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Volumn 76, Issue 1, 1998, Pages 107-113

Purification and kinetic characterization of hexokinase and glucose-6- phosphate dehydrogenase from Schizosaccharomyces pombe

Author keywords

Glucose 6 phosphate dehydrogenase; Yeast hexokinase

Indexed keywords

ADENOSINE TRIPHOSPHATE; GLUCOSE; GLUCOSE 6 PHOSPHATE DEHYDROGENASE; GUANOSINE TRIPHOSPHATE; HEXOKINASE; MAGNESIUM ION; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE;

EID: 0032458781     PISSN: 08298211     EISSN: None     Source Type: Journal    
DOI: 10.1139/bcb-76-1-107     Document Type: Article
Times cited : (31)

References (42)
  • 1
    • 0014652956 scopus 로고
    • The occurrence of a modified Entner-Doudoroff pathway in Clostridium aceticum
    • Andreesen, J.R., and Gottschalk, G. 1969. The occurrence of a modified Entner-Doudoroff pathway in Clostridium aceticum. Arch. Mikrobiol. 69: 160-170.
    • (1969) Arch. Mikrobiol. , vol.69 , pp. 160-170
    • Andreesen, J.R.1    Gottschalk, G.2
  • 2
    • 0016687069 scopus 로고
    • Sigmoid curves, non-linear double-reciprocal plots and allosterism
    • Bardsley, W.G., and Childs, R.E. 1975. Sigmoid curves, non-linear double-reciprocal plots and allosterism. Biochem. J. 149: 313-328.
    • (1975) Biochem. J. , vol.149 , pp. 313-328
    • Bardsley, W.G.1    Childs, R.E.2
  • 3
    • 0022549877 scopus 로고
    • Metabolism of glucose via a modified Entner-Doudoroff pathway in the thermoacidophilic archaebacterium, Thermoplasma acidophilum
    • Budgen, N., and Danson, M.J. 1986. Metabolism of glucose via a modified Entner-Doudoroff pathway in the thermoacidophilic archaebacterium, Thermoplasma acidophilum. FEBS Lett. 196: 207-210.
    • (1986) FEBS Lett. , vol.196 , pp. 207-210
    • Budgen, N.1    Danson, M.J.2
  • 4
    • 50549159930 scopus 로고
    • The kinetics of enzyme-catalyzed reactions with two or more substrates or products. I. Nomenclature and rate equations
    • Cleland, W.W. 1963a. The kinetics of enzyme-catalyzed reactions with two or more substrates or products. I. Nomenclature and rate equations. Biochim. Biophys. Acta, 67: 104-137.
    • (1963) Biochim. Biophys. Acta , vol.67 , pp. 104-137
    • Cleland, W.W.1
  • 5
    • 50549188738 scopus 로고
    • The kinetics of enzyme-catalyzed reactions with two or more substrates or products. II. Inhibition: Nomenclature and theory
    • Cleland, W.W. 1963b. The kinetics of enzyme-catalyzed reactions with two or more substrates or products. II. Inhibition: nomenclature and theory. Biochim. Biophys. Acta, 67: 173-187.
    • (1963) Biochim. Biophys. Acta , vol.67 , pp. 173-187
    • Cleland, W.W.1
  • 7
    • 0021696802 scopus 로고
    • Glucose metabolism in the extreme thermoacidophilic archaebacterium Sulfolobus solfaturicus
    • DeRosa, N., Gambacorta, A., Nicolaus, B., Giardina, P., Poerio, E., and Buonocore, V. 1984. Glucose metabolism in the extreme thermoacidophilic archaebacterium Sulfolobus solfaturicus. Biochem. J. 224: 407-414.
    • (1984) Biochem. J. , vol.224 , pp. 407-414
    • DeRosa, N.1    Gambacorta, A.2    Nicolaus, B.3    Giardina, P.4    Poerio, E.5    Buonocore, V.6
  • 8
    • 0016043671 scopus 로고
    • Regulation of the pentose phosphate cycle
    • Eggleston, L.V., and Krebs, H.A. 1974. Regulation of the pentose phosphate cycle. Biochem. J. 138: 423-435.
    • (1974) Biochem. J. , vol.138 , pp. 423-435
    • Eggleston, L.V.1    Krebs, H.A.2
  • 9
    • 76949122636 scopus 로고
    • Glucose and gluconic acid oxidation of Pseudomonas saccarophila
    • Entner, N., and Doudoroff, M. 1952. Glucose and gluconic acid oxidation of Pseudomonas saccarophila. J. Biol. Chem. 196: 853-862.
    • (1952) J. Biol. Chem. , vol.196 , pp. 853-862
    • Entner, N.1    Doudoroff, M.2
  • 10
    • 0026478668 scopus 로고
    • The Enter-Doudoroff pathway in Escherichia coli is induced for oxidative glucose metabolism via pyrroloquinoline quinone-dependent glucose dehydrogenase
    • Fliege, R., Tong, S., Shibata, A., Nikerson, K.W., and Conway, T. 1992. The Enter-Doudoroff pathway in Escherichia coli is induced for oxidative glucose metabolism via pyrroloquinoline quinone-dependent glucose dehydrogenase. Appl. Environ. Microbiol. 58: 3826-3829.
    • (1992) Appl. Environ. Microbiol. , vol.58 , pp. 3826-3829
    • Fliege, R.1    Tong, S.2    Shibata, A.3    Nikerson, K.W.4    Conway, T.5
  • 11
    • 0022386994 scopus 로고
    • Initial rate and isotope exchange studies of rat skeletal muscle hexokinase
    • Ganson, N.J., and Fromm, H.J. 1985. Initial rate and isotope exchange studies of rat skeletal muscle hexokinase. J. Biol. Chem. 260: 12 099-12 105.
    • (1985) J. Biol. Chem. , vol.260 , pp. 12099-12105
    • Ganson, N.J.1    Fromm, H.J.2
  • 12
    • 0013630755 scopus 로고
    • Regulation of glucose-6-phosphate dehydrogenase in blue-green algae
    • Grossman, A., and McGowan, R.E. 1975. Regulation of glucose-6-phosphate dehydrogenase in blue-green algae. Plant Physiol. 55: 658-662.
    • (1975) Plant Physiol. , vol.55 , pp. 658-662
    • Grossman, A.1    McGowan, R.E.2
  • 13
    • 0016244592 scopus 로고
    • Glucose-6-phosphate dehydrogenase of human blood platelets, kinetics and regulatory properties
    • Kosow, D.P. 1974. Glucose-6-phosphate dehydrogenase of human blood platelets, kinetics and regulatory properties. Arch. Biochem. Biophys. 102: 186-193.
    • (1974) Arch. Biochem. Biophys. , vol.102 , pp. 186-193
    • Kosow, D.P.1
  • 14
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of the head of bacteriophage T4
    • London
    • Laemmli, U.K. 1970. Cleavage of structural proteins during assembly of the head of bacteriophage T4. Nature (London), 227: 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 15
    • 0016703817 scopus 로고
    • D-Glucose-6-phosphate dehydrogenase (Entner-Doudoroff enzyme) from Pseudomonas fluorescens
    • Lessmann, D., Schmiz, K-L., and Kurz, G. 1975. D-Glucose-6-phosphate dehydrogenase (Entner-Doudoroff enzyme) from Pseudomonas fluorescens. Eur. J. Biochem. 59: 545-559.
    • (1975) Eur. J. Biochem. , vol.59 , pp. 545-559
    • Lessmann, D.1    Schmiz, K.-L.2    Kurz, G.3
  • 16
    • 0018296923 scopus 로고
    • Glucose-6-phosphate dehydrogenases
    • Levy, H.R. 1979. Glucose-6-phosphate dehydrogenases. Adv. Enzymol. 48: 97-192.
    • (1979) Adv. Enzymol. , vol.48 , pp. 97-192
    • Levy, H.R.1
  • 17
    • 0021103822 scopus 로고
    • Glucose-6-phosphate dehydrogenase from Leuconostoc mesenteroides: Revised kinetic mechanism and kinetics of ATP inhibition
    • Levy, H.R., Christoff, M., Ingulli, J., and Ho, E.M.L. 1983. Glucose-6-phosphate dehydrogenase from Leuconostoc mesenteroides: revised kinetic mechanism and kinetics of ATP inhibition. Arch. Biochem. Biophys. 222: 473-488.
    • (1983) Arch. Biochem. Biophys. , vol.222 , pp. 473-488
    • Levy, H.R.1    Christoff, M.2    Ingulli, J.3    Ho, E.M.L.4
  • 18
    • 73049130725 scopus 로고
    • A method for determining the sedimentation behavior of enzymes: Application to protein mixtures
    • Martin, R.G., and Ames, B.N. 1961. A method for determining the sedimentation behavior of enzymes: application to protein mixtures. J. Biol. Chem. 236: 1372-1379.
    • (1961) J. Biol. Chem. , vol.236 , pp. 1372-1379
    • Martin, R.G.1    Ames, B.N.2
  • 19
    • 0025259390 scopus 로고
    • Hexokinases and glucokinases
    • Middleton, R.J. 1990. Hexokinases and glucokinases. Biochem. Soc. Trans. 18: 180-183.
    • (1990) Biochem. Soc. Trans. , vol.18 , pp. 180-183
    • Middleton, R.J.1
  • 20
    • 9844256470 scopus 로고
    • Protein determination for large numbers of samples
    • Miller, G.L. 1959. Protein determination for large numbers of samples. Anal. Chem. 31: 964.
    • (1959) Anal. Chem. , vol.31 , pp. 964
    • Miller, G.L.1
  • 21
    • 77956849541 scopus 로고
    • Physiological and cytological methods for Schizosaccharomyces pombe
    • Mitchison, J.M. 1970. Physiological and cytological methods for Schizosaccharomyces pombe. Methods Cell Physiol. 4: 131-165.
    • (1970) Methods Cell Physiol. , vol.4 , pp. 131-165
    • Mitchison, J.M.1
  • 22
    • 0014293085 scopus 로고
    • Kinetic study of yeast hexokinase. I. Steady-state kinetics
    • Noat, G., Ricard, J., Borel, M., and Got, C. 1968. Kinetic study of yeast hexokinase. I. Steady-state kinetics. Eur. J. Biochem. 5: 55-70.
    • (1968) Eur. J. Biochem. , vol.5 , pp. 55-70
    • Noat, G.1    Ricard, J.2    Borel, M.3    Got, C.4
  • 23
    • 0014766662 scopus 로고
    • Kinetic study of yeast hexokinase. Inhibition of the reaction by magnesium and ATP
    • Noat, G. Ricard, J. Borel, M., and Got, C. 1970. Kinetic study of yeast hexokinase. Inhibition of the reaction by magnesium and ATP. Eur. J. Biochem. 13: 347-363.
    • (1970) Eur. J. Biochem. , vol.13 , pp. 347-363
    • Noat, G.1    Ricard, J.2    Borel, M.3    Got, C.4
  • 24
    • 0015217628 scopus 로고
    • Glucose-6-phosphate dehydrogenase from Leuconostoc mesenteroides. Kinetic studies
    • Olive, C., Geroch, M.E., and Levy, H.R. 1971. Glucose-6-phosphate dehydrogenase from Leuconostoc mesenteroides. Kinetic studies. J. Biol. Chem. 246: 2047-2057.
    • (1971) J. Biol. Chem. , vol.246 , pp. 2047-2057
    • Olive, C.1    Geroch, M.E.2    Levy, H.R.3
  • 25
    • 85012741391 scopus 로고
    • A possible role for kinetic reaction mechanism dependent substrate and product effects in enzyme regulation
    • Edited by B.L. Horecker and E.R. Stadtman. Academic Press, New York
    • Purich, D.L., and Fromm, H.J. 1972. A possible role for kinetic reaction mechanism dependent substrate and product effects in enzyme regulation. In Current topics in cellular regulation. Edited by B.L. Horecker and E.R. Stadtman. Academic Press, New York. pp. 131-167.
    • (1972) Current Topics in Cellular Regulation , pp. 131-167
    • Purich, D.L.1    Fromm, H.J.2
  • 26
    • 0015552481 scopus 로고
    • The hexokinases: Kinetic, physical and regulatory properties
    • Purich, D.L., Fromm, H.J., and Rudolph, F.B. 1973. The hexokinases: kinetic, physical and regulatory properties. Adv. Enzymol. 39: 249-326.
    • (1973) Adv. Enzymol. , vol.39 , pp. 249-326
    • Purich, D.L.1    Fromm, H.J.2    Rudolph, F.B.3
  • 27
    • 0015519070 scopus 로고
    • The theory of alternative substrates in enzyme kinetics and its application to yeast hexokinase
    • Ricard, J., Noat, G., Got, C., and Borel, M. 1972. The theory of alternative substrates in enzyme kinetics and its application to yeast hexokinase. Eur. J. Biochem. 31: 14-24.
    • (1972) Eur. J. Biochem. , vol.31 , pp. 14-24
    • Ricard, J.1    Noat, G.2    Got, C.3    Borel, M.4
  • 28
    • 0025772770 scopus 로고
    • Glucose repression in Saccharomyces cerevisiae is directly associated with hexose phosphorylation by hexokinase PI and PII
    • Rose, M., Albig, W., and Entian, K.-D. 1991. Glucose repression in Saccharomyces cerevisiae is directly associated with hexose phosphorylation by hexokinase PI and PII. Eur. J. Biochem. 199: 511-518.
    • (1991) Eur. J. Biochem. , vol.199 , pp. 511-518
    • Rose, M.1    Albig, W.2    Entian, K.-D.3
  • 29
    • 0014961140 scopus 로고    scopus 로고
    • Use of isotope competition and alternative substrates for studying the kinetic mechanism of enzyme action. I. Experiments with hexokinase and alcohol dehydrogenase
    • Rudolph, F.B., and Fromm, H.J. Use of isotope competition and alternative substrates for studying the kinetic mechanism of enzyme action. I. Experiments with hexokinase and alcohol dehydrogenase. Biochemistry, 9: 4660-4665.
    • Biochemistry , vol.9 , pp. 4660-4665
    • Rudolph, F.B.1    Fromm, H.J.2
  • 30
    • 0003518480 scopus 로고
    • Wiley Interscience, New York
    • Segel, I.H. 1975. Enzyme kinetics. Wiley Interscience, New York. pp. 247-248.
    • (1975) Enzyme Kinetics , pp. 247-248
    • Segel, I.H.1
  • 31
    • 0021348564 scopus 로고
    • Gluconate catabolism in cowpea rhizobia: Evidence for a ketogluconate pathway
    • Stowers, M.D., and Elkan, G.H. 1984. Gluconate catabolism in cowpea rhizobia: evidence for a ketogluconate pathway. Arch. Microbiol. 137: 3-9.
    • (1984) Arch. Microbiol. , vol.137 , pp. 3-9
    • Stowers, M.D.1    Elkan, G.H.2
  • 32
    • 0026512705 scopus 로고
    • Glucose repression in the yeast, Saccharomyces cerevisiae
    • Trumbly, R.J. 1992. Glucose repression in the yeast, Saccharomyces cerevisiae. Mol. Microbiol. 6: 15-21.
    • (1992) Mol. Microbiol. , vol.6 , pp. 15-21
    • Trumbly, R.J.1
  • 33
    • 0017823087 scopus 로고
    • Kinetic and mechanistic studies of methylated liver alcohol dehydrogenase
    • Tsai, C.S. 1978. Kinetic and mechanistic studies of methylated liver alcohol dehydrogenase. Biochem. J. 173: 483-496.
    • (1978) Biochem. J. , vol.173 , pp. 483-496
    • Tsai, C.S.1
  • 34
    • 0001754690 scopus 로고    scopus 로고
    • D-Glucose metabolism in Saccharomyces cerevisiae versus Schizosaccharomyces pombe
    • Tsai, C.S. 1996. D-Glucose metabolism in Saccharomyces cerevisiae versus Schizosaccharomyces pombe. Trends Comp. Biochem. Physiol. 2: 101-112.
    • (1996) Trends Comp. Biochem. Physiol. , vol.2 , pp. 101-112
    • Tsai, C.S.1
  • 35
    • 0000707936 scopus 로고
    • Diauxic growth of the fission yeast, Schizosaccharomyces pombe in mixture of D-glucose and ethanol or acetate
    • Tsai, C.S., Aveledo, A.J., McDonald, I.J., and Johnson, B.F. 1987. Diauxic growth of the fission yeast, Schizosaccharomyces pombe in mixture of D-glucose and ethanol or acetate. Can. J. Microbiol. 33: 593-597.
    • (1987) Can. J. Microbiol. , vol.33 , pp. 593-597
    • Tsai, C.S.1    Aveledo, A.J.2    McDonald, I.J.3    Johnson, B.F.4
  • 36
    • 0027105168 scopus 로고
    • Enzyme activities of D-glucose metabolism in the fission yeast, Schizosaccharomyces pombe
    • Tsai, C.S., Shi, J.L., Su, Y.J., Beehler, B.W., and Beck, B. 1992. Enzyme activities of D-glucose metabolism in the fission yeast, Schizosaccharomyces pombe. Can. J. Microbiol. 38: 1313-1319.
    • (1992) Can. J. Microbiol. , vol.38 , pp. 1313-1319
    • Tsai, C.S.1    Shi, J.L.2    Su, Y.J.3    Beehler, B.W.4    Beck, B.5
  • 37
    • 0028870089 scopus 로고
    • Carbon-13 NMR studies and purification of gluconate pathway enzymes from Schizosaccharomyces pombe
    • Tsai, C.S., Ye, H.G., and Shi, J.L. 1995a. Carbon-13 NMR studies and purification of gluconate pathway enzymes from Schizosaccharomyces pombe. Arch. Biochem. Biophys. 316: 155-162.
    • (1995) Arch. Biochem. Biophys. , vol.316 , pp. 155-162
    • Tsai, C.S.1    Ye, H.G.2    Shi, J.L.3
  • 38
    • 0028809157 scopus 로고
    • Kinetic studies of gluconate pathway enzymes from Schizosaccharomyces pombe
    • Tsai, C.S., Shi, J.L., and Ye, H.G. 1995b. Kinetic studies of gluconate pathway enzymes from Schizosaccharomyces pombe. Arch. Biochem. Biophys. 316: 163-168.
    • (1995) Arch. Biochem. Biophys. , vol.316 , pp. 163-168
    • Tsai, C.S.1    Shi, J.L.2    Ye, H.G.3
  • 39
    • 0025030281 scopus 로고
    • Regulation of sugar and ethanol metabolism in Saccharomyces cerevisiae
    • Willis, C. 1990. Regulation of sugar and ethanol metabolism in Saccharomyces cerevisiae. Crit. Rev. Biochem. Mol. Biol. 25: 245-280.
    • (1990) Crit. Rev. Biochem. Mol. Biol. , vol.25 , pp. 245-280
    • Willis, C.1
  • 41
    • 0019882018 scopus 로고
    • Silver staining of proteins in polyacrylamide gels
    • Wray, W., Boulikas, T., Wray, V.P., and Hancock, R. 1981. Silver staining of proteins in polyacrylamide gels. Anal. Biochem. 118: 197-203.
    • (1981) Anal. Biochem. , vol.118 , pp. 197-203
    • Wray, W.1    Boulikas, T.2    Wray, V.P.3    Hancock, R.4
  • 42
    • 0015918157 scopus 로고
    • Hemolytic anemia and G6PD deficiency
    • Washington, D.C.
    • Yoshida, A. 1973. Hemolytic anemia and G6PD deficiency. Science (Washington, D.C.), 179: 532-537.
    • (1973) Science , vol.179 , pp. 532-537
    • Yoshida, A.1


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