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Volumn 243, Issue 1-2, 1997, Pages 442-451

Cloning, sequencing and developmental expression of phosphofructokinase from Dictyostelium discoideum

Author keywords

Allosteric regulation; Developmental gene expression; Dictyostelium discoideum; Phosphofructokinase; Yeast

Indexed keywords

6 PHOSPHOFRUCTOKINASE;

EID: 0031020105     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1997.0442a.x     Document Type: Article
Times cited : (6)

References (59)
  • 1
    • 77956892317 scopus 로고
    • Phosphofructokinase
    • Boyer, P. D., ed. Academic Press, New York
    • Bloxham, D. P. & Lardy, H. A. (1973) Phosphofructokinase, in The enzymes (Boyer, P. D., ed.) vol. 8, pp. 239-278, Academic Press, New York.
    • (1973) The Enzymes , vol.8 , pp. 239-278
    • Bloxham, D.P.1    Lardy, H.A.2
  • 2
    • 85047669951 scopus 로고
    • Allosteric regulatory properties of muscle phosphofructokinase
    • Kemp, R. G. & Foe, L. G. (1983) Allosteric regulatory properties of muscle phosphofructokinase, Mol. Cell. Biochem. 57, 147-154.
    • (1983) Mol. Cell. Biochem. , vol.57 , pp. 147-154
    • Kemp, R.G.1    Foe, L.G.2
  • 3
    • 0021883206 scopus 로고
    • Nucleotide sequence and high-level expression of the major Escherichia coli phosphofructokinase
    • Hellinga, H. W. & Evans, P. R. (1985) Nucleotide sequence and high-level expression of the major Escherichia coli phosphofructokinase, Eur. J. Biochem. 149, 363-373.
    • (1985) Eur. J. Biochem. , vol.149 , pp. 363-373
    • Hellinga, H.W.1    Evans, P.R.2
  • 5
    • 0023780743 scopus 로고
    • Liver (B-type) phosphofructokinase mRNA
    • Gehnrich, S. C., Gekakis, N. & Sul, H. S. (1988) Liver (B-type) phosphofructokinase mRNA, J. Biol. Chem. 263, 11 755-11 759.
    • (1988) J. Biol. Chem. , vol.263 , pp. 11755-11759
    • Gehnrich, S.C.1    Gekakis, N.2    Sul, H.S.3
  • 6
    • 0023664085 scopus 로고
    • The rabbit muscle phosphofructokinase gene. Implications for protein structure, function, and tissue specificity
    • Lee, C. P., Kao, M. C., French, B. A., Putney, S. D. & Chang, S. H. (1987) The rabbit muscle phosphofructokinase gene. Implications for protein structure, function, and tissue specificity, J. Biol. Chem. 262, 4195-4199.
    • (1987) J. Biol. Chem. , vol.262 , pp. 4195-4199
    • Lee, C.P.1    Kao, M.C.2    French, B.A.3    Putney, S.D.4    Chang, S.H.5
  • 8
    • 0023070868 scopus 로고
    • Nucleotide sequence of the phosphofructokinase gene from Bacillus stearothermophilus and comparison with the homologous Escherichia coli gene
    • French, B. A. & Chang, S. H. (1987) Nucleotide sequence of the phosphofructokinase gene from Bacillus stearothermophilus and comparison with the homologous Escherichia coli gene, Gene (Amst.) 54, 65-71.
    • (1987) Gene (Amst.) , vol.54 , pp. 65-71
    • French, B.A.1    Chang, S.H.2
  • 9
    • 0028111477 scopus 로고
    • Structure, distribution, and functional expression of the phosphofructokinase C isozyme
    • Gekakis, N., Johnson, R. C., Jerkins, A., Mains, R. E. & Sul, H. S. (1994) Structure, distribution, and functional expression of the phosphofructokinase C isozyme, J. Biol. Chem. 269, 3348-3355.
    • (1994) J. Biol. Chem. , vol.269 , pp. 3348-3355
    • Gekakis, N.1    Johnson, R.C.2    Jerkins, A.3    Mains, R.E.4    Sul, H.S.5
  • 10
    • 0022976785 scopus 로고
    • Crystallographic structure of allosterically inhibited phosphofructokinase at 7 Å resolution
    • Evans, P. R., Farrants, G. W. & Lawrence, M. C. (1986) Crystallographic structure of allosterically inhibited phosphofructokinase at 7 Å resolution, J. Mol. Biol. 191, 713-720.
    • (1986) J. Mol. Biol. , vol.191 , pp. 713-720
    • Evans, P.R.1    Farrants, G.W.2    Lawrence, M.C.3
  • 11
    • 0024215739 scopus 로고
    • Crystal structure of the complex of phosphofructokinase from Escherichia coli with its reaction products
    • Shirakihara, Y. & Evans, P. R. (1988) Crystal structure of the complex of phosphofructokinase from Escherichia coli with its reaction products, J. Mol. Biol. 204, 973-994.
    • (1988) J. Mol. Biol. , vol.204 , pp. 973-994
    • Shirakihara, Y.1    Evans, P.R.2
  • 12
    • 0025189804 scopus 로고
    • Structural basis of the allosteric behaviour of phosphofructokinase
    • Schirmer, T. & Evans, P. R. (1990) Structural basis of the allosteric behaviour of phosphofructokinase, Nature 343, 140-145.
    • (1990) Nature , vol.343 , pp. 140-145
    • Schirmer, T.1    Evans, P.R.2
  • 13
    • 0023668313 scopus 로고
    • Site-directed mutagenesis in the effector site of Escherichia coli phosphofructokinase
    • Lau, F. T. K., Fersht, A. R., Hellinga, H. W. & Evans, P. R. (1987) Site-directed mutagenesis in the effector site of Escherichia coli phosphofructokinase, Biochemistry 26, 4143-4148.
    • (1987) Biochemistry , vol.26 , pp. 4143-4148
    • Lau, F.T.K.1    Fersht, A.R.2    Hellinga, H.W.3    Evans, P.R.4
  • 14
    • 0023274246 scopus 로고
    • Mutations in the active site of Escherichia coli phosphofructokinase
    • Hellinga, H. W. & Evans, P. R. (1987) Mutations in the active site of Escherichia coli phosphofructokinase, Nature 327, 437-439.
    • (1987) Nature , vol.327 , pp. 437-439
    • Hellinga, H.W.1    Evans, P.R.2
  • 15
    • 0025073262 scopus 로고
    • Active-site mutants altering the cooperativity of E. coli phosphofructokinase
    • Berger, S. A. & Evans, P. R. (1990) Active-site mutants altering the cooperativity of E. coli phosphofructokinase, Nature 343, 575-576.
    • (1990) Nature , vol.343 , pp. 575-576
    • Berger, S.A.1    Evans, P.R.2
  • 16
    • 0028200251 scopus 로고
    • The cooperatively and allosteric inhibition of Escherichia coli phosphofructokinase depend on the interaction between threonine-125 and ATP
    • Auzat, I., Le Bras, G. & Garel, J.-R. (1994) The cooperatively and allosteric inhibition of Escherichia coli phosphofructokinase depend on the interaction between threonine-125 and ATP, Proc. Natl Acad. Sci. USA 91, 5242-5246.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 5242-5246
    • Auzat, I.1    Le Bras, G.2    Garel, J.-R.3
  • 17
    • 0029043841 scopus 로고
    • Role of residue 161 in the allosteric transitions of two bacterial phosphofructokinases
    • Auzat, I., Byrnes, W. M., Garel, J.-R. & Chang, S. H. (1995) Role of residue 161 in the allosteric transitions of two bacterial phosphofructokinases, Biochemistry 34, 7062-7068.
    • (1995) Biochemistry , vol.34 , pp. 7062-7068
    • Auzat, I.1    Byrnes, W.M.2    Garel, J.-R.3    Chang, S.H.4
  • 18
    • 0028952327 scopus 로고
    • Role of glycine 212 in the allosteric behavior of phosphofructokinase from Bacillus stearothermophilus
    • Zhu, X., Byrnes, M., Nelson, J. W. & Chang, S. H. (1995) Role of glycine 212 in the allosteric behavior of phosphofructokinase from Bacillus stearothermophilus, Biochemistry 34, 2560-2565.
    • (1995) Biochemistry , vol.34 , pp. 2560-2565
    • Zhu, X.1    Byrnes, M.2    Nelson, J.W.3    Chang, S.H.4
  • 19
    • 0025316446 scopus 로고
    • A new transient activator of phosphofructokinase during initiation of rapid glycolysis in brain
    • Ogushi, S., Lawson, J. W. R., Dobson, G. P., Veech, R. L. & Uyeda, K. (1990) A new transient activator of phosphofructokinase during initiation of rapid glycolysis in brain, J. Biol. Chem. 265, 10 943-10 949.
    • (1990) J. Biol. Chem. , vol.265 , pp. 10943-10949
    • Ogushi, S.1    Lawson, J.W.R.2    Dobson, G.P.3    Veech, R.L.4    Uyeda, K.5
  • 20
    • 0021953958 scopus 로고
    • Modulation of muscle phosphofructokinase at physiological concentration of enzyme
    • Boscá, L., Aragón, J. J. & Sols, A. (1985) Modulation of muscle phosphofructokinase at physiological concentration of enzyme, J. Biol. Chem. 260, 2100-2107.
    • (1985) J. Biol. Chem. , vol.260 , pp. 2100-2107
    • Boscá, L.1    Aragón, J.J.2    Sols, A.3
  • 21
    • 0025889001 scopus 로고
    • Regulation of enzyme activity in the cell: Effect of enzyme concentration
    • Aragón, J. J. & Sols, A. (1991) Regulation of enzyme activity in the cell: effect of enzyme concentration, FASEB J. 5, 2945-2950.
    • (1991) FASEB J. , vol.5 , pp. 2945-2950
    • Aragón, J.J.1    Sols, A.2
  • 22
    • 0023654467 scopus 로고
    • Desensitization of muscle phosphofructokinase to ATP inhibition by removal of a carboxyl-terminal heptadecapeptide
    • Valaitis, A. P., Foe, L. G. & Kemp, R. G. (1987) Desensitization of muscle phosphofructokinase to ATP inhibition by removal of a carboxyl-terminal heptadecapeptide, J. Biol. Chem. 262, 5044-5048.
    • (1987) J. Biol. Chem. , vol.262 , pp. 5044-5048
    • Valaitis, A.P.1    Foe, L.G.2    Kemp, R.G.3
  • 23
    • 0014940723 scopus 로고
    • Studies on heart phosphofructokinase. Nature of the enzyme desensitized to allosteric control by photo-oxidation and by acylation with ethoxyformic anhydride
    • Setlow, B. & Mansour, T. E. (1970) Studies on heart phosphofructokinase. Nature of the enzyme desensitized to allosteric control by photo-oxidation and by acylation with ethoxyformic anhydride, J. Biol. Chem. 245, 5524-5533.
    • (1970) J. Biol. Chem. , vol.245 , pp. 5524-5533
    • Setlow, B.1    Mansour, T.E.2
  • 24
    • 0017097537 scopus 로고
    • Phosphofructokinase. II. Role of ligands in pH-dependent structural changes of the rabbit muscle enzyme
    • Bock, P. E. & Frieden, C. (1976) Phosphofructokinase. II. Role of ligands in pH-dependent structural changes of the rabbit muscle enzyme, J. Biol. Chem. 251, 5637-5643.
    • (1976) J. Biol. Chem. , vol.251 , pp. 5637-5643
    • Bock, P.E.1    Frieden, C.2
  • 25
    • 0023656320 scopus 로고
    • Reaction of Ascaris suum phosphofructokinase with diethylpyrocarbonate. Inactivation and desensitization to allosteric modulation
    • Rao, G. S. J., Wariso, B. A., Cook, P. F., Hofer, H. W. & Harris, B. G. (1987) Reaction of Ascaris suum phosphofructokinase with diethylpyrocarbonate. Inactivation and desensitization to allosteric modulation, J. Biol. Chem. 262, 14 068-14 073.
    • (1987) J. Biol. Chem. , vol.262 , pp. 14068-14073
    • Rao, G.S.J.1    Wariso, B.A.2    Cook, P.F.3    Hofer, H.W.4    Harris, B.G.5
  • 26
    • 0021256418 scopus 로고
    • Evolution of phosphofructokinase: Gene duplication and creation of new effector sites
    • Poorman, R. A., Randolph, A., Kemp, R. G. & Heinrikson, R. L. (1984) Evolution of phosphofructokinase: gene duplication and creation of new effector sites, Nature 309, 467-469.
    • (1984) Nature , vol.309 , pp. 467-469
    • Poorman, R.A.1    Randolph, A.2    Kemp, R.G.3    Heinrikson, R.L.4
  • 27
    • 0027363656 scopus 로고
    • Site-directed mutagenesis of rabbit muscle phosphofructokinase cDNA. Mutations at glutamine 200 affect the allosteric properties of the enzyme
    • Li, J., Zhu, X., Byrnes, M., Nelson, J. W. & Chang, S. H. (1993) Site-directed mutagenesis of rabbit muscle phosphofructokinase cDNA. Mutations at glutamine 200 affect the allosteric properties of the enzyme, J. Biol. Chem. 268, 24 599-24 606.
    • (1993) J. Biol. Chem. , vol.268 , pp. 24599-24606
    • Li, J.1    Zhu, X.2    Byrnes, M.3    Nelson, J.W.4    Chang, S.H.5
  • 28
    • 0028246641 scopus 로고
    • Studies on the function of yeast phosphofructokinase subunits by in vitro mutagenesis
    • Arvanitidis, A. & Heinisch, J. J. (1994) Studies on the function of yeast phosphofructokinase subunits by in vitro mutagenesis, J. Biol. Chem. 269, 8911-8918.
    • (1994) J. Biol. Chem. , vol.269 , pp. 8911-8918
    • Arvanitidis, A.1    Heinisch, J.J.2
  • 29
    • 0002016562 scopus 로고
    • Comparative biology of cellular slime molds
    • Loomis, W. F., ed. Academic Press, New York
    • Bonner, J. T. (1982) Comparative biology of cellular slime molds, in The development of Dictyostelium discoideum (Loomis, W. F., ed.) pp. 1-33, Academic Press, New York.
    • (1982) The Development of Dictyostelium Discoideum , pp. 1-33
    • Bonner, J.T.1
  • 30
    • 0028606474 scopus 로고
    • Purification and properties of phosphofructokinase from Dictyostelium discoideum
    • Martínez-Costa, O. H., Estévez, A. M., Sánchez, V. & Aragón, J. J. (1994) Purification and properties of phosphofructokinase from Dictyostelium discoideum, Eur. J. Biochem. 226, 1007-1017.
    • (1994) Eur. J. Biochem. , vol.226 , pp. 1007-1017
    • Martínez-Costa, O.H.1    Estévez, A.M.2    Sánchez, V.3    Aragón, J.J.4
  • 31
    • 0014841120 scopus 로고
    • Growth of myxamoebae of the cellular slime mold Dictyostelium discoideum in axenic culture
    • Watts, D. J. & Ashworth, J. M. (1970) Growth of myxamoebae of the cellular slime mold Dictyostelium discoideum in axenic culture, Biochem. J. 119, 171-174.
    • (1970) Biochem. J. , vol.119 , pp. 171-174
    • Watts, D.J.1    Ashworth, J.M.2
  • 32
    • 0021943518 scopus 로고
    • Improved M13 phage cloning vectors and host strains: Nucleotide sequences of the M13mp18 and pUC19 vectors
    • Yanisch-Perron, C., Vieira, J. & Messing, J. (1985) Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors, Gene (Amst.) 33, 103-109.
    • (1985) Gene (Amst.) , vol.33 , pp. 103-109
    • Yanisch-Perron, C.1    Vieira, J.2    Messing, J.3
  • 34
    • 0342891330 scopus 로고
    • Immunoscreenig λgt11 recombinant DNA libraries
    • Setlow, J. K. & Hollaender, A., eds Plenum Press, New York
    • Young, R. A. & Davis, R. W. (1985) Immunoscreenig λgt11 recombinant DNA libraries, in Genetic engineering: principles and methods (Setlow, J. K. & Hollaender, A., eds) vol. 7, pp. 29-41, Plenum Press, New York.
    • (1985) Genetic Engineering: Principles and Methods , vol.7 , pp. 29-41
    • Young, R.A.1    Davis, R.W.2
  • 36
    • 0023481280 scopus 로고
    • A ten-minute DNA preparation from yeast efficiently releases autonomous plasmids for transformation of Escherichia coli
    • Hoffman, C. S. & Winston, F. (1987) A ten-minute DNA preparation from yeast efficiently releases autonomous plasmids for transformation of Escherichia coli, Gene (Amst.) 57, 267-272.
    • (1987) Gene (Amst.) , vol.57 , pp. 267-272
    • Hoffman, C.S.1    Winston, F.2
  • 37
    • 8044229463 scopus 로고
    • The isolation of cDNAs in λgt11 using antibody probes
    • Boulnois, G. J., ed. Blackwell Scientific Publications, Boston
    • Jones, P. (1987) The isolation of cDNAs in λgt11 using antibody probes, in Gene cloning and analysis. A laboratory guide (Boulnois, G. J., ed.) pp. 37-43, Blackwell Scientific Publications, Boston.
    • (1987) Gene Cloning and Analysis. A Laboratory Guide , pp. 37-43
    • Jones, P.1
  • 39
    • 0021760092 scopus 로고
    • A comprehensive set of sequence analysis programs for the VAX
    • Devereux, J., Haberli, P. & Smithies, O. (1984) A comprehensive set of sequence analysis programs for the VAX, Nucleic Acids Res. 12, 387-395.
    • (1984) Nucleic Acids Res. , vol.12 , pp. 387-395
    • Devereux, J.1    Haberli, P.2    Smithies, O.3
  • 40
    • 0025342577 scopus 로고
    • Unified approach to alignment and phylogenies
    • Hein, J. (1990) Unified approach to alignment and phylogenies, Methods Enzymol. 183, 626-645.
    • (1990) Methods Enzymol. , vol.183 , pp. 626-645
    • Hein, J.1
  • 41
    • 0024234855 scopus 로고
    • CLUSTAL: A package for performing multiple sequence alignment on a microcomputer
    • Higgins, D. G. & Sharp, P. M. (1988) CLUSTAL: a package for performing multiple sequence alignment on a microcomputer, Gene (Amst.) 73, 237-244.
    • (1988) Gene (Amst.) , vol.73 , pp. 237-244
    • Higgins, D.G.1    Sharp, P.M.2
  • 42
    • 0000122573 scopus 로고
    • PHYLIP. Phylogeny inference package (version 3.2)
    • Felsenstein, J. (1989) PHYLIP. Phylogeny inference package (version 3.2), Cladistics 5, 164-166.
    • (1989) Cladistics , vol.5 , pp. 164-166
    • Felsenstein, J.1
  • 43
    • 0024152983 scopus 로고
    • Phylogenies from molecular sequences: Inference and reliability
    • Felsenstein, J. (1988) Phylogenies from molecular sequences: inference and reliability, Annu. Rev. Genet. 22, 521-565.
    • (1988) Annu. Rev. Genet. , vol.22 , pp. 521-565
    • Felsenstein, J.1
  • 44
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantitation 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
  • 45
    • 0002266688 scopus 로고
    • The organization and expression of the Dictyostelium genome
    • Loomis, W. F., ed. Academic Press, New York
    • Kimmel, A. R. & Firtel, R. A. (1982) The organization and expression of the Dictyostelium genome, in The development of Dictyostelium discoideum (Loomis, W. F., ed.) pp. 233-324, Academic Press, New York.
    • (1982) The Development of Dictyostelium Discoideum , pp. 233-324
    • Kimmel, A.R.1    Firtel, R.A.2
  • 46
    • 0019321115 scopus 로고
    • Optimal spatial requirements for the location of basic residues in peptide substrates for the cyclic AMP-dependent protein kinase
    • Faremisco, J. R., Glass, D. B. & Krebs, E. G. (1980) Optimal spatial requirements for the location of basic residues in peptide substrates for the cyclic AMP-dependent protein kinase, J. Biol. Chem. 255, 4240-4245.
    • (1980) J. Biol. Chem. , vol.255 , pp. 4240-4245
    • Faremisco, J.R.1    Glass, D.B.2    Krebs, E.G.3
  • 47
    • 0024967181 scopus 로고
    • Codon usage and gene expression level in Dictyostelium discoideum: Highly expressed genes do prefer optimal codons
    • Sharp, P. M. & Devine, K. M. (1989) Codon usage and gene expression level in Dictyostelium discoideum: highly expressed genes do prefer optimal codons, Nucleic Acids Res. 17, 5029-5039.
    • (1989) Nucleic Acids Res. , vol.17 , pp. 5029-5039
    • Sharp, P.M.1    Devine, K.M.2
  • 48
    • 0025318864 scopus 로고
    • The effective number of codons used in a gene
    • Wright, F. (1990) The effective number of codons used in a gene, Gene (Amst.) 87, 23-29.
    • (1990) Gene (Amst.) , vol.87 , pp. 23-29
    • Wright, F.1
  • 50
    • 0025828793 scopus 로고
    • Nucleotide sequence of the Rhodobacter capsulatus fruK gene, which encodes fructose-1-phosphate kinase: Evidence for a kinase superfamily including both phosphofructokinases of Escherichia coli
    • Wu, L.-F., Reizer, A., Reizer, J., Cai, B., Tomich, J. M. & Saier, M. H. Jr (1991) Nucleotide sequence of the Rhodobacter capsulatus fruK gene, which encodes fructose-1-phosphate kinase: evidence for a kinase superfamily including both phosphofructokinases of Escherichia coli, J. Bacteriol. 173, 3117-3127.
    • (1991) J. Bacteriol. , vol.173 , pp. 3117-3127
    • Wu, L.-F.1    Reizer, A.2    Reizer, J.3    Cai, B.4    Tomich, J.M.5    Saier Jr., M.H.6
  • 52
    • 0025606351 scopus 로고
    • Molecular phylogeny of Dictyostelium discoideum by protein sequence comparison
    • Loomis, W. F. & Smith, D. W. (1990) Molecular phylogeny of Dictyostelium discoideum by protein sequence comparison, Proc. Natl Acad. Sci. USA 87, 9093-9097.
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 9093-9097
    • Loomis, W.F.1    Smith, D.W.2
  • 53
    • 0028793189 scopus 로고
    • Functional complementation of yeast phosphofructokinase mutants by the non-allosteric enzyme from Dictyostelium discoideum
    • Estévez, A. M., Heinisch, J. J. & Aragón, J. J. (1995) Functional complementation of yeast phosphofructokinase mutants by the non-allosteric enzyme from Dictyostelium discoideum, FEBS Lett. 374, 100-104.
    • (1995) FEBS Lett. , vol.374 , pp. 100-104
    • Estévez, A.M.1    Heinisch, J.J.2    Aragón, J.J.3
  • 54
    • 0015694843 scopus 로고
    • Two fructose 6-phosphate kinase activities in Escherichia coli
    • Fraenkel, D. G., Kotlarz, D. & Buc, H. (1973) Two fructose 6-phosphate kinase activities in Escherichia coli, J. Biol. Chem. 248, 4865-4866.
    • (1973) J. Biol. Chem. , vol.248 , pp. 4865-4866
    • Fraenkel, D.G.1    Kotlarz, D.2    Buc, H.3
  • 55
    • 0017759685 scopus 로고
    • Physicochemical parameters and subunit composition of yeast phosphofructokinase
    • Kopperschläger, G., Bär, J., Nissler, K. & Hoffman, E. (1977) Physicochemical parameters and subunit composition of yeast phosphofructokinase, Eur. J. Biochem. 81, 317-325.
    • (1977) Eur. J. Biochem. , vol.81 , pp. 317-325
    • Kopperschläger, G.1    Bär, J.2    Nissler, K.3    Hoffman, E.4
  • 56
    • 0023157057 scopus 로고
    • Nature of the subunits of the 6-phosphofructo-1-kinase isoenzymes from rat tissues
    • Dunaway, G. A. & Kasten, T. P. (1987) Nature of the subunits of the 6-phosphofructo-1-kinase isoenzymes from rat tissues, Biochem. J. 242, 667-671.
    • (1987) Biochem. J. , vol.242 , pp. 667-671
    • Dunaway, G.A.1    Kasten, T.P.2
  • 57
    • 0002285939 scopus 로고
    • Activity and allosteric regulation in bacterial phosphofructokinase
    • Evans, P. R. (1992) Activity and allosteric regulation in bacterial phosphofructokinase, Proc. Robert A. Welch Found. Conf. 36, 39-54.
    • (1992) Proc. Robert A. Welch Found. Conf. , vol.36 , pp. 39-54
    • Evans, P.R.1
  • 58
    • 0030037752 scopus 로고    scopus 로고
    • A yeast phosphofructokinase insensitive to the allosteric activator fructose 2,6-bisphosphate. Glycolysis/metabolic regulation/allosteric control
    • Heinisch, J. J., Boles, E. & Timpel, C. (1996) A yeast phosphofructokinase insensitive to the allosteric activator fructose 2,6-bisphosphate. Glycolysis/metabolic regulation/allosteric control, J. Biol. Chem. 271, 15 928-15 933.
    • (1996) J. Biol. Chem. , vol.271 , pp. 15928-15933
    • Heinisch, J.J.1    Boles, E.2    Timpel, C.3
  • 59
    • 0025734579 scopus 로고
    • Fructose-2,6-bisphosphate and AMP increase the affinity of the Ascaris suum phosphofructokinase for fructose 6-phosphate in a process separate from the relief of ATP inhibition
    • Payne, M. A., Rao, G. S. J., Harris, B. G. & Cook, P. F. (1991) Fructose-2,6-bisphosphate and AMP increase the affinity of the Ascaris suum phosphofructokinase for fructose 6-phosphate in a process separate from the relief of ATP inhibition, J. Biol. Chem. 266, 8891-8896.
    • (1991) J. Biol. Chem. , vol.266 , pp. 8891-8896
    • Payne, M.A.1    Rao, G.S.J.2    Harris, B.G.3    Cook, P.F.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.