and a plant have functional homologues of the Sar1 and Sec12 proteins involved in ER to Golgi traffic in budding yeast. EMBO J. 11:1992;4205-4211.
    • (1992) EMBO J. , vol.11 , pp. 4205-4211
    • D'Enfert, C.1    Gensse, M.2    Gaillardin, C.3
  • 39
    • 0026715777 scopus 로고
    • A method for the determination of changes of glycolytic metabolites in yeast on a subsecond time scale using extraction at neutral pH
    • de Koning W., van Dam K. A method for the determination of changes of glycolytic metabolites in yeast on a subsecond time scale using extraction at neutral pH. Anal. Biochem. 204:1992;118-123.
    • (1992) Anal. Biochem. , vol.204 , pp. 118-123
    • De Koning, W.1    Van Dam, K.2
  • 40
    • 0027947964 scopus 로고
    • Quantification of trehalose in biological samples with a conidial trehalase from the thermophilic fungus Humicola grisea var. thermoidea
    • Neves M.J., Terenzi H.F., Leone F.A., Jorge J.A. Quantification of trehalose in biological samples with a conidial trehalase from the thermophilic fungus Humicola grisea var. thermoidea. World J. Microbiol. Biotechnol. 10:1994;17-19.
    • (1994) World J. Microbiol. Biotechnol. , vol.10 , pp. 17-19
    • Neves, M.J.1    Terenzi, H.F.2    Leone, F.A.3    Jorge, J.A.4
  • 41
    • 0015238985 scopus 로고
    • A kinetic study of glycolytic enzyme synthesis in yeast
    • Maitra P.K., Lobo Z. A kinetic study of glycolytic enzyme synthesis in yeast. J. Biol. Chem. 246:1971;475-488.
    • (1971) J. Biol. Chem. , vol.246 , pp. 475-488
    • Maitra, P.K.1    Lobo, Z.2
  • 42
    • 77957005673 scopus 로고
    • Preparation and assay of deoxyribonucleic acids from animal tissues
    • Zamenhoff S. Preparation and assay of deoxyribonucleic acids from animal tissues. Methods Enzymol. 3:1957;696-704.
    • (1957) Methods Enzymol. , vol.3 , pp. 696-704
    • Zamenhoff, S.1
  • 43
    • 0030891998 scopus 로고    scopus 로고
    • Kinetic characterization of individual hexose transporters of Saccharomyces cerevisiae and their relation to the triggering mechanisms of glucose repression
    • Reifenberger E., Boles E., Ciriacy M. Kinetic characterization of individual hexose transporters of Saccharomyces cerevisiae and their relation to the triggering mechanisms of glucose repression. Eur. J. Biochem. 245:1997;324-333.
    • (1997) Eur. J. Biochem. , vol.245 , pp. 324-333
    • Reifenberger, E.1    Boles, E.2    Ciriacy, M.3
  • 44
    • 0343930747 scopus 로고    scopus 로고
    • Schizosaccharomyces pombe possesses an unusual and a conventional hexokinase: Biochemical and molecular characterization of both hexokinases
    • Petit T., Blazquez M.A., Gancedo C. Schizosaccharomyces pombe possesses an unusual and a conventional hexokinase: biochemical and molecular characterization of both hexokinases. FEBS Lett. 378:1996;185-189.
    • (1996) FEBS Lett. , vol.378 , pp. 185-189
    • Petit, T.1    Blazquez, M.A.2    Gancedo, C.3
  • 45
    • 2242461686 scopus 로고
    • The hexokinases
    • P.D. Boyer. New York: Academic Press
    • Colowick S.P. The hexokinases. Boyer P.D. The Enzymes. 1973;1-48 Academic Press, New York.
    • (1973) The Enzymes , pp. 1-48
    • Colowick, S.P.1
  • 46
    • 0028272233 scopus 로고
    • Characterization and regulatory properties of a single hexokinase from the citric acid accumulating fungus Aspergillus niger
    • Steinbock F., Choojun S., Held I., Roehr M., Kubicek C.P. Characterization and regulatory properties of a single hexokinase from the citric acid accumulating fungus Aspergillus niger. Biochim. Biophys. Acta (G). 1200:1994;215-223.
    • (1994) Biochim. Biophys. Acta (G) , vol.1200 , pp. 215-223
    • Steinbock, F.1    Choojun, S.2    Held, I.3    Roehr, M.4    Kubicek, C.P.5
  • 47
    • 0032533977 scopus 로고    scopus 로고
    • Cloning and biochemical characterisation of Aspergillus niger hexokinase-the enzyme is strongly inhibited by physiological concentrations of trehalose 6-phosphate
    • Panneman H., Ruijter G.J.G., van den Broeck H.C., Visser J. Cloning and biochemical characterisation of Aspergillus niger hexokinase-the enzyme is strongly inhibited by physiological concentrations of trehalose 6-phosphate. Eur. J. Biochem. 258:1998;223-232.
    • (1998) Eur. J. Biochem. , vol.258 , pp. 223-232
    • Panneman, H.1    Ruijter, G.J.G.2    Van Den Broeck, H.C.3    Visser, J.4
  • 48
    • 0032697881 scopus 로고    scopus 로고
    • Molecular cloning and characterization of the gene HXK1 encoding the hexokinase from Yarrowia lipolytica
    • Petit T., Gancedo C. Molecular cloning and characterization of the gene HXK1 encoding the hexokinase from Yarrowia lipolytica. Yeast. 15:1999;1573-1584.
    • (1999) Yeast , vol.15 , pp. 1573-1584
    • Petit, T.1    Gancedo, C.2
  • 49
    • 1842376846 scopus 로고    scopus 로고
    • Hexokinase as a sugar sensor in higher plants
    • Jang J.C., Leon P., Zhou L., Sheen J. Hexokinase as a sugar sensor in higher plants. Plant Cell. 9:1997;5-19.
    • (1997) Plant Cell , vol.9 , pp. 5-19
    • Jang, J.C.1    Leon, P.2    Zhou, L.3    Sheen, J.4
  • 50
    • 0034528042 scopus 로고    scopus 로고
    • The role of hexokinase in plant sugar signal transduction and growth and development
    • Xiao W., Sheen J., Jang J.C. The role of hexokinase in plant sugar signal transduction and growth and development. Plant Mol. Biol. 44:2000;451-461.
    • (2000) Plant Mol. Biol. , vol.44 , pp. 451-461
    • Xiao, W.1    Sheen, J.2    Jang, J.C.3
  • 51
    • 0033102055 scopus 로고    scopus 로고
    • Mannose inhibits Arabidopsis germination via a hexokinase-mediated step
    • Pego J.V., Weisbeek P.J., Smeekens S.C.M. Mannose inhibits Arabidopsis germination via a hexokinase-mediated step. Plant Physiol. 119:1999;1017-1023.
    • (1999) Plant Physiol. , vol.119 , pp. 1017-1023
    • Pego, J.V.1    Weisbeek, P.J.2    Smeekens, S.C.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.