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Volumn 135, Issue 2, 2003, Pages 197-218

Pyruvate kinase: Current status of regulatory and functional properties

Author keywords

Allosteric regulation; Glycolytic pathway; Phylogenetic tree; Pyruvate kinase; Structure function analysis

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; BACTERIAL ENZYME; CATION; FUNGAL ENZYME; GLYCOLYTIC ENZYME; MAGNESIUM ION; MANGANESE; PHOSPHOENOLPYRUVATE; POTASSIUM ION; PYRUVATE KINASE;

EID: 0038241711     PISSN: 10964959     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1096-4959(03)00081-2     Document Type: Review
Times cited : (165)

References (136)
  • 1
    • 0001381881 scopus 로고    scopus 로고
    • Refined three-dimensional structure of cat-muscle (M1) pyruvate kinase at a resolution of 2.6 Å
    • Allen S.C., Muirhead H. Refined three-dimensional structure of cat-muscle (M1) pyruvate kinase at a resolution of 2.6 Å Acta Cryst. D52:1996;499-504.
    • (1996) Acta Cryst. , vol.D52 , pp. 499-504
    • Allen, S.C.1    Muirhead, H.2
  • 2
    • 0025923075 scopus 로고
    • Molecular cloning and analysis of two tandemly linked genes for pyruvate kinase of Trypanosoma brucei
    • Allert S., Ernest I., Poliszcak A., Opperdoes F.R., Michels P.AM. Molecular cloning and analysis of two tandemly linked genes for pyruvate kinase of Trypanosoma brucei. Eur. J. Biochem. 200:1991;19-27.
    • (1991) Eur. J. Biochem. , vol.200 , pp. 19-27
    • Allert, S.1    Ernest, I.2    Poliszcak, A.3    Opperdoes, F.R.4    Michels, P.AM.5
  • 4
    • 0026503387 scopus 로고
    • Transcriptional stimulation by thyroid hormone of a cytosolic thyroid hormone binding protein which is homologous to a subunit of pyruvate kinase M1
    • Ashizawa K., Fukuda T., Sheue-yann P. Transcriptional stimulation by thyroid hormone of a cytosolic thyroid hormone binding protein which is homologous to a subunit of pyruvate kinase M1. Biochemistry. 31:1992;2774-2778.
    • (1992) Biochemistry , vol.31 , pp. 2774-2778
    • Ashizawa, K.1    Fukuda, T.2    Sheue-yann, P.3
  • 5
    • 0027221646 scopus 로고
    • Analysis of pyruvate kinase-deficiency mutations that produce nonspherocytic hemolytic anemia
    • Barociani L., Beutler E. Analysis of pyruvate kinase-deficiency mutations that produce nonspherocytic hemolytic anemia. Proc. Natl. Acad. Sci. USA. 90:1993;4324-4327.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 4324-4327
    • Barociani, L.1    Beutler, E.2
  • 6
    • 0014513032 scopus 로고
    • Factors affecting the activity of pyruvate kinase of Acetobacter xylinum
    • Benziman M. Factors affecting the activity of pyruvate kinase of Acetobacter xylinum. Biochem. J. 112:1969;631-636.
    • (1969) Biochem. J , vol.112 , pp. 631-636
    • Benziman, M.1
  • 7
  • 9
    • 0025508719 scopus 로고
    • Cloning and characterization of a cDNA for the cytosolic isozyme of plant pyruvate kinase: The relationship between the plant and non-plant enzyme
    • Blakeley S.D., Plaxton W.C., Dennis D.T. Cloning and characterization of a cDNA for the cytosolic isozyme of plant pyruvate kinase: the relationship between the plant and non-plant enzyme. Plant Mol. Biol. 15:1990;665-669.
    • (1990) Plant Mol. Biol. , vol.15 , pp. 665-669
    • Blakeley, S.D.1    Plaxton, W.C.2    Dennis, D.T.3
  • 10
    • 0008685665 scopus 로고
    • Relationship between the subunits of leucoplast pyruvate kinase from Ricinus communis and a comparison with the enzyme from other sources
    • Blakeley S.D., Plaxton W.C., Dennis D.T. Relationship between the subunits of leucoplast pyruvate kinase from Ricinus communis and a comparison with the enzyme from other sources. Plant Physiol. 96:1991;1283-1288.
    • (1991) Plant Physiol. , vol.96 , pp. 1283-1288
    • Blakeley, S.D.1    Plaxton, W.C.2    Dennis, D.T.3
  • 11
    • 0029108039 scopus 로고
    • Molecular characterization of plastid pyruvate kinase from castor and tobacco
    • Blakeley S., Gottlob-McHugh S., Wan J., Crews L., Miki B. Molecular characterization of plastid pyruvate kinase from castor and tobacco. Plant Mol. Biol. 27:1995;79-89.
    • (1995) Plant Mol. Biol. , vol.27 , pp. 79-89
    • Blakeley, S.1    Gottlob-McHugh, S.2    Wan, J.3    Crews, L.4    Miki, B.5
  • 12
    • 0030971548 scopus 로고    scopus 로고
    • Characterization of a glucose-repressed pyruvate kinase (Pyk2p) in Saccharomyces cerevisiae that is catalytically insensitive to fructose-1,6-bisphosphate
    • Boles E., Schulte F., Miosga T., Freidel K., Schlüter E., Zimmermann F.K., et al. Characterization of a glucose-repressed pyruvate kinase (Pyk2p) in Saccharomyces cerevisiae that is catalytically insensitive to fructose-1,6-bisphosphate. J. Bacteriol. 179:1997;2987-2993.
    • (1997) J. Bacteriol. , vol.179 , pp. 2987-2993
    • Boles, E.1    Schulte, F.2    Miosga, T.3    Freidel, K.4    Schlüter, E.5    Zimmermann, F.K.6
  • 13
    • 0030873139 scopus 로고    scopus 로고
    • Mck1, a member of the glycogen synthase kinase 3 family of protein kinases, is a negative regulator of pyruvate kinase in the yeast Saccharomyces cerevisiae
    • Brazill D.T., Thorner J., Martin G.S. Mck1, a member of the glycogen synthase kinase 3 family of protein kinases, is a negative regulator of pyruvate kinase in the yeast Saccharomyces cerevisiae. J. Bacteriol. 179:1997;4415-4418.
    • (1997) J. Bacteriol. , vol.179 , pp. 4415-4418
    • Brazill, D.T.1    Thorner, J.2    Martin, G.S.3
  • 14
    • 0025130389 scopus 로고
    • A cGMP stimulated protein kinase phosphorylates pyruvate kinase in an anoxia tolerant marine mollusk
    • Brooks S.P., Storey K.B. A cGMP stimulated protein kinase phosphorylates pyruvate kinase in an anoxia tolerant marine mollusk. J. Comp. Physiol. B. 160:1990;309-316.
    • (1990) J. Comp. Physiol. B , vol.160 , pp. 309-316
    • Brooks, S.P.1    Storey, K.B.2
  • 15
    • 0031439608 scopus 로고    scopus 로고
    • Time course of enzyme changes after a switch from high-fat to lower-fat diet
    • Brooks S.P.J., Lampi B.J. Time course of enzyme changes after a switch from high-fat to lower-fat diet. Comp. Biochem. Physiol. 118B:1997;359-365.
    • (1997) Comp. Biochem. Physiol. , vol.118 , pp. 359-365
    • Brooks, S.P.J.1    Lampi, B.J.2
  • 16
    • 0028500931 scopus 로고
    • Metabolic depression in land snails: In vitro analysis of protein kinase involvement in pyruvate kinase controlling isolated Otala lacteal tissues
    • Brooks S.P., Storey K.B. Metabolic depression in land snails: in vitro analysis of protein kinase involvement in pyruvate kinase controlling isolated Otala lacteal tissues. J. Exp. Zool. 269:1994;507-514.
    • (1994) J. Exp. Zool. , vol.269 , pp. 507-514
    • Brooks, S.P.1    Storey, K.B.2
  • 17
    • 0020580026 scopus 로고
    • The isolation, characterization, and sequence of the pyruvate kinase gene of Saccharomyces cerevisiae
    • Burke R.L., Tekamp-Olson P., Najarian R. The isolation, characterization, and sequence of the pyruvate kinase gene of Saccharomyces cerevisiae. J. Biol. Chem. 258:1983;2193-2201.
    • (1983) J. Biol. Chem. , vol.258 , pp. 2193-2201
    • Burke, R.L.1    Tekamp-Olson, P.2    Najarian, R.3
  • 18
    • 0032732076 scopus 로고    scopus 로고
    • Growth factors stimulate the activity of key glycolytic enzymes in isolated digestive gland cells from mussels (Mytilus galloprovincialis Lam.) through tyrosine kinase mediated signal transudation
    • Canesi L., Ciacci C., Betti M., Malatesta M., Gazzanelli G., Gallo G. Growth factors stimulate the activity of key glycolytic enzymes in isolated digestive gland cells from mussels (Mytilus galloprovincialis Lam.) through tyrosine kinase mediated signal transudation. Gen. Comp. Endocrinol. 116:1999;241-248.
    • (1999) Gen. Comp. Endocrinol. , vol.116 , pp. 241-248
    • Canesi, L.1    Ciacci, C.2    Betti, M.3    Malatesta, M.4    Gazzanelli, G.5    Gallo, G.6
  • 19
    • 0033118209 scopus 로고    scopus 로고
    • Glucose repression in yeast
    • Carlson M. Glucose repression in yeast. Curr. Opin. Microbiol. 2:1999;202-207.
    • (1999) Curr. Opin. Microbiol. , vol.2 , pp. 202-207
    • Carlson, M.1
  • 20
    • 0026733875 scopus 로고
    • Archaeobacteria: Biochemistry and biotechnology
    • M.S. Dauson, D.H. Hough, & G.G. Lunt.
    • Cowan D.O. Archaeobacteria: biochemistry and biotechnology. Dauson M.S., Hough D.H., Lunt G.G. Biochemistry Society Symposium no. 58. 1992;149-168.
    • (1992) Biochemistry Society Symposium no. 58 , pp. 149-168
    • Cowan, D.O.1
  • 21
    • 0032974921 scopus 로고    scopus 로고
    • Reversible phosphorylation control of skeletal muscle pyruvate kinase and phosphofructokinase during estivation in the spadefoot toad, Scaphiopus couchii
    • Cowan K.J., Storey K.B. Reversible phosphorylation control of skeletal muscle pyruvate kinase and phosphofructokinase during estivation in the spadefoot toad, Scaphiopus couchii. Mol. Cell Biochem. 195:1999;173-181.
    • (1999) Mol. Cell Biochem. , vol.195 , pp. 173-181
    • Cowan, K.J.1    Storey, K.B.2
  • 22
    • 0017294301 scopus 로고
    • Oxaloacetate decarboxylase activity in muscle is due to pyruvate kinase
    • Creighton D.J., Rose I.A. Oxaloacetate decarboxylase activity in muscle is due to pyruvate kinase. J. Biol. Chem. 251:1976;69-72.
    • (1976) J. Biol. Chem. , vol.251 , pp. 69-72
    • Creighton, D.J.1    Rose, I.A.2
  • 24
    • 0034646796 scopus 로고    scopus 로고
    • Pyruvate kinase from the thermophilic eubacterium Bacillus acidocaldarius as the probe to monitor the sodium concentrations in the blood
    • D'Auria S., Rossi M., Herman P., Lakowicz J.R. Pyruvate kinase from the thermophilic eubacterium Bacillus acidocaldarius as the probe to monitor the sodium concentrations in the blood. Biophys. Chem. 84:2000;167-176.
    • (2000) Biophys. Chem. , vol.84 , pp. 167-176
    • D'Auria, S.1    Rossi, M.2    Herman, P.3    Lakowicz, J.R.4
  • 25
    • 0033215210 scopus 로고    scopus 로고
    • Pathway alignment: Application to the comparative analysis of glycolytic enzymes
    • Dandekar T., Schuster M.S., Snel B., Huynen M., Bork P. Pathway alignment: application to the comparative analysis of glycolytic enzymes. Biochem. J. 343:1999;115-124.
    • (1999) Biochem. J. , vol.343 , pp. 115-124
    • Dandekar, T.1    Schuster, M.S.2    Snel, B.3    Huynen, M.4    Bork, P.5
  • 26
    • 0032528420 scopus 로고    scopus 로고
    • Six previously undescribed pyruvate kinase mutations causing enzyme deficiency
    • Demina A., Varughese K.I., Barbot J., Forman L., Beutler E. Six previously undescribed pyruvate kinase mutations causing enzyme deficiency. Blood. 92:1999;647-652.
    • (1999) Blood , vol.92 , pp. 647-652
    • Demina, A.1    Varughese, K.I.2    Barbot, J.3    Forman, L.4    Beutler, E.5
  • 27
    • 0030883032 scopus 로고    scopus 로고
    • Regulated nuclear translocation of the Mig1 glucose repressor
    • De Vit M.J., Waddle J.A., Johnson M. Regulated nuclear translocation of the Mig1 glucose repressor. Mol. Biol. Cell. 8:1997;1603-1618.
    • (1997) Mol. Biol. Cell. , vol.8 , pp. 1603-1618
    • De Vit, M.J.1    Waddle, J.A.2    Johnson, M.3
  • 28
    • 0034984865 scopus 로고    scopus 로고
    • Trangenic Arabidopsis plants with decreased activity of fructose-6-phosphate, 2-kinase/fructose-2, 6-bisphosphatase have altered carbon partitioning
    • Draborg H., Villadsen D., Nielsen T.H. Trangenic Arabidopsis plants with decreased activity of fructose-6-phosphate, 2-kinase/fructose-2, 6-bisphosphatase have altered carbon partitioning. Plant. Physiol. 126:2001;750-758.
    • (2001) Plant. Physiol. , vol.126 , pp. 750-758
    • Draborg, H.1    Villadsen, D.2    Nielsen, T.H.3
  • 29
    • 0031763886 scopus 로고    scopus 로고
    • Pyruvate kinase and the interaction of amino acid and carbohydrate metabolism in solid tumors
    • Eigenbrodt E., Kallinowski F., Ott M., Mazurek S., Vaupel P. Pyruvate kinase and the interaction of amino acid and carbohydrate metabolism in solid tumors. Anticancer Res. 18:1998;3267-3274.
    • (1998) Anticancer Res. , vol.18 , pp. 3267-3274
    • Eigenbrodt, E.1    Kallinowski, F.2    Ott, M.3    Mazurek, S.4    Vaupel, P.5
  • 30
    • 0033107827 scopus 로고    scopus 로고
    • Glucose catabolism of Escherichia coli strains with increased activity and altered regulation of key glycolytic enzymes
    • Emmerling M., Baley J.E., Sauer U. Glucose catabolism of Escherichia coli strains with increased activity and altered regulation of key glycolytic enzymes. Metab. Eng. 1:1999;117-127.
    • (1999) Metab. Eng. , vol.1 , pp. 117-127
    • Emmerling, M.1    Baley, J.E.2    Sauer, U.3
  • 31
    • 0028200842 scopus 로고
    • Cloning and sequence analysis of the gene encoding pyruvate kinase in Trypanosoma borelli
    • Ernest I., Opperdoes F.R., Michels P.A.M. Cloning and sequence analysis of the gene encoding pyruvate kinase in Trypanosoma borelli. Biochem. Biophys. Res. Com. 201:1994;727-732.
    • (1994) Biochem. Biophys. Res. Com. , vol.201 , pp. 727-732
    • Ernest, I.1    Opperdoes, F.R.2    Michels, P.A.M.3
  • 32
    • 0015935610 scopus 로고
    • Magnetic resonance and catalytic studies of pyruvate kinase with essential sulfhydryl or lysyl epsilon-amino groups chemically modified
    • Flashner M., Tamir J., Mildvan A.S., Meloche H.P., Coon M.J. Magnetic resonance and catalytic studies of pyruvate kinase with essential sulfhydryl or lysyl epsilon-amino groups chemically modified. J. Biol. Chem. 248:1973;3419-3425.
    • (1973) J. Biol. Chem. , vol.248 , pp. 3419-3425
    • Flashner, M.1    Tamir, J.2    Mildvan, A.S.3    Meloche, H.P.4    Coon, M.J.5
  • 34
    • 0033983045 scopus 로고    scopus 로고
    • Leishmania pyruvate kinase: The crystal structure reveals the structural basis of its unique regulatory properties
    • Fothergill-Gilmore L.A., Rigden D.J., Michels P.A.M., Phillips S.E.V. Leishmania pyruvate kinase: the crystal structure reveals the structural basis of its unique regulatory properties. Biochem. Soc. Trans. 28:2000;186-190.
    • (2000) Biochem. Soc. Trans. , vol.28 , pp. 186-190
    • Fothergill-Gilmore, L.A.1    Rigden, D.J.2    Michels, P.A.M.3    Phillips, S.E.V.4
  • 35
    • 0023133802 scopus 로고
    • Purification and kinetic properties of pyruvate kinase isoenzymes of Salmonella typhimurium
    • Garcia-Olalla C., Garrido-Pertierra A. Purification and kinetic properties of pyruvate kinase isoenzymes of Salmonella typhimurium. Biochem. J. 241:1987;573-581.
    • (1987) Biochem. J. , vol.241 , pp. 573-581
    • Garcia-Olalla, C.1    Garrido-Pertierra, A.2
  • 36
    • 0028985644 scopus 로고
    • Cloning, sequencing and characterization of the alkaline phosphatase gene (phoD) from Zymomonas mobilis
    • Gomez P.F., Ingram L.O. Cloning, sequencing and characterization of the alkaline phosphatase gene (phoD) from Zymomonas mobilis. FEMS Microbiol. Lett. 125:1995;237-246.
    • (1995) FEMS Microbiol. Lett. , vol.125 , pp. 237-246
    • Gomez, P.F.1    Ingram, L.O.2
  • 37
    • 0017129688 scopus 로고
    • Dual divalent cation requirement for activation of pyruvate kinase: Essential roles of both enzyme- and nucleotide-bound metal ions
    • Gupta R.K., Oesterling M., Mildvan A.S. Dual divalent cation requirement for activation of pyruvate kinase: essential roles of both enzyme- and nucleotide-bound metal ions. Biochemistry. 15:1976;2881-2887.
    • (1976) Biochemistry , vol.15 , pp. 2881-2887
    • Gupta, R.K.1    Oesterling, M.2    Mildvan, A.S.3
  • 38
    • 0018224094 scopus 로고
    • Isozymes of pyruvate kinase in vertebrates: Their physical, chemical and immunological properties
    • Hall E.R., Cottam G.L. Isozymes of pyruvate kinase in vertebrates: their physical, chemical and immunological properties. Int. J. Biochem. 9:1978;785-793.
    • (1978) Int. J. Biochem. , vol.9 , pp. 785-793
    • Hall, E.R.1    Cottam, G.L.2
  • 39
    • 0026832754 scopus 로고
    • Acetic acid formation in Escherichia coli fermentation
    • Han, K., Lim, H.C, Hong, J., 1992. Acetic acid formation in Escherichia coli fermentation. Biotech. Bioeng. 39, 663-671.
    • (1992) Biotech. Bioeng. , vol.39 , pp. 663-671
    • Han, K.1    Lim H.C2    Hong, J.3
  • 40
    • 0031717105 scopus 로고    scopus 로고
    • The AMP-activated/SNF1 protein kinase subfamily: Metabolic sensors of the eukaryotic cell?
    • Hardie D.G., Carling D., Carlson M. The AMP-activated/SNF1 protein kinase subfamily: metabolic sensors of the eukaryotic cell? Annu. Rev. Biochem. 67:1998;821-855.
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 821-855
    • Hardie, D.G.1    Carling, D.2    Carlson, M.3
  • 41
    • 0033560109 scopus 로고    scopus 로고
    • AMP-activated protein kinase: An ultrasensitive system for monitoring cellular energy charge
    • Hardie D.G., Salt I.P., Hawley S.A., Davies S.P. AMP-activated protein kinase: an ultrasensitive system for monitoring cellular energy charge. Biochem. J. 338:1999;717-722.
    • (1999) Biochem. J. , vol.338 , pp. 717-722
    • Hardie, D.G.1    Salt, I.P.2    Hawley, S.A.3    Davies, S.P.4
  • 43
    • 0037154102 scopus 로고    scopus 로고
    • Pyruvate site of pyruvate phosphate dikinase: Crystal structure of the enzyme-phosphoenolpyruvate complex, and mutant analysis
    • Herzberg O., Chen C.C., Liu S., Tempczyk A., Howard A., Wei M., et al. Pyruvate site of pyruvate phosphate dikinase: crystal structure of the enzyme-phosphoenolpyruvate complex, and mutant analysis. Biochemistry. 41:2002;780-787.
    • (2002) Biochemistry , vol.41 , pp. 780-787
    • Herzberg, O.1    Chen, C.C.2    Liu, S.3    Tempczyk, A.4    Howard, A.5    Wei, M.6
  • 44
    • 0015239124 scopus 로고
    • Role of lysyl epsilon-amino groups in adenosine diphosphate binding and catalytic activity of pyruvate kinase
    • Hollenberg P.F., Flashner M., Coon M.J. Role of lysyl epsilon-amino groups in adenosine diphosphate binding and catalytic activity of pyruvate kinase. J. Biol. Chem. 246:1971;946-953.
    • (1971) J. Biol. Chem. , vol.246 , pp. 946-953
    • Hollenberg, P.F.1    Flashner, M.2    Coon, M.J.3
  • 45
    • 0030248716 scopus 로고    scopus 로고
    • Purification and characterization of cytosolic pyruvate kinase from leaves of the castor oil plant
    • Hu Z.H., Plaxton W.C. Purification and characterization of cytosolic pyruvate kinase from leaves of the castor oil plant. Arch. Biochem. Biophys. 333:1996;298-307.
    • (1996) Arch. Biochem. Biophys. , vol.333 , pp. 298-307
    • Hu, Z.H.1    Plaxton, W.C.2
  • 46
    • 0030795097 scopus 로고    scopus 로고
    • Conversion of non-allosteric pyruvate kinase isozyme into an allosteric enzyme by a single amino acid substitution
    • Ikeda Y., Tanaka T., Noguchi T. Conversion of non-allosteric pyruvate kinase isozyme into an allosteric enzyme by a single amino acid substitution. J. Biol. Chem. 272:1997;20495-20501.
    • (1997) J. Biol. Chem. , vol.272 , pp. 20495-20501
    • Ikeda, Y.1    Tanaka, T.2    Noguchi, T.3
  • 48
    • 0014690622 scopus 로고
    • Some original characteristics of latex pyruvate kinase from Hevea brasiliensis
    • Jacob J.L., D'Auzac J. Some original characteristics of latex pyruvate kinase from Hevea brasiliensis. Bull. Chem. Biol. 51:1969;511-525.
    • (1969) Bull. Chem. Biol. , vol.51 , pp. 511-525
    • Jacob, J.L.1    D'Auzac, J.2
  • 49
    • 0028229433 scopus 로고
    • Structural and functional analysis of pyruvate kinase from Corynebacterium glutamicum
    • Jetten M.S.M., Gubler M.E., Sang H.L., Sinskey A.J. Structural and functional analysis of pyruvate kinase from Corynebacterium glutamicum. Appl. Environ. Microbiol. 60:1994;2501-2507.
    • (1994) Appl. Environ. Microbiol. , vol.60 , pp. 2501-2507
    • Jetten, M.S.M.1    Gubler, M.E.2    Sang, H.L.3    Sinskey, A.J.4
  • 50
    • 0018802751 scopus 로고
    • Isolation and sequence determination of a peptide located in or near the active site of bovine muscle pyruvate kinase
    • Johnson S.C., Bailey T., Becker R.R., Cardenas J.M. Isolation and sequence determination of a peptide located in or near the active site of bovine muscle pyruvate kinase. Biochem. Biophys. Res. Comm. 90:1979;525-530.
    • (1979) Biochem. Biophys. Res. Comm. , vol.90 , pp. 525-530
    • Johnson, S.C.1    Bailey, T.2    Becker, R.R.3    Cardenas, J.M.4
  • 52
    • 0030841937 scopus 로고    scopus 로고
    • Transcriptional regulation by glucose in the liver
    • Kahn A. Transcriptional regulation by glucose in the liver. Biochimie. 79:1997;113-118.
    • (1997) Biochimie , vol.79 , pp. 113-118
    • Kahn, A.1
  • 53
    • 0030606607 scopus 로고    scopus 로고
    • Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions
    • Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., et al. Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions. DNA Res. 3:1996;109-136.
    • (1996) DNA Res. , vol.3 , pp. 109-136
    • Kaneko, T.1    Sato, S.2    Kotani, H.3    Tanaka, A.4    Asamizu, E.5    Nakamura, Y.6
  • 54
    • 0020805830 scopus 로고
    • Purification and properties of pyruvate kinase from Mycobacterium smegmatis
    • Kapoor R., Venkitasubramanian T.A. Purification and properties of pyruvate kinase from Mycobacterium smegmatis. Arch. Biochem. Biophys. 225:1983;320-330.
    • (1983) Arch. Biochem. Biophys. , vol.225 , pp. 320-330
    • Kapoor, R.1    Venkitasubramanian, T.A.2
  • 55
    • 0035923516 scopus 로고    scopus 로고
    • Glucose and cAMP regulate the L-type pyruvate kinase gene by phosphorylation/dephosphorylation of the carbohydrate response element binding protein
    • Kawaguchi T., Takenoshita M., Kabashima T., Uyeda K. Glucose and cAMP regulate the L-type pyruvate kinase gene by phosphorylation/dephosphorylation of the carbohydrate response element binding protein. Proc. Natl. Acad. Sci. USA. 98:2001;13710-13715.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 13710-13715
    • Kawaguchi, T.1    Takenoshita, M.2    Kabashima, T.3    Uyeda, K.4
  • 56
    • 0037040185 scopus 로고    scopus 로고
    • Mechanism for fatty acid 'sparing' effect on glucose-induced transcription: Regulation of carbohydrate-responsive element-binding protein by AMP-activated protein kinase
    • Kawaguchi T., Osatomi K., Yamashita H., Kabashima T., Uyeda K. Mechanism for fatty acid 'sparing' effect on glucose-induced transcription: regulation of carbohydrate-responsive element-binding protein by AMP-activated protein kinase. J. Biol. Chem. 277:2002;3829-3835.
    • (2002) J. Biol. Chem. , vol.277 , pp. 3829-3835
    • Kawaguchi, T.1    Osatomi, K.2    Yamashita, H.3    Kabashima, T.4    Uyeda, K.5
  • 57
    • 77956902867 scopus 로고
    • Pyruvate kinase
    • Boyer P.D.
    • Kayne F.J. Pyruvate kinase. Boyer P.D. The Enzymes. VIII:1973;353-382.
    • (1973) The Enzymes , vol.8 , pp. 353-382
    • Kayne, F.J.1
  • 58
    • 0030760294 scopus 로고    scopus 로고
    • Upstream stimulatory factor-2 (USF2) activity is required for glucose stimulation of L-pyruvate kinase promoter activity in single living islet beta-cells
    • Kennedy H.J., Viollet B., Rafiq I., Kahn A., Rutter G.A. Upstream stimulatory factor-2 (USF2) activity is required for glucose stimulation of L-pyruvate kinase promoter activity in single living islet beta-cells. J. Biol. Chem. 272:1997;20636-20640.
    • (1997) J. Biol. Chem. , vol.272 , pp. 20636-20640
    • Kennedy, H.J.1    Viollet, B.2    Rafiq, I.3    Kahn, A.4    Rutter, G.A.5
  • 59
    • 0028052113 scopus 로고    scopus 로고
    • Kleman, G.L., Strohl, W.R., 1994. Acetate metabolism by Escherichia coli in high-cell density fermentation. Appl. Environ. Microbiol. 60, 3952-3958
    • Kleman, G.L., Strohl, W.R., 1994. Acetate metabolism by Escherichia coli in high-cell density fermentation. Appl. Environ. Microbiol. 60, 3952-3958.
  • 60
    • 0024820260 scopus 로고
    • Purification of a novel pyruvate kinase from a green alga
    • Knowles V.L., Dennis D.T., Plaxton W.C. Purification of a novel pyruvate kinase from a green alga. FEB. 259:1989;130-132.
    • (1989) FEB , vol.259 , pp. 130-132
    • Knowles, V.L.1    Dennis, D.T.2    Plaxton, W.C.3
  • 61
    • 0035877824 scopus 로고    scopus 로고
    • Knowles, V.L., Smith, C.S., Smith, C.R., Plaxton, W.C., 2001. Structural and regulatory properties of pyruvate kinase from the cyanobacterium Synechococcus PCC 6301. J. Biol. Chem. 276, 20966-20972
    • Knowles, V.L., Smith, C.S., Smith, C.R., Plaxton, W.C., 2001. Structural and regulatory properties of pyruvate kinase from the cyanobacterium Synechococcus PCC 6301. J. Biol. Chem. 276, 20966-20972.
  • 62
    • 0002842808 scopus 로고
    • Gluconeogenesis in the castor bean endosperm. I Changes in glycolytic intermediates
    • Kobr J., Beevers H. Gluconeogenesis in the castor bean endosperm. I Changes in glycolytic intermediates. Plant Physiol. 47:1971;48-52.
    • (1971) Plant Physiol. , vol.47 , pp. 48-52
    • Kobr, J.1    Beevers, H.2
  • 63
    • 0034681335 scopus 로고    scopus 로고
    • Glucose regulation of mouse S14 gene expression in hepatocytes. Involvement of a novel transcription factor complex
    • Koo S.H., Towle H.C. Glucose regulation of mouse S14 gene expression in hepatocytes. Involvement of a novel transcription factor complex. J. Biol. Chem. 275:2000;5200-5207.
    • (2000) J. Biol. Chem. , vol.275 , pp. 5200-5207
    • Koo, S.H.1    Towle, H.C.2
  • 65
    • 0031574153 scopus 로고    scopus 로고
    • The monovalent cation requirement of rabbit muscle pyruvate kinase is eliminated by substitution of lysine for glutamate 117
    • Laughlin L.T., Reed G.R. The monovalent cation requirement of rabbit muscle pyruvate kinase is eliminated by substitution of lysine for glutamate 117. Arch. Biochem. Biophys. 348:1997;262-267.
    • (1997) Arch. Biochem. Biophys. , vol.348 , pp. 262-267
    • Laughlin, L.T.1    Reed, G.R.2
  • 66
    • 0015040563 scopus 로고
    • Regulation at the PEP branchpoint in Azotobacter vinelandii: Pyruvate kinase
    • Liao C.L., Atkinson D.E. Regulation at the PEP branchpoint in Azotobacter vinelandii: pyruvate kinase. J. Bacteriol. 106:1971;37-44.
    • (1971) J. Bacteriol. , vol.106 , pp. 37-44
    • Liao, C.L.1    Atkinson, D.E.2
  • 67
    • 0024969479 scopus 로고
    • Pyruvate kinase isozymes from the green alga, Selenastrum minutum. I. Purification and physical and immunological characterization
    • Lin M., Turpin D.H., Plaxton W.C. Pyruvate kinase isozymes from the green alga, Selenastrum minutum. I. Purification and physical and immunological characterization. Arch. Biochem. Biophys. 269:1989;219-227.
    • (1989) Arch. Biochem. Biophys. , vol.269 , pp. 219-227
    • Lin, M.1    Turpin, D.H.2    Plaxton, W.C.3
  • 68
    • 0024969730 scopus 로고
    • Pyruvate kinase isozymes from the green alga, Selenastrum minutum. II. Kinetic and regulatory properties
    • Lin M., Turpin D.H., Plaxton W.C. Pyruvate kinase isozymes from the green alga, Selenastrum minutum. II. Kinetic and regulatory properties. Arch. Biochem. Biophys. 269:1989;228-238.
    • (1989) Arch. Biochem. Biophys. , vol.269 , pp. 228-238
    • Lin, M.1    Turpin, D.H.2    Plaxton, W.C.3
  • 69
    • 0022525913 scopus 로고
    • Complete nucleotide and derived amino acid sequences of rat L-type pyruvate kinase
    • Lone Y.C., Simon M.P., Khan A., Marie J. Complete nucleotide and derived amino acid sequences of rat L-type pyruvate kinase. FEBS Lett. 195:1986;97-100.
    • (1986) FEBS Lett. , vol.195 , pp. 97-100
    • Lone, Y.C.1    Simon, M.P.2    Khan, A.3    Marie, J.4
  • 70
    • 0020440318 scopus 로고
    • AMP- and fructose 1,6-bisphosphate-activated pyruvate kinase from Escherichia coli
    • Malcovati M., Valentini G. AMP- and fructose 1,6-bisphosphate-activated pyruvate kinase from Escherichia coli. Methods Enzymol. 90:1982;170-179.
    • (1982) Methods Enzymol. , vol.90 , pp. 170-179
    • Malcovati, M.1    Valentini, G.2
  • 71
    • 0027436399 scopus 로고
    • The pyruvate kinase gene as a model for studies of glucose-dependent regulation of gene expression in the endocrine pancreatic beta-cell type
    • Marie S., Díaz-Guerra M.J., Miquerol L., Kahn A., Iynedjian P.B. The pyruvate kinase gene as a model for studies of glucose-dependent regulation of gene expression in the endocrine pancreatic beta-cell type. J. Biol. Chem. 268:1993;23881-23890.
    • (1993) J. Biol. Chem. , vol.268 , pp. 23881-23890
    • Marie, S.1    Díaz-Guerra, M.J.2    Miquerol, L.3    Kahn, A.4    Iynedjian, P.B.5
  • 72
    • 0034869665 scopus 로고    scopus 로고
    • Isolation and characterization of four genes encoding pyruvate, phosphate dikinase in the oomycete plant pathogen Phytophthora cinnamomi
    • Marshall J., Ashton A.R., Govers F., Hardham A.R. Isolation and characterization of four genes encoding pyruvate, phosphate dikinase in the oomycete plant pathogen Phytophthora cinnamomi. Curr. Genet. 40:2001;73-81.
    • (2001) Curr. Genet. , vol.40 , pp. 73-81
    • Marshall, J.1    Ashton, A.R.2    Govers, F.3    Hardham, A.R.4
  • 73
    • 0029645125 scopus 로고
    • Crystal structure of Escherichia coli pyruvate kinase type I: Molecular basis of the allosteric transition
    • Mattevi A., Valentini G., Rizzi M., Speranza M.L., Bolognesi M., Coda A. Crystal structure of Escherichia coli pyruvate kinase type I: molecular basis of the allosteric transition. Structure. 3:1995;729-741.
    • (1995) Structure , vol.3 , pp. 729-741
    • Mattevi, A.1    Valentini, G.2    Rizzi, M.3    Speranza, M.L.4    Bolognesi, M.5    Coda, A.6
  • 74
    • 0030600132 scopus 로고    scopus 로고
    • The allosteric regulation of pyruvate kinase
    • Mattevi A., Bolognesi M., Valentini G. The allosteric regulation of pyruvate kinase. FEBS Lett. 389:1996;15-19.
    • (1996) FEBS Lett. , vol.389 , pp. 15-19
    • Mattevi, A.1    Bolognesi, M.2    Valentini, G.3
  • 75
    • 0030969449 scopus 로고    scopus 로고
    • Metal-ion-mediated allosteric triggering of yeast pyruvate kinase. 1. A multidimensional thermodynamic linked-unction analysis
    • Mesecar A.D., Nowak T. Metal-ion-mediated allosteric triggering of yeast pyruvate kinase. 1. A multidimensional thermodynamic linked-unction analysis. Biochemistry. 36:1997;6792-6802.
    • (1997) Biochemistry , vol.36 , pp. 6792-6802
    • Mesecar, A.D.1    Nowak, T.2
  • 76
    • 0030966962 scopus 로고    scopus 로고
    • Metal-ion-mediated allosteric triggering of yeast pyruvate kinase. 2. A multidimensional thermodynamic linked-unction analysis
    • Mesecar A.D., Nowak T. Metal-ion-mediated allosteric triggering of yeast pyruvate kinase. 2. A multidimensional thermodynamic linked-unction analysis. Biochemistry. 36:1997;6803-6813.
    • (1997) Biochemistry , vol.36 , pp. 6803-6813
    • Mesecar, A.D.1    Nowak, T.2
  • 77
    • 0032520197 scopus 로고    scopus 로고
    • The allosteric regulation of pyruvate kinase by fructose-1,6-bisphosphate
    • Mesecar J.M.S., Heath P.J., Nowak T., Stoddard B.L. The allosteric regulation of pyruvate kinase by fructose-1,6-bisphosphate. Structure. 6:1998;195-210.
    • (1998) Structure , vol.6 , pp. 195-210
    • Mesecar, J.M.S.1    Heath, P.J.2    Nowak, T.3    Stoddard, B.L.4
  • 79
    • 0344075899 scopus 로고    scopus 로고
    • Molecular cloning of the gene that codes for the pyruvate kinase of Bacillus subtilis, primary characterization of a strain carrying this gene insertionally inactivated
    • Muñoz M-E., Le Borgne S., Bolívar F., Valle F. Molecular cloning of the gene that codes for the pyruvate kinase of Bacillus subtilis, primary characterization of a strain carrying this gene insertionally inactivated. Microbiology. 39:1997;129-140.
    • (1997) Microbiology , vol.39 , pp. 129-140
    • Muñoz, M-E.1    Le Borgne, S.2    Bolívar, F.3    Valle, F.4
  • 80
    • 0028804016 scopus 로고
    • Cloning and sequencing of a gene encoding pyruvate kinase from Schizosaccharomyces pombe: Implications for quaternary structure and regulation of the enzyme
    • Nairn J., Smith S., Allison P.J., Rigden D., Fothergill-Gilmore L.A., Price N. Cloning and sequencing of a gene encoding pyruvate kinase from Schizosaccharomyces pombe: implications for quaternary structure and regulation of the enzyme. FEMS Microbiol. Lett. 134:1995;221-226.
    • (1995) FEMS Microbiol. Lett. , vol.134 , pp. 221-226
    • Nairn, J.1    Smith, S.2    Allison, P.J.3    Rigden, D.4    Fothergill-Gilmore, L.A.5    Price, N.6
  • 81
    • 0029177638 scopus 로고
    • Suborganellar localization and molecular characterization of nonproteolytic degraded leucoplast pyruvate kinase from developing castor oil seeds
    • Negm F.B., Cornel F.A., Plaxton W.C. Suborganellar localization and molecular characterization of nonproteolytic degraded leucoplast pyruvate kinase from developing castor oil seeds. Plant Physiol. 109:1995;1461-1469.
    • (1995) Plant Physiol. , vol.109 , pp. 1461-1469
    • Negm, F.B.1    Cornel, F.A.2    Plaxton, W.C.3
  • 82
    • 0028886180 scopus 로고
    • Phylogenetic analysis of the putative phosphorylation domain in the pyruvate kinase of Bacillus stearothermophilus
    • Nguyen C.C., Saier M.H. Jr. Phylogenetic analysis of the putative phosphorylation domain in the pyruvate kinase of Bacillus stearothermophilus. Res. Microbiol. 146:1995;713-719.
    • (1995) Res. Microbiol. , vol.146 , pp. 713-719
    • Nguyen, C.C.1    Saier M.H., Jr.2
  • 83
    • 0022930036 scopus 로고
    • The M1- and M2-type isozymes of rat pyruvate kinase are produced from the same gene by alternative RNA splicing
    • Noguchi T., Inoue H., Tanaka T. The M1- and M2-type isozymes of rat pyruvate kinase are produced from the same gene by alternative RNA splicing. J. Biol. Chem. 261:1986;13807-13812.
    • (1986) J. Biol. Chem. , vol.261 , pp. 13807-13812
    • Noguchi, T.1    Inoue, H.2    Tanaka, T.3
  • 84
    • 12944257426 scopus 로고    scopus 로고
    • Polytrauma induces increased expression of pyruvate kinase in neutrophils
    • Oehler R., Weingartmann G., Manhart N., Saizer U., Meissner M., Schlegel W., et al. Polytrauma induces increased expression of pyruvate kinase in neutrophils. Blood. 95:2000;1086-1092.
    • (2000) Blood , vol.95 , pp. 1086-1092
    • Oehler, R.1    Weingartmann, G.2    Manhart, N.3    Saizer, U.4    Meissner, M.5    Schlegel, W.6
  • 85
    • 0032780468 scopus 로고    scopus 로고
    • The pyruvate kinase isoenzyme tumor M2 (Tu M2-PK) as a tumor marker for renal carcinoma
    • Oremek G.M., Teigelkamp S., Kramer W., Eigenbrodt E., Usadel K.H. The pyruvate kinase isoenzyme tumor M2 (Tu M2-PK) as a tumor marker for renal carcinoma. Anticancer Res. 19:1999;2599-2601.
    • (1999) Anticancer Res. , vol.19 , pp. 2599-2601
    • Oremek, G.M.1    Teigelkamp, S.2    Kramer, W.3    Eigenbrodt, E.4    Usadel, K.H.5
  • 86
    • 0014576813 scopus 로고
    • Regulation of the TCA and glyoxylate cycles in Brevibacterium flavum. II. Regulation of PEP carboxylase and pyruvate kinase
    • Ozaki H., Shiio I. Regulation of the TCA and glyoxylate cycles in Brevibacterium flavum. II. Regulation of PEP carboxylase and pyruvate kinase. J. Biochem. 66:1969;297-311.
    • (1969) J. Biochem. , vol.66 , pp. 297-311
    • Ozaki, H.1    Shiio, I.2
  • 87
    • 0028243762 scopus 로고
    • Involvement of liver and skeletal muscle in sucrose-induced insulin resistance: Dose-response studies
    • Pagliassotti M.J., Shahrokhi K.A., Moscarello M. Involvement of liver and skeletal muscle in sucrose-induced insulin resistance: dose-response studies. Am. J. Physiol. 266:1994;R1637-R1644.
    • (1994) Am. J. Physiol. , vol.266
    • Pagliassotti, M.J.1    Shahrokhi, K.A.2    Moscarello, M.3
  • 88
    • 0023050194 scopus 로고
    • Isolation and properties of the glycolytic enzymes from Zymomonas mobilis
    • Pawluk A., Scopes R.K., Griffiths-Smith K. Isolation and properties of the glycolytic enzymes from Zymomonas mobilis. Biochem. J. 238:1986;275-281.
    • (1986) Biochem. J. , vol.238 , pp. 275-281
    • Pawluk, A.1    Scopes, R.K.2    Griffiths-Smith, K.3
  • 89
    • 0024669157 scopus 로고
    • Molecular and immunological characterization of plastid and cytosolic pyruvate kinase isozymes from castor-oil-plant endosperm and leaf
    • Plaxton W.C. Molecular and immunological characterization of plastid and cytosolic pyruvate kinase isozymes from castor-oil-plant endosperm and leaf. Eur. J. Biochem. 181:1989;443-451.
    • (1989) Eur. J. Biochem. , vol.181 , pp. 443-451
    • Plaxton, W.C.1
  • 90
    • 0000666466 scopus 로고
    • Purification of leucoplast pyruvate kinase from developing castor bean endosperm
    • Plaxton W.C., Dennis D.T., Knowles V.L. Purification of leucoplast pyruvate kinase from developing castor bean endosperm. Plant Physiol. 94:1990;1528-1534.
    • (1990) Plant Physiol. , vol.94 , pp. 1528-1534
    • Plaxton, W.C.1    Dennis, D.T.2    Knowles, V.L.3
  • 91
    • 0001252798 scopus 로고
    • Leucoplast pyruvate kinase from developing castor seeds. Characterization of the enzyme's degradation by cysteine endopeptidase
    • Plaxton W.C. Leucoplast pyruvate kinase from developing castor seeds. Characterization of the enzyme's degradation by cysteine endopeptidase. Plant Physiol. 97:1991;1334-1338.
    • (1991) Plant Physiol. , vol.97 , pp. 1334-1338
    • Plaxton, W.C.1
  • 93
    • 0036544591 scopus 로고    scopus 로고
    • Molecular and regulatory properties of leucoplast pyruvate kinase from Brassica napus (rapeseed) suspension cells
    • Plaxton W.C., Smith C.R., Knowles V.L. Molecular and regulatory properties of leucoplast pyruvate kinase from Brassica napus (rapeseed) suspension cells. Arch. Biochem. Biophys. 400:2002;54-62.
    • (2002) Arch. Biochem. Biophys. , vol.400 , pp. 54-62
    • Plaxton, W.C.1    Smith, C.R.2    Knowles, V.L.3
  • 94
    • 0025606663 scopus 로고
    • Analysis of sequence homologies in plant and bacterial pyruvate phosphate dikinase, enzyme I of bacterial PEP: Sugar phosphotransferase system and other PEP-utilizing enzymes. Identification of potential catalytic and regulatory motifs
    • Pocalyko D.J., Carrol L.J., Martin B.M., Babbitt C., Dunaway-Mariano D. Analysis of sequence homologies in plant and bacterial pyruvate phosphate dikinase, enzyme I of bacterial PEP: sugar phosphotransferase system and other PEP-utilizing enzymes. Identification of potential catalytic and regulatory motifs. Biochemistry. 29:1990;10757-10765.
    • (1990) Biochemistry , vol.29 , pp. 10757-10765
    • Pocalyko, D.J.1    Carrol, L.J.2    Martin, B.M.3    Babbitt, C.4    Dunaway-Mariano, D.5
  • 95
    • 0026459657 scopus 로고
    • Plant cytosolic pyruvate kinase: A kinetic study
    • Podestá F.E., Plaxton W.C. Plant cytosolic pyruvate kinase: a kinetic study. Biochim. Biophys. Acta. 1160:1992;213-220.
    • (1992) Biochim. Biophys. Acta , vol.1160 , pp. 213-220
    • Podestá, F.E.1    Plaxton, W.C.2
  • 96
    • 0027974775 scopus 로고
    • Regulation of cytosolic carbon metabolism in germination Ricinus communis cotyledons. II. Properties of phosphoenolpyruvate carboxylase and cytosolic pyruvate kinase associated with the regulation of glycolysis and nitrogen assimilation
    • Podestá F.E., Plaxton W.C. Regulation of cytosolic carbon metabolism in germination Ricinus communis cotyledons. II. Properties of phosphoenolpyruvate carboxylase and cytosolic pyruvate kinase associated with the regulation of glycolysis and nitrogen assimilation. Planta. 194:1994;381-387.
    • (1994) Planta , vol.194 , pp. 381-387
    • Podestá, F.E.1    Plaxton, W.C.2
  • 97
    • 0029610838 scopus 로고
    • Cloning of the two pyruvate kinase isoenzymes structural genes from Escherichia coli: The relative roles of these enzymes in pyruvate biosynthesis
    • Ponce E., Flores N., Martínez A., Valle F., Bolívar F. Cloning of the two pyruvate kinase isoenzymes structural genes from Escherichia coli: the relative roles of these enzymes in pyruvate biosynthesis. J. Bacteriol. 177:1995;5719-5722.
    • (1995) J. Bacteriol. , vol.177 , pp. 5719-5722
    • Ponce, E.1    Flores, N.2    Martínez, A.3    Valle, F.4    Bolívar, F.5
  • 98
    • 2642704983 scopus 로고    scopus 로고
    • Stimulation of glucose catabolism through the pentose pathway by the absence of the two pyruvate kinase isoenzymes in Escherichia coli
    • Ponce E., Martinez A., Bolivar F., Valle F. Stimulation of glucose catabolism through the pentose pathway by the absence of the two pyruvate kinase isoenzymes in Escherichia coli. Biotechnol. Bioeng. 58:1998;292-295.
    • (1998) Biotechnol. Bioeng. , vol.58 , pp. 292-295
    • Ponce, E.1    Martinez, A.2    Bolivar, F.3    Valle, F.4
  • 99
    • 85031176186 scopus 로고    scopus 로고
    • Postma, P.W., Lengeler, J.W., Jacobson, G.R., 1996. Phosphoenolpyruvate: carbohydrate phophotransferase systems. In: Neidhardt, F.C. (Ed.), Escherichia coli and Salmonella Cellular and Molecular Biology, vol. 1. American Society for Microbiology. ASM Press, Washington, pp. 1149-1174
    • Postma, P.W., Lengeler, J.W., Jacobson, G.R., 1996. Phosphoenolpyruvate: carbohydrate phophotransferase systems. In: Neidhardt, F.C. (Ed.), Escherichia coli and Salmonella Cellular and Molecular Biology, vol. 1. American Society for Microbiology. ASM Press, Washington, pp. 1149-1174.
  • 100
    • 0026570202 scopus 로고
    • The pyruvate kinase of Thermoplasma acidophilum: Purification, kinetic characterization and use as a phylogenetic marker
    • Potter S., Fothergill-Gilmore L.A. The pyruvate kinase of Thermoplasma acidophilum: purification, kinetic characterization and use as a phylogenetic marker. Bioch. Soc. Trans. 20:1991;11S.
    • (1991) Bioch. Soc. Trans. , vol.20
    • Potter, S.1    Fothergill-Gilmore, L.A.2
  • 101
    • 0027076558 scopus 로고
    • Combinatorial crosstalk of transacting factors biding to the L-type pyruvate kinase promoter elements analyzed in vitro
    • Puzenat N., Vaulont S., Kahn A., Raymondjean M.J. Combinatorial crosstalk of transacting factors biding to the L-type pyruvate kinase promoter elements analyzed in vitro. Biochem. Biophys. Res. Commun. 189:1992;1119-1128.
    • (1992) Biochem. Biophys. Res. Commun. , vol.189 , pp. 1119-1128
    • Puzenat, N.1    Vaulont, S.2    Kahn, A.3    Raymondjean, M.J.4
  • 102
    • 0028948211 scopus 로고
    • Characterization of redox proteins from extreme thermophilic Archaebacteria: Studies on alcohol dehydrogenase and thioredoxins
    • Raia C.A., D'Auria S., Guagliardi A., Bartolucci S., De Rosa M., Rossi M. Characterization of redox proteins from extreme thermophilic Archaebacteria: studies on alcohol dehydrogenase and thioredoxins. Biosensors Bioelectron. 10:1995;135-140.
    • (1995) Biosensors Bioelectron. , vol.10 , pp. 135-140
    • Raia, C.A.1    D'Auria, S.2    Guagliardi, A.3    Bartolucci, S.4    De Rosa, M.5    Rossi, M.6
  • 103
    • 0037053342 scopus 로고    scopus 로고
    • Direct and novel regulation of camp-dependent protein kinase by Mck1p, a yeast glycogen synthase kinase-3
    • Rayner T.F., Gray J.V., Thorner J.W. Direct and novel regulation of camp-dependent protein kinase by Mck1p, a yeast glycogen synthase kinase-3. J. Biol. Chem. 277:2002;16814-16822.
    • (2002) J. Biol. Chem. , vol.277 , pp. 16814-16822
    • Rayner, T.F.1    Gray, J.V.2    Thorner, J.W.3
  • 104
    • 0033588341 scopus 로고    scopus 로고
    • The structure of pyruvate kinase from Leishmania mexicana reveals details of the allosteric transition and unusual effector specificity
    • Rigden D.J., Phillips D.J., Michels P.A., Fothergill-Gilmore L.A. The structure of pyruvate kinase from Leishmania mexicana reveals details of the allosteric transition and unusual effector specificity. J. Mol. Biol. 291:1999;615-635.
    • (1999) J. Mol. Biol. , vol.291 , pp. 615-635
    • Rigden, D.J.1    Phillips, D.J.2    Michels, P.A.3    Fothergill-Gilmore, L.A.4
  • 105
    • 0031888152 scopus 로고    scopus 로고
    • Expression and characterization of recombinant pyruvate phosphate dikinase from Entamoeba histolytica
    • Saavedra-Lira E., Ramírez-Silva L., Pérez-Montfort R. Expression and characterization of recombinant pyruvate phosphate dikinase from Entamoeba histolytica. Biochim. Biophys. Acta. 1382:1998;47-54.
    • (1998) Biochim. Biophys. Acta , vol.1382 , pp. 47-54
    • Saavedra-Lira, E.1    Ramírez-Silva, L.2    Pérez-Montfort, R.3
  • 106
    • 0016304189 scopus 로고
    • Pyruvate kinase of Escherichia coli. Its role in supplying nucleoside triphosphates in cells under anaerobic conditions
    • Saeki T., Hori M., Umezawa H. Pyruvate kinase of Escherichia coli. Its role in supplying nucleoside triphosphates in cells under anaerobic conditions. J. Biochem. 76:1974;631-637.
    • (1974) J. Biochem. , vol.76 , pp. 631-637
    • Saeki, T.1    Hori, M.2    Umezawa, H.3
  • 107
    • 0028104094 scopus 로고
    • The bacterial phosphotransferase system: New frontiers 30 years later
    • Saier M.H. Jr., Raizer J. The bacterial phosphotransferase system: new frontiers 30 years later. Mol. Microbiol. 13:1994;755-764.
    • (1994) Mol. Microbiol. , vol.13 , pp. 755-764
    • Saier M.H., Jr.1    Raizer, J.2
  • 108
    • 0023375195 scopus 로고
    • The neighbor-joining method: A new method for reconstructing phylogenetic trees
    • Saitou N., Nei M. The neighbor-joining method: a new method for reconstructing phylogenetic trees. Mol. Biol. Evol. 4:1987;406-425.
    • (1987) Mol. Biol. Evol. , vol.4 , pp. 406-425
    • Saitou, N.1    Nei, M.2
  • 109
    • 0022612227 scopus 로고
    • Purification and properties of pyruvate kinase from Bacillus stearothermophilus
    • Sakai H., Suzuki K., Imahori K. Purification and properties of pyruvate kinase from Bacillus stearothermophilus. J. Biochem. 99:1986;1157-1167.
    • (1986) J. Biochem. , vol.99 , pp. 1157-1167
    • Sakai, H.1    Suzuki, K.2    Imahori, K.3
  • 110
    • 0027418071 scopus 로고
    • Molecular cloning and nucleotide sequence of the gene for pyruvate kinase of Bacillus stearothermophilus and the production of the enzyme in Escherichia coli
    • Sakai H., Ohta T. Molecular cloning and nucleotide sequence of the gene for pyruvate kinase of Bacillus stearothermophilus and the production of the enzyme in Escherichia coli. Eur. J. Biochem. 211:1993;851-859.
    • (1993) Eur. J. Biochem. , vol.211 , pp. 851-859
    • Sakai, H.1    Ohta, T.2
  • 111
    • 0034020750 scopus 로고    scopus 로고
    • Pyruvate kinase of the hyperthermophilic crenarchaeote Thermoproteus tenax: Physiological role and phylogenetic aspects
    • Schramm A., Siebers B., Tjaden B., Brinkmann H., Hensel R. Pyruvate kinase of the hyperthermophilic crenarchaeote Thermoproteus tenax: physiological role and phylogenetic aspects. J. Bacteriol. 182:2000;2001-2009.
    • (2000) J. Bacteriol. , vol.182 , pp. 2001-2009
    • Schramm, A.1    Siebers, B.2    Tjaden, B.3    Brinkmann, H.4    Hensel, R.5
  • 112
    • 0032768263 scopus 로고    scopus 로고
    • The SNF1 kinase complex from Saccharomyces cerevisiae phosphorylates the transcriptional repressor protein Mig1p in vitro at four sites within or near regulatory domain 1
    • Smith F.C., Davies S.P., Wilson W.A., Carling D., Hardie D.G. The SNF1 kinase complex from Saccharomyces cerevisiae phosphorylates the transcriptional repressor protein Mig1p in vitro at four sites within or near regulatory domain 1. FEBS Lett. 453:1999;219-223.
    • (1999) FEBS Lett. , vol.453 , pp. 219-223
    • Smith, F.C.1    Davies, S.P.2    Wilson, W.A.3    Carling, D.4    Hardie, D.G.5
  • 113
    • 0033942009 scopus 로고    scopus 로고
    • Purification and characterization of cytosolic pyruvate kinase from Brassica napus (rapeseed) suspension cells cultures
    • Smith C.R., Knowles V.L., Plaxton W.C. Purification and characterization of cytosolic pyruvate kinase from Brassica napus (rapeseed) suspension cells cultures. Eur. J. Biochem. 267:2000;4477-4485.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 4477-4485
    • Smith, C.R.1    Knowles, V.L.2    Plaxton, W.C.3
  • 114
    • 0024635967 scopus 로고
    • Primary structure of three peptides at the catalytic and allosteric sites of the fructose-1,6-bisphosphate-activated pyruvate kinase from Escherichia coli
    • Speranza M.L., Valentini G., Iadarola P., Stoppini M., Malcovati M., Ferri G. Primary structure of three peptides at the catalytic and allosteric sites of the fructose-1,6-bisphosphate-activated pyruvate kinase from Escherichia coli. Biol. Chem. Hoppe Seiler. 370:1989;211-216.
    • (1989) Biol. Chem. Hoppe Seiler , vol.370 , pp. 211-216
    • Speranza, M.L.1    Valentini, G.2    Iadarola, P.3    Stoppini, M.4    Malcovati, M.5    Ferri, G.6
  • 115
    • 0016789840 scopus 로고
    • Three dimensional structure of cat muscle pyruvate kinase at 6 Å resolution
    • Stammers D.K., Muirhead H. Three dimensional structure of cat muscle pyruvate kinase at 6 Å resolution. J. Mol. Biol. 95:1975;213-225.
    • (1975) J. Mol. Biol. , vol.95 , pp. 213-225
    • Stammers, D.K.1    Muirhead, H.2
  • 117
    • 0018792428 scopus 로고
    • Crystal structure of cat muscle pyruvate kinase at a resolution of 2.6 Å
    • Stuart D.I., Levine M., Muirhead H., Stammers D.K. Crystal structure of cat muscle pyruvate kinase at a resolution of 2.6 Å J. Mol. Biol. 134:1979;109-142.
    • (1979) J. Mol. Biol. , vol.134 , pp. 109-142
    • Stuart, D.I.1    Levine, M.2    Muirhead, H.3    Stammers, D.K.4
  • 118
    • 0029934166 scopus 로고    scopus 로고
    • Nucleoside diphosphate kinase from Pseudomonas aerations: Characterization of the gene and its role in cellular growth and exopolysaccharide alginate synthesis
    • Sundin G.W., Shankar K., Chugani S.A., Chopade B.A., Black A.K., Chakrabarty A.M. Nucleoside diphosphate kinase from Pseudomonas aerations: characterization of the gene and its role in cellular growth and exopolysaccharide alginate synthesis. Mol. Microbiol. 20:1996;965-979.
    • (1996) Mol. Microbiol. , vol.20 , pp. 965-979
    • Sundin, G.W.1    Shankar, K.2    Chugani, S.A.3    Chopade, B.A.4    Black, A.K.5    Chakrabarty, A.M.6
  • 119
    • 0029346887 scopus 로고
    • Molecular cloning of the genes for pyruvate kinase of the two bacilli, Bacillus psychrophilus and Bacillus licheniformis, and comparison of the properties of the enzymes produced in Escherichia coli
    • Tanaka K., Sakai H., Ohta T., Matsuzawa H. Molecular cloning of the genes for pyruvate kinase of the two bacilli, Bacillus psychrophilus and Bacillus licheniformis, and comparison of the properties of the enzymes produced in Escherichia coli. Biosci. Biotech. Biochem. 59:1995;1536-1542.
    • (1995) Biosci. Biotech. Biochem. , vol.59 , pp. 1536-1542
    • Tanaka, K.1    Sakai, H.2    Ohta, T.3    Matsuzawa, H.4
  • 120
    • 0024121596 scopus 로고
    • Human liver type pyruvate kinase: Complete amino acid sequence and expression in mammalian cells
    • Tani K., Fujii H., Nagata S., Miwa S. Human liver type pyruvate kinase: complete amino acid sequence and expression in mammalian cells. Proc. Natl. Acad. Sci. USA. 85:1988;1792-1795.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 1792-1795
    • Tani, K.1    Fujii, H.2    Nagata, S.3    Miwa, S.4
  • 123
    • 0030484738 scopus 로고    scopus 로고
    • Basic and applied aspects of metabolic diversity: The PEP node
    • Valle F., Ponce E., Flores N., Bolívar F. Basic and applied aspects of metabolic diversity: the PEP node. J. Ind. Microbiol. 17:1996;458-462.
    • (1996) J. Ind. Microbiol. , vol.17 , pp. 458-462
    • Valle, F.1    Ponce, E.2    Flores, N.3    Bolívar, F.4
  • 124
    • 0028509254 scopus 로고
    • TREECON for Windows: A software package for the construction and drawing of evolutionary trees for the Microsoft Windows environment
    • Van de Peer Y., De Wachter R. TREECON for Windows: a software package for the construction and drawing of evolutionary trees for the Microsoft Windows environment. Comput. Appl. Biosci. 10:1994;569-570.
    • (1994) Comput. Appl. Biosci , vol.10 , pp. 569-570
    • Van de Peer, Y.1    De Wachter, R.2
  • 125
    • 0022373073 scopus 로고
    • Stimulation of Trypanosoma brucei pyruvate kinase by fructose 2,6-bisphosphate
    • Van Schaftingen E., Opperdoes F.R., Hers H.G. Stimulation of Trypanosoma brucei pyruvate kinase by fructose 2,6-bisphosphate. Eur. J. Biochem. 153:1985;403-406.
    • (1985) Eur. J. Biochem. , vol.153 , pp. 403-406
    • Van Schaftingen, E.1    Opperdoes, F.R.2    Hers, H.G.3
  • 126
    • 0023019274 scopus 로고
    • Transcriptional and post-transcriptional regulation of L-type pyruvate kinase gene expression in rat liver
    • Vaulont S., Munnich A., Decaux J.F., Kahn A. Transcriptional and post-transcriptional regulation of L-type pyruvate kinase gene expression in rat liver. J. Biol. Chem. 261:1986;7621-7625.
    • (1986) J. Biol. Chem. , vol.261 , pp. 7621-7625
    • Vaulont, S.1    Munnich, A.2    Decaux, J.F.3    Kahn, A.4
  • 127
    • 0024420244 scopus 로고
    • Protein binding to the liver-specific pyruvate kinase gene promoter. A unique combination of known factors
    • Vaulont S., Puzenat N., Kahn A., Raymondjean M.J. Protein binding to the liver-specific pyruvate kinase gene promoter. A unique combination of known factors. Mol. Biol. 209:1989;205-219.
    • (1989) Mol. Biol. , vol.209 , pp. 205-219
    • Vaulont, S.1    Puzenat, N.2    Kahn, A.3    Raymondjean, M.J.4
  • 128
    • 0035503868 scopus 로고    scopus 로고
    • N-terminal truncation affects the kinetics and structure of fructose-6-phosphate 2-kinase/fructose-2,6-bisphosphatase from Arabidopsis thaliana
    • Villadsen D., Nielsen T.H. N-terminal truncation affects the kinetics and structure of fructose-6-phosphate 2-kinase/fructose-2,6-bisphosphatase from Arabidopsis thaliana. Biochem. J. 359:2001;591-597.
    • (2001) Biochem. J , vol.359 , pp. 591-597
    • Villadsen, D.1    Nielsen, T.H.2
  • 129
    • 0026490822 scopus 로고
    • Key residues in the allosteric transition of Bacillus stearothermophilus pyruvate kinase identified by site-directed mutagenesis
    • Walker D., Chia W.N., Muirhead H. Key residues in the allosteric transition of Bacillus stearothermophilus pyruvate kinase identified by site-directed mutagenesis. J. Mol. Biol. 228:1992;265-276.
    • (1992) J. Mol. Biol. , vol.228 , pp. 265-276
    • Walker, D.1    Chia, W.N.2    Muirhead, H.3
  • 130
    • 0015988609 scopus 로고
    • The control of pyruvate kinases of Escherichia coli. I. Physicochemical and regulatory properties of the enzyme activated by fructose 1,6-diphosphate
    • Waygood E.B., Sanwal B.D. The control of pyruvate kinases of Escherichia coli. I. Physicochemical and regulatory properties of the enzyme activated by fructose 1,6-diphosphate. J. Biol. Chem. 249:1974;265-274.
    • (1974) J. Biol. Chem. , vol.249 , pp. 265-274
    • Waygood, E.B.1    Sanwal, B.D.2
  • 131
    • 0016610086 scopus 로고
    • The control of pyruvate kinases of Escherichia coli. II Effectors and regulatory properties of the enzyme activated by ribose 5-phosphate
    • Waygood E.B., Raymanl M.K., Sanwal B.D. The control of pyruvate kinases of Escherichia coli. II Effectors and regulatory properties of the enzyme activated by ribose 5-phosphate. Can. J. Biochem. 53:1975;444-454.
    • (1975) Can. J. Biochem. , vol.53 , pp. 444-454
    • Waygood, E.B.1    Raymanl, M.K.2    Sanwal, B.D.3
  • 132
    • 0017286403 scopus 로고
    • The control of pyruvate kinase of Escherichia coli. Binding of substrate and allosteric effectors to the enzyme activated by fructose 1,6-bisphosphate
    • Waygood E.B., Mort J.S., Sanwal B.D. The control of pyruvate kinase of Escherichia coli. Binding of substrate and allosteric effectors to the enzyme activated by fructose 1,6-bisphosphate. Biochemistry. 15:1976;277-282.
    • (1976) Biochemistry , vol.15 , pp. 277-282
    • Waygood, E.B.1    Mort, J.S.2    Sanwal, B.D.3
  • 133
    • 0032792665 scopus 로고    scopus 로고
    • AMP-activated protein kinase, a metabolic master switch: Possible roles in type 2 diabetes
    • Winder W.W., Hardie D.G. AMP-activated protein kinase, a metabolic master switch: possible roles in type 2 diabetes. Am. J. Physiol. Endocrinol. Methods. 40:1999;E1-E10.
    • (1999) Am. J. Physiol. Endocrinol. Methods , vol.40
    • Winder, W.W.1    Hardie, D.G.2
  • 134
    • 0034636006 scopus 로고    scopus 로고
    • Role of AMP-activated protein kinase in the regulation by glucose of islet beta cell gene expression
    • Xavier G.S., Leclerc I., Salt I.P., Doiron B., Hardie D.G., Kahn A. Role of AMP-activated protein kinase in the regulation by glucose of islet beta cell gene expression. Proc. Natl. Acad. Sci. USA. 97:2000;4023-4028.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 4023-4028
    • Xavier, G.S.1    Leclerc, I.2    Salt, I.P.3    Doiron, B.4    Hardie, D.G.5    Kahn, A.6
  • 135
    • 0032906762 scopus 로고    scopus 로고
    • Nutrient and hormonal regulation of pyruvate kinase gene expression
    • Yamada K., Noguchi T. Nutrient and hormonal regulation of pyruvate kinase gene expression. Biochem. J. 337:1999;1-11.
    • (1999) Biochem. J , vol.337 , pp. 1-11
    • Yamada, K.1    Noguchi, T.2


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