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Volumn 206, Issue 12, 2003, Pages 2049-2057

Isozymes of mammalian hexokinase: Structure, subcellular localization and metabolic function

Author keywords

Hexokinase; Isozyme; Mammalian; Mitochondria; Subcellular localization

Indexed keywords

GLUCOSE 6 PHOSPHATE; HEXOKINASE; ISOENZYME;

EID: 0038714272     PISSN: 00220949     EISSN: None     Source Type: Journal    
DOI: 10.1242/jeb.00241     Document Type: Review
Times cited : (848)

References (56)
  • 3
    • 0026662331 scopus 로고
    • Functional consequences of mutation of highly conserved serine residues, found at equivalent positions in the N- and C-terminal domains of mammalian hexokinases
    • Baijal, M. and Wilson, J. E. (1992). Functional consequences of mutation of highly conserved serine residues, found at equivalent positions in the N- and C-terminal domains of mammalian hexokinases. Arch. Biochem. Biophys. 298, 271-278.
    • (1992) Arch. Biochem. Biophys. , vol.298 , pp. 271-278
    • Baijal, M.1    Wilson, J.E.2
  • 4
    • 0025797664 scopus 로고
    • Hexokinase of rat blain mitochondria: Relative importance of adenylate kinase and oxidative phosphorylation as sources of substrate ATP, and interaction with intramitochondrial compartments of ATP and ADP
    • BeltrandelRio, H. and Wilson, J. E. (1991). Hexokinase of rat blain mitochondria: relative importance of adenylate kinase and oxidative phosphorylation as sources of substrate ATP, and interaction with intramitochondrial compartments of ATP and ADP. Arch. Biochem. Biophys. 286, 183-194.
    • (1991) Arch. Biochem. Biophys. , vol.286 , pp. 183-194
    • BeltrandelRio, H.1    Wilson, J.E.2
  • 5
    • 0026722459 scopus 로고
    • Coordinated regulation of cerebral glycolysis and oxidative metabolism, mediated by mitochondrially bound hexokinase dependent on intramitochondrially generated ATP
    • BeltrandelRio, H. and Wilson, J. E. (1992a). Coordinated regulation of cerebral glycolysis and oxidative metabolism, mediated by mitochondrially bound hexokinase dependent on intramitochondrially generated ATP. Arch. Biochem. Biophys. 296, 667-677.
    • (1992) Arch. Biochem. Biophys. , vol.296 , pp. 667-677
    • BeltrandelRio, H.1    Wilson, J.E.2
  • 6
    • 0026494731 scopus 로고
    • Interaction of mitochondrially bound rat brain hexokinase with intramitochondrial compartments of ATP generated by oxidative phosphorylation and creatine kinase
    • BeltrandelRio, H. and Wilson, J. E. (1992b). Interaction of mitochondrially bound rat brain hexokinase with intramitochondrial compartments of ATP generated by oxidative phosphorylation and creatine kinase. Arch. Biochem. Biophys. 299, 116-124.
    • (1992) Arch. Biochem. Biophys. , vol.299 , pp. 116-124
    • BeltrandelRio, H.1    Wilson, J.E.2
  • 7
    • 0027404023 scopus 로고
    • Convergent evolution of similar enzymatic function on different protein folds: The hexokinase, ribokinase, and galactokinase families of sugar kinases
    • Bork, P., Sander, C. and Valencia, A. (1993). Convergent evolution of similar enzymatic function on different protein folds: the hexokinase, ribokinase, and galactokinase families of sugar kinases. Prot. Sci. 2, 31-40.
    • (1993) Prot. Sci. , vol.2 , pp. 31-40
    • Bork, P.1    Sander, C.2    Valencia, A.3
  • 9
    • 0000202516 scopus 로고    scopus 로고
    • Circulation and energy metabolism in the brain
    • ed. G. J. Siegel, B. W. Agranoff, R. W. Albers, S. K. Fisher and M. D. Uhler. Philadelphia: Lippincott, Williams & Wilkins
    • Clarke, D. D. and Sokoloff, L. (1998). Circulation and energy metabolism in the brain. In Basic Neurochemistry: Molecular, Cellular and Medical Aspects, 6th edition (ed. G. J. Siegel, B. W. Agranoff, R. W. Albers, S. K. Fisher and M. D. Uhler), pp. 637-669. Philadelphia: Lippincott, Williams & Wilkins.
    • (1998) Basic Neurochemistry: Molecular, Cellular and Medical Aspects, 6th Edition , pp. 637-669
    • Clarke, D.D.1    Sokoloff, L.2
  • 10
    • 0006857425 scopus 로고
    • The association of hexokinase with particulate fractions of brain and other tissue homogenates
    • Crane, R. K. and Sols, A. (1953). The association of hexokinase with particulate fractions of brain and other tissue homogenates. J. Biol. Chem. 203, 273-292.
    • (1953) J. Biol. Chem. , vol.203 , pp. 273-292
    • Crane, R.K.1    Sols, A.2
  • 11
    • 0028790926 scopus 로고
    • Application of a double isotope labeling method to a study of the interaction of mitochondrially bound rat brain hexokinase with intramitochondrial compartments of ATP generated by oxidative phosphorylation
    • De Cerqueira Cesar, M. and Wilson, J. E. (1995). Application of a double isotope labeling method to a study of the interaction of mitochondrially bound rat brain hexokinase with intramitochondrial compartments of ATP generated by oxidative phosphorylation. Arch. Biochem. Biophys. 324, 9-14.
    • (1995) Arch. Biochem. Biophys. , vol.324 , pp. 9-14
    • De Cerqueira Cesar, M.1    Wilson, J.E.2
  • 12
    • 0031852596 scopus 로고    scopus 로고
    • Further studies on the coupling of mitochondrially bound hexokinase to intramitochondrially compartmented ATP, generated by oxidative phosphorylation
    • De Cerqueira Cesar, M. and Wilson, J. E. (1998). Further studies on the coupling of mitochondrially bound hexokinase to intramitochondrially compartmented ATP, generated by oxidative phosphorylation. Arch. Biochem. Biophys. 350, 109-117.
    • (1998) Arch. Biochem. Biophys. , vol.350 , pp. 109-117
    • De Cerqueira Cesar, M.1    Wilson, J.E.2
  • 13
    • 0036327487 scopus 로고    scopus 로고
    • Functional characteristics of hexokinase bound to the Type A and Type B sites of bovine brain mitochondria
    • De Cerqueira Cesar, M. and Wilson, J. E. (2002). Functional characteristics of hexokinase bound to the Type A and Type B sites of bovine brain mitochondria. Arch. Biochem. Biophys. 397, 106-112.
    • (2002) Arch. Biochem. Biophys. , vol.397 , pp. 106-112
    • De Cerqueira Cesar, M.1    Wilson, J.E.2
  • 14
    • 0023153250 scopus 로고
    • Subfractionation of the outer membrane of rat brain mitochondria: Evidence for the existence of a domain containing the porinhexokinase complex
    • Dorbani, L., Jancsik, V., Lindén, M., Leterrier, J. F., Nelson, B. D. and Rendon, A. (1987). Subfractionation of the outer membrane of rat brain mitochondria: evidence for the existence of a domain containing the porinhexokinase complex. Arch. Biochem. Biophys. 252, 188-196.
    • (1987) Arch. Biochem. Biophys. , vol.252 , pp. 188-196
    • Dorbani, L.1    Jancsik, V.2    Lindén, M.3    Leterrier, J.F.4    Nelson, B.D.5    Rendon, A.6
  • 15
    • 0018801012 scopus 로고
    • Purification of a hexokinase-binding protein from the outer mitochondrial membrane
    • Felgner, P. L., Messer, J. L. and Wilson, J. E. (1979). Purification of a hexokinase-binding protein from the outer mitochondrial membrane. J. Biol. Chem. 254, 4946-4949.
    • (1979) J. Biol. Chem. , vol.254 , pp. 4946-4949
    • Felgner, P.L.1    Messer, J.L.2    Wilson, J.E.3
  • 16
    • 0020482168 scopus 로고
    • Evidence for identity between the hexokinase-binding protein and the mitochondrial porin in the outer membrane of rat liver mitochondria
    • Fiek, C., Benz, R., Roos, N. and Brdiczka, D. (1982). Evidence for identity between the hexokinase-binding protein and the mitochondrial porin in the outer membrane of rat liver mitochondria. Biochim. Blophys. Acta 688, 429-440.
    • (1982) Biochim. Blophys. Acta , vol.688 , pp. 429-440
    • Fiek, C.1    Benz, R.2    Roos, N.3    Brdiczka, D.4
  • 18
  • 19
    • 0034541155 scopus 로고    scopus 로고
    • Membrane potential-dependent conformational changes in mitochondrially bound hexokinase of brain
    • Hashimoto, M. and Wilson, J. E. (2000). Membrane potential-dependent conformational changes in mitochondrially bound hexokinase of brain. Arch. Biochem. Biophys. 384, 163-173.
    • (2000) Arch. Biochem. Biophys. , vol.384 , pp. 163-173
    • Hashimoto, M.1    Wilson, J.E.2
  • 20
    • 0033968457 scopus 로고    scopus 로고
    • Mouse hexokinase II gene: Structure, cDNA, promoter analysis, and expression pattern
    • Heikkinen, S., Supploa, S., Malkki, M. and Deeb, S. (2000). Mouse hexokinase II gene: structure, cDNA, promoter analysis, and expression pattern. Mamm. Genome 11, 91-96.
    • (2000) Mamm. Genome , vol.11 , pp. 91-96
    • Heikkinen, S.1    Supploa, S.2    Malkki, M.3    Deeb, S.4
  • 21
    • 0027953617 scopus 로고
    • Low-frequency stimulation of rat fast-twitch muscle enhances the expression of hexokinase II and both the translocation and expression of glucose transporter 4 (GLUT-4)
    • Hofmann, S. and Pette, D. (1994). Low-frequency stimulation of rat fast-twitch muscle enhances the expression of hexokinase II and both the translocation and expression of glucose transporter 4 (GLUT-4). Eur. J. Biochem. 219, 307-315.
    • (1994) Eur. J. Biochem. , vol.219 , pp. 307-315
    • Hofmann, S.1    Pette, D.2
  • 22
    • 0001272626 scopus 로고
    • The intracellular distribution of glycolytic and other enzymes in rat brain homogenates and mitochondrial preparations
    • Johnson, M. K. (1960). The intracellular distribution of glycolytic and other enzymes in rat brain homogenates and mitochondrial preparations. Biochem. J. 77, 610-618.
    • (1960) Biochem. J. , vol.77 , pp. 610-618
    • Johnson, M.K.1
  • 23
    • 0032741851 scopus 로고    scopus 로고
    • Expression of hexokinase 1 and hexokinase 2 in mammary tissue of nonlactating and lactating rats: Evaluation by RT-PCR
    • Kaselonis, G. L., McCabe, E. R. B. and Gray, S. M. (1999). Expression of hexokinase 1 and hexokinase 2 in mammary tissue of nonlactating and lactating rats: Evaluation by RT-PCR. Mol. Gen. Metab. 68, 371-374.
    • (1999) Mol. Gen. Metab. , vol.68 , pp. 371-374
    • Kaselonis, G.L.1    McCabe, E.R.B.2    Gray, S.M.3
  • 24
    • 0013808687 scopus 로고
    • Multiple forms of hexokinase in the rat: Tissue distribution, age dependency, and properties
    • Katzen, H. M. and Schimke, R. T. (1965). Multiple forms of hexokinase in the rat: Tissue distribution, age dependency, and properties. Proc. Natl. Acad. Sci. USA 54, 1218-1225.
    • (1965) Proc. Natl. Acad. Sci. USA , vol.54 , pp. 1218-1225
    • Katzen, H.M.1    Schimke, R.T.2
  • 25
    • 0023686353 scopus 로고
    • Mitochondrial boundary membrane contact sites in brain: Points of hexokinase and creatine kinase location, and control of Ca2+ transport
    • Kottke, M., Adam, V., Riesinger, I., Bremm, G., Bosch, W., Brdiczka, D., Sandri, G. and Panfili, E. (1988). Mitochondrial boundary membrane contact sites in brain: points of hexokinase and creatine kinase location, and control of Ca2+ transport. Biochim. Biophys. Acta 935, 87-102.
    • (1988) Biochim. Biophys. Acta , vol.935 , pp. 87-102
    • Kottke, M.1    Adam, V.2    Riesinger, I.3    Bremm, G.4    Bosch, W.5    Brdiczka, D.6    Sandri, G.7    Panfili, E.8
  • 26
    • 0014934381 scopus 로고
    • Hexokinase binding sites on mitochondrial membranes
    • Kropp, E. S. and Wilson, J. E. (1970). Hexokinase binding sites on mitochondrial membranes. Biochem. Biophys. Res. Commun. 38, 74-79.
    • (1970) Biochem. Biophys. Res. Commun. , vol.38 , pp. 74-79
    • Kropp, E.S.1    Wilson, J.E.2
  • 27
    • 0027508151 scopus 로고
    • Brain hexokinase and intramitochondrial compartments of ATP: Fact and artifact
    • Laterveer, F., Nicolay, K., BeltrandelRio, H. and Wilson, J. E. (1993). Brain hexokinase and intramitochondrial compartments of ATP: fact and artifact. Arch. Biochem. Biophys. 306, 285-286.
    • (1993) Arch. Biochem. Biophys. , vol.306 , pp. 285-286
    • Laterveer, F.1    Nicolay, K.2    BeltrandelRio, H.3    Wilson, J.E.4
  • 28
    • 0020485742 scopus 로고
    • Pore protein and the hexokinase-binding protein from the outer membrane of rat liver mitochondria are identical
    • Lindén, M., Gellerfors, P. and Nelson, B. D. (1982). Pore protein and the hexokinase-binding protein from the outer membrane of rat liver mitochondria are identical. FEBS Lett. 141, 189-192.
    • (1982) FEBS Lett. , vol.141 , pp. 189-192
    • Lindén, M.1    Gellerfors, P.2    Nelson, B.D.3
  • 29
    • 0031260326 scopus 로고    scopus 로고
    • Two Sp sites are important cis elements regulating the upstream promoter region of the gene for rat Type I hexokinase
    • Liu, W. and Wilson, J. E. (1997). Two Sp sites are important cis elements regulating the upstream promoter region of the gene for rat Type I hexokinase. Arch. Biochem. Biophys. 346, 142-150.
    • (1997) Arch. Biochem. Biophys. , vol.346 , pp. 142-150
    • Liu, W.1    Wilson, J.E.2
  • 30
    • 0002809955 scopus 로고
    • Effect of ischemia on known substrates and cofactors of the glycolytic pathway in brain
    • Lowry, O. H., Passonneau, J. V., Hasselberger, F. X. and Schulz, D. W. (1964). Effect of ischemia on known substrates and cofactors of the glycolytic pathway in brain. J. Biol. Chem. 239, 18-30.
    • (1964) J. Biol. Chem. , vol.239 , pp. 18-30
    • Lowry, O.H.1    Passonneau, J.V.2    Hasselberger, F.X.3    Schulz, D.W.4
  • 31
    • 0026128356 scopus 로고
    • Blood glucose level and morphological brain damage following cerebral ischemia
    • Marie, C. and Bralet, J. (1991). Blood glucose level and morphological brain damage following cerebral ischemia. Cerebrovasc. Brain Metab. Rev. 3, 29-38.
    • (1991) Cerebrovasc. Brain Metab. Rev. , vol.3 , pp. 29-38
    • Marie, C.1    Bralet, J.2
  • 32
    • 0029063507 scopus 로고
    • Glucose catabolism in cancer cells. Isolation, sequence, and activity of the promoter for Type II hexokinase
    • Mathupala, S. P., Rempel, A. and Pedersen, P. L. (1995). Glucose catabolism in cancer cells. Isolation, sequence, and activity of the promoter for Type II hexokinase. J. Biol. Chem. 270, 16918-16925.
    • (1995) J. Biol. Chem. , vol.270 , pp. 16918-16925
    • Mathupala, S.P.1    Rempel, A.2    Pedersen, P.L.3
  • 33
    • 0030035972 scopus 로고    scopus 로고
    • Identification and characterization of basal and cyclic AMP response elements in the promoter of the rat hexokinase II gene
    • Osawa, H., Robey, R. B., Printz, R. L. and Granner D. K. (1996). Identification and characterization of basal and cyclic AMP response elements in the promoter of the rat hexokinase II gene. J. Biol. Chem. 271, 17296-17303.
    • (1996) J. Biol. Chem. , vol.271 , pp. 17296-17303
    • Osawa, H.1    Robey, R.B.2    Printz, R.L.3    Granner, D.K.4
  • 34
    • 0033991699 scopus 로고    scopus 로고
    • Macromolecular compartmentation and channeling
    • Ovádi, J. and Srere, P. A. (2000). Macromolecular compartmentation and channeling. Intl. Rev. Cytol. 192, 255-280.
    • (2000) Intl. Rev. Cytol. , vol.192 , pp. 255-280
    • Ovádi, J.1    Srere, P.A.2
  • 35
    • 0021966411 scopus 로고
    • An intact hydrophobic N-terminal sequence is critical for binding of rat brain hexokinase to mitochondria
    • Polakis, P. G. and Wilson, J. E. (1985). An intact hydrophobic N-terminal sequence is critical for binding of rat brain hexokinase to mitochondria. Arch. Biochem. Biophys. 236, 328-337.
    • (1985) Arch. Biochem. Biophys. , vol.236 , pp. 328-337
    • Polakis, P.G.1    Wilson, J.E.2
  • 36
    • 0035787576 scopus 로고    scopus 로고
    • Cell-specific roles of glucokinase in glucose metabolism
    • Postic, C., Shiota, M. and Magnuson, M. A. (2001). Cell-specific roles of glucokinase in glucose metabolism. Recent Prog. Horm. Res. 56, 195-217.
    • (2001) Recent Prog. Horm. Res. , vol.56 , pp. 195-217
    • Postic, C.1    Shiota, M.2    Magnuson, M.A.3
  • 37
    • 0026680847 scopus 로고
    • Localization of the Type III isozyme of hexokinase at the nuclear periphery
    • Preller, A. and Wilson, J. E. (1992). Localization of the Type III isozyme of hexokinase at the nuclear periphery. Arch. Biochem. Biophys. 294, 482-492.
    • (1992) Arch. Biochem. Biophys. , vol.294 , pp. 482-492
    • Preller, A.1    Wilson, J.E.2
  • 38
    • 0023090673 scopus 로고
    • Hexokinase isozymes from the Novikoff hepatoma. Purification, kinetic and structural characterization, with emphasis on hexokinase C
    • Radojkovíc, J. and Ureta, T. (1987). Hexokinase isozymes from the Novikoff hepatoma. Purification, kinetic and structural characterization, with emphasis on hexokinase C. Biochem. J. 242, 895-903.
    • (1987) Biochem. J. , vol.242 , pp. 895-903
    • Radojkovíc, J.1    Ureta, T.2
  • 39
    • 0035339662 scopus 로고    scopus 로고
    • The hexokinase 2 protein regulates the expression of the GLK1, HXK1 and HXK2 genes of Saccharomyces cerevisiae
    • Rodríguez, A., de la Cera, T., Herrero, P. and Moreno, F. (2001). The hexokinase 2 protein regulates the expression of the GLK1, HXK1 and HXK2 genes of Saccharomyces cerevisiae. Biochem. J. 355, 625-631.
    • (2001) Biochem. J. , vol.355 , pp. 625-631
    • Rodríguez, A.1    De La Cera, T.2    Herrero, P.3    Moreno, F.4
  • 40
    • 0014198143 scopus 로고
    • Mitochondrial hexokinase: Release, rebinding, and location
    • Rose, I. A. and Warms, J. V. B. (1967). Mitochondrial hexokinase: release, rebinding, and location. J. Biol. Chem. 242, 1635-1645.
    • (1967) J. Biol. Chem. , vol.242 , pp. 1635-1645
    • Rose, I.A.1    Warms, J.V.B.2
  • 41
    • 0033615550 scopus 로고    scopus 로고
    • Characterization of the rat Type III hexokinase gene promoter. A functional octamer 1 motif is critical for basal promoter activity
    • Sebastian, S., White, J. A. and Wilson, J. E. (1999). Characterization of the rat Type III hexokinase gene promoter. A functional octamer 1 motif is critical for basal promoter activity. J. Biol. Chem. 274, 31700-31706.
    • (1999) J. Biol. Chem. , vol.274 , pp. 31700-31706
    • Sebastian, S.1    White, J.A.2    Wilson, J.E.3
  • 42
    • 0034696843 scopus 로고    scopus 로고
    • Anabolic function of the Type II isozyme of hexokinase in hepatic lipid synthesis
    • Sebastian, S., Horton, J. D. and Wilson, J. E. (2000). Anabolic function of the Type II isozyme of hexokinase in hepatic lipid synthesis. Biochem. Biophys. Res. Commun. 270, 886-891.
    • (2000) Biochem. Biophys. Res. Commun. , vol.270 , pp. 886-891
    • Sebastian, S.1    Horton, J.D.2    Wilson, J.E.3
  • 43
    • 0035498843 scopus 로고    scopus 로고
    • The human gen for the Type III isozyme of hexokinase. Structure, basal promoter, and evolution
    • Sebastian, S., Edassery, S. and Wilson, J. E. (2001). The human gen for the Type III isozyme of hexokinase. Structure, basal promoter, and evolution. Arch. Biochem. Biophys. 395, 113-120.
    • (2001) Arch. Biochem. Biophys. , vol.395 , pp. 113-120
    • Sebastian, S.1    Edassery, S.2    Wilson, J.E.3
  • 44
    • 0028279307 scopus 로고
    • Steady state transcript levels of the type II hexokinase and type 1 glucose transporter in human tumor cells
    • Shinohara, Y., Yamamoto, K., Kogure, K., Ichihara, J. and Terada, H. (1994). Steady state transcript levels of the type II hexokinase and type 1 glucose transporter in human tumor cells. Cancer Lett. 82, 27-32.
    • (1994) Cancer Lett. , vol.82 , pp. 27-32
    • Shinohara, Y.1    Yamamoto, K.2    Kogure, K.3    Ichihara, J.4    Terada, H.5
  • 45
    • 0031238860 scopus 로고    scopus 로고
    • Structural determinants for the intracellular localization of the isozymes of mammalian hexokinase: Intracellular localization of fusion constructs incorporating structural elements from the hexokinase isozymes and the green fluorescent protein
    • Sui, D. and Wilson, J. E. (1997). Structural determinants for the intracellular localization of the isozymes of mammalian hexokinase: Intracellular localization of fusion constructs incorporating structural elements from the hexokinase isozymes and the green fluorescent protein. Arch. Biochem. Biophys. 345, 111-125.
    • (1997) Arch. Biochem. Biophys. , vol.345 , pp. 111-125
    • Sui, D.1    Wilson, J.E.2
  • 47
    • 0028819431 scopus 로고
    • Functional organization of mammalian hexokinases: Characterization of chimeric hexokinases constructed from the N- and C-terminal halves of the rat Type I and Type II isozymes
    • Tsai, H. J. and Wilson, J. E. (1995). Functional organization of mammalian hexokinases: Characterization of chimeric hexokinases constructed from the N- and C-terminal halves of the rat Type I and Type II isozymes. Arch. Biochem. Biophys. 316, 206-214.
    • (1995) Arch. Biochem. Biophys. , vol.316 , pp. 206-214
    • Tsai, H.J.1    Wilson, J.E.2
  • 48
    • 0029886531 scopus 로고    scopus 로고
    • Functional organization of mammalian hexokinases. Both N- and C-terminal halves of the rat Type II isozyme possess catalytic sites
    • Tsai, H. J. and Wilson, J. E. (1996). Functional organization of mammalian hexokinases. Both N- and C-terminal halves of the rat Type II isozyme possess catalytic sites. Arch. Biochem. Biophys. 329, 17-23.
    • (1996) Arch. Biochem. Biophys. , vol.329 , pp. 17-23
    • Tsai, H.J.1    Wilson, J.E.2
  • 49
    • 0031568855 scopus 로고    scopus 로고
    • Functional organization of mammalian hexokinases. Characterization of the rat Type III isozyme and its chimeric forms, constructed with the N- and C-terminal halves of the Type I and Type II isozymes
    • Tsai, H. J. and Wilson, J. E. (1997). Functional organization of mammalian hexokinases. Characterization of the rat Type III isozyme and its chimeric forms, constructed with the N- and C-terminal halves of the Type I and Type II isozymes. Arch. Biochem. Biophys. 338, 183-192.
    • (1997) Arch. Biochem. Biophys. , vol.338 , pp. 183-192
    • Tsai, H.J.1    Wilson, J.E.2
  • 50
    • 0017831488 scopus 로고
    • The role of isozymes in metabolism: A model of metabolic pathways as the basis for the biological role of isozymes
    • Ureta, T. (1978). The role of isozymes in metabolism: A model of metabolic pathways as the basis for the biological role of isozymes. Curr. Top. Cell. Regul. 13, 233-258.
    • (1978) Curr. Top. Cell. Regul. , vol.13 , pp. 233-258
    • Ureta, T.1
  • 51
    • 0024415432 scopus 로고
    • Isolation and characterization of the discrete N- and C-terminal halves of rat brain hexokinase: Retention of full catalytic activity in the isolated C-terminal half
    • White, T. K. and Wilson, J. E. (1989). Isolation and characterization of the discrete N- and C-terminal halves of rat brain hexokinase: Retention of full catalytic activity in the isolated C-terminal half. Arch. Biochem. Biophys. 274, 373-393.
    • (1989) Arch. Biochem. Biophys. , vol.274 , pp. 373-393
    • White, T.K.1    Wilson, J.E.2
  • 52
    • 0030296430 scopus 로고    scopus 로고
    • Isolation of the promoter for Type I hexokinase from rat
    • White, J. A., Liu, W. and Wilson, J. E. (1996). Isolation of the promoter for Type I hexokinase from rat. Arch. Biochem. Biophys. 335, 161-172.
    • (1996) Arch. Biochem. Biophys. , vol.335 , pp. 161-172
    • White, J.A.1    Liu, W.2    Wilson, J.E.3
  • 53
    • 85132263639 scopus 로고
    • Regulation of mammalian hexokinase activity
    • ed. R. Beitner. Boca Raton, FL: CRC Press, Inc.
    • Wilson, J. E. (1985). Regulation of mammalian hexokinase activity. In Regulation of Carbohydrate Metabolism, Vol. I (ed. R. Beitner), pp. 45-85. Boca Raton, FL: CRC Press, Inc.
    • (1985) Regulation of Carbohydrate Metabolism , vol.1 , pp. 45-85
    • Wilson, J.E.1
  • 55
    • 0031044417 scopus 로고    scopus 로고
    • An introduction to the isoenzymes of mammalian hexokinase types I-III
    • Wilson, J. E. (1997). An introduction to the isoenzymes of mammalian hexokinase types I-III. Biochem. Soc. Trans. 25, 103-108.
    • (1997) Biochem. Soc. Trans. , vol.25 , pp. 103-108
    • Wilson, J.E.1
  • 56
    • 0024246133 scopus 로고
    • Rat brain hexokinase: The hydrophobic N-terminus of the mitochondrially bound enzyme is inserted in the lipid bilayer
    • Xie, G. and Wilson, J. E. (1988). Rat brain hexokinase: The hydrophobic N-terminus of the mitochondrially bound enzyme is inserted in the lipid bilayer. Arch. Biochem. Biophys. 267, 803-810.
    • (1988) Arch. Biochem. Biophys. , vol.267 , pp. 803-810
    • Xie, G.1    Wilson, J.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.