메뉴 건너뛰기




Volumn 375, Issue 2, 2003, Pages 231-246

The unique features of glycolytic pathways in Archaea

Author keywords

Archaea; Embden Meyerhof pathway; Entner Douderoff pathway; Glycolysis; Glycolytic enzyme; Polysaccharide

Indexed keywords

BACTERIA; ENZYMES; GENES; GLUCOSE; METABOLISM;

EID: 0142138858     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20021472     Document Type: Review
Times cited : (200)

References (134)
  • 1
    • 0031058143 scopus 로고    scopus 로고
    • Theoretical approaches to the evolutionary optimization of glycolysis - Chemical analysis
    • Meléndez-Hevia, E., Waddell, T. G., Heinrich, R. and Montero, F. (1997) Theoretical approaches to the evolutionary optimization of glycolysis - chemical analysis. Eur. J. Biochem. 244, 527-543
    • (1997) Eur. J. Biochem. , vol.244 , pp. 527-543
    • Meléndez-Hevia, E.1    Waddell, T.G.2    Heinrich, R.3    Montero, F.4
  • 2
    • 0032464663 scopus 로고    scopus 로고
    • What's for dinner?: Entner-Doudoroff metabolism in Escherichia coli
    • Peekhaus, N. and Conway, T. (1998) What's for dinner?: Entner-Doudoroff metabolism in Escherichia coli. J. Bacteriol. 180, 3495-3502
    • (1998) J. Bacteriol. , vol.180 , pp. 3495-3502
    • Peekhaus, N.1    Conway, T.2
  • 4
    • 0028245448 scopus 로고
    • Evidence for the operation of a novel Embden-Meyerhof pathway that involves ADP-dependent kinases during sugar fermentation by Pyrococcus furiosus
    • Kengen, S. W., de Bok, F. A., van Loo, N. D., Dijkema, C., Stams, A. J. and de Vos, W. M. (1994) Evidence for the operation of a novel Embden-Meyerhof pathway that involves ADP-dependent kinases during sugar fermentation by Pyrococcus furiosus. J. Biol. Chem. 269, 17537-17541
    • (1994) J. Biol. Chem. , vol.269 , pp. 17537-17541
    • Kengen, S.W.1    De Bok, F.A.2    Van Loo, N.D.3    Dijkema, C.4    Stams, A.J.5    De Vos, W.M.6
  • 5
    • 0031002263 scopus 로고    scopus 로고
    • Comparative analysis of Embden-Meyerhof and Entner-Doudoroff glycolytic pathways in hyperthermophilic archaea and the bacterium Thermotoga
    • Selig, M., Xavier, K. B., Santos, H. and Schönheit, P. (1997) Comparative analysis of Embden-Meyerhof and Entner-Doudoroff glycolytic pathways in hyperthermophilic archaea and the bacterium Thermotoga. Arch. Microbiol. 167, 217-232
    • (1997) Arch. Microbiol. , vol.167 , pp. 217-232
    • Selig, M.1    Xavier, K.B.2    Santos, H.3    Schönheit, P.4
  • 6
    • 0027249393 scopus 로고
    • Glucose catabolism of the hyperthermophilic archaeum Thermoproteus tenax
    • Siebers, B. and Hensel, R. (1993) Glucose catabolism of the hyperthermophilic archaeum Thermoproteus tenax. FEMS Microbiol. Lett. 111, 1-8
    • (1993) FEMS Microbiol. Lett. , vol.111 , pp. 1-8
    • Siebers, B.1    Hensel, R.2
  • 7
    • 0026721082 scopus 로고
    • 2 in the anaerobic hyperthermophilic archaeaon Pyrococcus furiosus: Evidence for the operation of a novel sugar fermentation pathway
    • 2 in the anaerobic hyperthermophilic archaeaon Pyrococcus furiosus: evidence for the operation of a novel sugar fermentation pathway. Arch. Microbiol. 158, 188-202
    • (1992) Arch. Microbiol. , vol.158 , pp. 188-202
    • Schäfer, T.1    Schönheit, P.2
  • 8
    • 0029417337 scopus 로고
    • Purification and characterization of a novel ADP-dependent glucokinase from the hyperthermophilic archaeon Pyrococcus furiosus
    • Kengen, S. W., Tuininga, J. E., de Bok, F. A., Stams, A. J. and de Vos, W. M. (1995) Purification and characterization of a novel ADP-dependent glucokinase from the hyperthermophilic archaeon Pyrococcus furiosus. J. Biol. Chem. 270, 30453-30457
    • (1995) J. Biol. Chem. , vol.270 , pp. 30453-30457
    • Kengen, S.W.1    Tuininga, J.E.2    De Bok, F.A.3    Stams, A.J.4    De Vos, W.M.5
  • 9
    • 0033215210 scopus 로고    scopus 로고
    • Pathway alignment: Application to the comparative analysis of glycolytic enzymes
    • Dandekar, T., Schuster, S., Snel, B., Huynen, M. and Bork, P. (1999) Pathway alignment: application to the comparative analysis of glycolytic enzymes. Biochem. J. 343, 115-124
    • (1999) Biochem. J. , vol.343 , pp. 115-124
    • Dandekar, T.1    Schuster, S.2    Snel, B.3    Huynen, M.4    Bork, P.5
  • 10
    • 0142197447 scopus 로고    scopus 로고
    • Distribution and phylogenies of enzymes of the Embden-Meyerhof-Parnas pathway from archaea and hyperthermophilic bacteria support a gluconeogenic origin of metabolism
    • in the press
    • Ronimus, R. S. and Morgan, H. W. (2003) Distribution and phylogenies of enzymes of the Embden-Meyerhof-Parnas pathway from archaea and hyperthermophilic bacteria support a gluconeogenic origin of metabolism. Archaea, in the press
    • (2003) Archaea
    • Ronimus, R.S.1    Morgan, H.W.2
  • 17
    • 0002866714 scopus 로고
    • Pyrococcus furiosus sp. nov. represents a novel genus of marine heterotrophic archaebacteria growing optimally at 100°C
    • Fiala, G. and Stetter, K. O. (1986) Pyrococcus furiosus sp. nov. represents a novel genus of marine heterotrophic archaebacteria growing optimally at 100°C. Arch. Microbiol. 161, 168-175
    • (1986) Arch. Microbiol. , vol.161 , pp. 168-175
    • Fiala, G.1    Stetter, K.O.2
  • 18
    • 0018928663 scopus 로고
    • The Sulfolobus-"Caldariella" group: Taxonomy on the basis of the structure of DNA-dependent RNA polymerases
    • Zillig, W., Stetter, K. O., Wunderl, S., Schulz, W., Priess, H. and Scholz, I. (1980) The Sulfolobus-"Caldariella" group: taxonomy on the basis of the structure of DNA-dependent RNA polymerases. Arch. Microbiol. 125, 259-269
    • (1980) Arch. Microbiol. , vol.125 , pp. 259-269
    • Zillig, W.1    Stetter, K.O.2    Wunderl, S.3    Schulz, W.4    Priess, H.5    Scholz, I.6
  • 19
    • 0027465230 scopus 로고
    • Purification and characterization of an extremely thermostable β-glucosidase from the hyperthermophilic archaeon Pyrococcus furiosus
    • Kengen, S. W., Luesink, E. J., Stams, A. J. and Zehnder, A. J. (1993) Purification and characterization of an extremely thermostable β-glucosidase from the hyperthermophilic archaeon Pyrococcus furiosus. Eur. J. Biochem. 213, 305-312
    • (1993) Eur. J. Biochem. , vol.213 , pp. 305-312
    • Kengen, S.W.1    Luesink, E.J.2    Stams, A.J.3    Zehnder, A.J.4
  • 20
    • 0031437663 scopus 로고    scopus 로고
    • Molecular and biochemical characterization of an endo-β-1,3- glucanase of the hyperthermophilic archaeon Pyrococcus furiosus
    • Gueguen, Y., Voorhorst, W. G., van der Oost, J. and de Vos, W. M. (1997) Molecular and biochemical characterization of an endo-β-1,3-glucanase of the hyperthermophilic archaeon Pyrococcus furiosus. J. Biol. Chem. 272, 31258-31264
    • (1997) J. Biol. Chem. , vol.272 , pp. 31258-31264
    • Gueguen, Y.1    Voorhorst, W.G.2    Van Der Oost, J.3    De Vos, W.M.4
  • 21
    • 0033027296 scopus 로고    scopus 로고
    • Relationship between glycosyl hydrolase inventory and growth physiology of the hyperthermophile Pyrococcus furiosus on carbohydrate-based media
    • Driskill, L. E., Kusy, K., Bauer, M. W. and Kelly, R. M. (1999) Relationship between glycosyl hydrolase inventory and growth physiology of the hyperthermophile Pyrococcus furiosus on carbohydrate-based media. Appl. Environ. Microbiol. 65, 893-897
    • (1999) Appl. Environ. Microbiol. , vol.65 , pp. 893-897
    • Driskill, L.E.1    Kusy, K.2    Bauer, M.W.3    Kelly, R.M.4
  • 22
    • 0024351039 scopus 로고
    • Phenotypic characterization of the archaebacterial genus Sulfolobus: Comparison of five wild-type strains
    • Grogan, D. W. (1989) Phenotypic characterization of the archaebacterial genus Sulfolobus: comparison of five wild-type strains. J. Bacteriol. 171, 6710-6719
    • (1989) J. Bacteriol. , vol.171 , pp. 6710-6719
    • Grogan, D.W.1
  • 23
    • 0035057117 scopus 로고    scopus 로고
    • Sugar transport in Sulfolobus solfataricus is mediated by two families of binding protein-dependent ABC transporters
    • Elferink, M. G., Albers, S. V., Konings, W. N. and Driessen, A. J. (2001) Sugar transport in Sulfolobus solfataricus is mediated by two families of binding protein-dependent ABC transporters. Mol. Microbiol. 39, 1494-1503
    • (2001) Mol. Microbiol. , vol.39 , pp. 1494-1503
    • Elferink, M.G.1    Albers, S.V.2    Konings, W.N.3    Driessen, A.J.4
  • 25
    • 0025061657 scopus 로고
    • Extremely thermostable amylolytic enzyme from the archaebacterium Pyrococcus furiosus
    • Koch, R., Zablowski, P., Spreinat, A. and Antranikian, G. (1990) Extremely thermostable amylolytic enzyme from the archaebacterium Pyrococcus furiosus. FEMS Microbiol. Lett. 71, 21-26
    • (1990) FEMS Microbiol. Lett. , vol.71 , pp. 21-26
    • Koch, R.1    Zablowski, P.2    Spreinat, A.3    Antranikian, G.4
  • 26
    • 0030910823 scopus 로고    scopus 로고
    • Cloning, sequencing, characterization, and expression of an extracellular α-amylase from the hyperthermophilic archaeon Pyrococcus furiosus in Escherichia coli and Bacillus subtilis
    • Jorgensen, S., Vorgias, C. E. and Antranikian, G. (1997) Cloning, sequencing, characterization, and expression of an extracellular α-amylase from the hyperthermophilic archaeon Pyrococcus furiosus in Escherichia coli and Bacillus subtilis. J. Biol. Chem. 272, 16335-16342
    • (1997) J. Biol. Chem. , vol.272 , pp. 16335-16342
    • Jorgensen, S.1    Vorgias, C.E.2    Antranikian, G.3
  • 27
    • 0027179678 scopus 로고
    • Characterization of amylolytic enzymes, having both α-1,4 and α-1,6 hydrolytic activity, from thermophilic archaea Pyrococcus furiosus and Thermococcus litoralis
    • Brown, S. H. and Kelly, R. M. (1993) Characterization of amylolytic enzymes, having both α-1,4 and α-1,6 hydrolytic activity, from thermophilic archaea Pyrococcus furiosus and Thermococcus litoralis. Appl. Environ. Microbiol. 59, 2614-2621
    • (1993) Appl. Environ. Microbiol. , vol.59 , pp. 2614-2621
    • Brown, S.H.1    Kelly, R.M.2
  • 28
    • 0030826555 scopus 로고    scopus 로고
    • Cloning, sequencing, and expression of the gene encoding extracellular α-amylase from Pyrococcus furiosus and biochemical characterization of the recombinant enzyme
    • Dong, G., Vieille, C., Savchenko, A. and Zeikus, J. G. (1997) Cloning, sequencing, and expression of the gene encoding extracellular α-amylase from Pyrococcus furiosus and biochemical characterization of the recombinant enzyme. Appl. Environ. Microbiol. 63, 3569-3576
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 3569-3576
    • Dong, G.1    Vieille, C.2    Savchenko, A.3    Zeikus, J.G.4
  • 30
    • 0034885332 scopus 로고    scopus 로고
    • Cellobiose uptake in the hyperthermophilic archaeon Pyrococcus furiosus is mediated by an inducible, high-affinity ABC transporter
    • Koning, S. M., Elferink, M. G., Konings, W. N. and Driessen, A. J. (2001) Cellobiose uptake in the hyperthermophilic archaeon Pyrococcus furiosus is mediated by an inducible, high-affinity ABC transporter. J. Bacteriol. 183, 4979-4984
    • (2001) J. Bacteriol. , vol.183 , pp. 4979-4984
    • Koning, S.M.1    Elferink, M.G.2    Konings, W.N.3    Driessen, A.J.4
  • 31
    • 0031888811 scopus 로고    scopus 로고
    • Archaeal binding protein-dependent ABC transporter: Molecular and biochemical analysis of the trehalose/maltose transport system of the hyperthermophilic archaeon Thermococcus litoralis
    • Horlacher, R., Xavier, K. B., Santos, H., DiRuggiero, J., Kossmann, M. and Boos, W. (1998) Archaeal binding protein-dependent ABC transporter: molecular and biochemical analysis of the trehalose/maltose transport system of the hyperthermophilic archaeon Thermococcus litoralis. J. Bacteriol. 180, 680-689
    • (1998) J. Bacteriol. , vol.180 , pp. 680-689
    • Horlacher, R.1    Xavier, K.B.2    Santos, H.3    DiRuggiero, J.4    Kossmann, M.5    Boos, W.6
  • 32
    • 0029779716 scopus 로고    scopus 로고
    • High-affinity maltose/trehalose transport system in the hyperthermophilic archaeon Thermococcus litoralis
    • Xavier, K. B., Martins, L. O., Peist, R., Kossmann, M., Boos, W. and Santos, H. (1996) High-affinity maltose/trehalose transport system in the hyperthermophilic archaeon Thermococcus litoralis. J. Bacteriol. 178, 4773-4777
    • (1996) J. Bacteriol. , vol.178 , pp. 4773-4777
    • Xavier, K.B.1    Martins, L.O.2    Peist, R.3    Kossmann, M.4    Boos, W.5    Santos, H.6
  • 33
    • 0345151823 scopus 로고    scopus 로고
    • Genetic identification of three ABC transporters as essential elements for nitrate respiration in Haloferax volcanii
    • Wanner, C. and Soppa, J. (1999) Genetic identification of three ABC transporters as essential elements for nitrate respiration in Haloferax volcanii. Genetics 152, 1417-1428
    • (1999) Genetics , vol.152 , pp. 1417-1428
    • Wanner, C.1    Soppa, J.2
  • 34
    • 0026086583 scopus 로고
    • +-electrochemical potential gradient and inhibitors for the mammalian glucose transporter inhibit the transport
    • +-electrochemical potential gradient and inhibitors for the mammalian glucose transporter inhibit the transport. Biochim. Biophys. Acta 1070, 293-299
    • (1991) Biochim. Biophys. Acta , vol.1070 , pp. 293-299
    • Tawara, E.1    Kamo, N.2
  • 35
    • 0032808951 scopus 로고    scopus 로고
    • Glucose transport in the extremely thermoacidophilic Sulfolobus solfataricus involves a high-affinity membrane-integrated binding protein
    • Albers, S. V., Elferink, M. G., Charlebois, R. L., Sensen, C. W., Driessen, A. J. and Konings, W. N. (1999) Glucose transport in the extremely thermoacidophilic Sulfolobus solfataricus involves a high-affinity membrane-integrated binding protein. J. Bacteriol. 181, 4285-4291
    • (1999) J. Bacteriol. , vol.181 , pp. 4285-4291
    • Albers, S.V.1    Elferink, M.G.2    Charlebois, R.L.3    Sensen, C.W.4    Driessen, A.J.5    Konings, W.N.6
  • 36
    • 0025340796 scopus 로고
    • Purification and characterization of an α-glucosidase from a hyperthermophilic archaebacterium, Pyrococcus furiosus, exhibiting a temperature optimum of 105 to 115°C
    • Constantino, H. R., Bron, S. H. and Kelly, R. M. (1990) Purification and characterization of an α-glucosidase from a hyperthermophilic archaebacterium, Pyrococcus furiosus, exhibiting a temperature optimum of 105 to 115°C. J. Bacteriol. 173, 3654-3660
    • (1990) J. Bacteriol. , vol.173 , pp. 3654-3660
    • Constantino, H.R.1    Bron, S.H.2    Kelly, R.M.3
  • 37
    • 0025101538 scopus 로고
    • Thermostable β-galactosidase from the archaebacterium Sulfolobus solfataricus: Purification and properties
    • Pisani, F. M., Rella, R., Raia, C. A., Rozzo, C., Nucci, R., Gambacorta, A., De Rosa, M. and Rossi, M. (1990) Thermostable β-galactosidase from the archaebacterium Sulfolobus solfataricus: purification and properties. Eur. J. Biochem. 187, 321-328
    • (1990) Eur. J. Biochem. , vol.187 , pp. 321-328
    • Pisani, F.M.1    Rella, R.2    Raia, C.A.3    Rozzo, C.4    Nucci, R.5    Gambacorta, A.6    De Rosa, M.7    Rossi, M.8
  • 38
    • 84982036435 scopus 로고
    • Exo-glucosidase activity and substrate specificity of the β-glycosidase isolated from the extreme thermophile Sulfolobus solfataricus
    • Nucci, R., Moracci, M., Vaccaro, C., Vespa, N. and Rossi, M. (1993) Exo-glucosidase activity and substrate specificity of the β-glycosidase isolated from the extreme thermophile Sulfolobus solfataricus. Biotechnol. Appl. Biochem. 17, 239-250
    • (1993) Biotechnol. Appl. Biochem. , vol.17 , pp. 239-250
    • Nucci, R.1    Moracci, M.2    Vaccaro, C.3    Vespa, N.4    Rossi, M.5
  • 39
    • 0028852767 scopus 로고
    • Purification and characterization of a maltase from the extremely thermophilic crenarchaeote Sulfolobus solfataricus
    • Rolfsmeier, M. and Blum, P. (1995) Purification and characterization of a maltase from the extremely thermophilic crenarchaeote Sulfolobus solfataricus. J. Bacteriol. 177, 482-485
    • (1995) J. Bacteriol. , vol.177 , pp. 482-485
    • Rolfsmeier, M.1    Blum, P.2
  • 40
    • 0027386619 scopus 로고
    • Purification and characterization of pyruvate ferredoxin oxidoreductase from the hyperthermophilic archaeon Pyrococcus furiosus
    • Blamey, J. M. and Adams, M. W. (1993) Purification and characterization of pyruvate ferredoxin oxidoreductase from the hyperthermophilic archaeon Pyrococcus furiosus. Biochim. Biophys. Acta 1161, 19-27
    • (1993) Biochim. Biophys. Acta , vol.1161 , pp. 19-27
    • Blamey, J.M.1    Adams, M.W.2
  • 41
    • 0033168449 scopus 로고    scopus 로고
    • Variation and evolution of the citric-acid cycle: A genomic perspective
    • Huynen, M. A., Dandekar, T. and Bork, P. (1999) Variation and evolution of the citric-acid cycle: a genomic perspective. Trends Microbiol. 7, 281-291
    • (1999) Trends Microbiol. , vol.7 , pp. 281-291
    • Huynen, M.A.1    Dandekar, T.2    Bork, P.3
  • 43
    • 0032885357 scopus 로고    scopus 로고
    • Acetyl coenzyme a synthetase (ADP forming) from the hyperthermophilic Archaeon Pyrococcus furiosus: Identification, cloning, separate expression of the encoding genes, acdAl and acdBl, in Escherichia coli, and in vitro reconstitution of the active heterotetrameric enzyme from its recombinant subunits
    • Musfeldt, M., Selig, M. and Schönheit, P. (1999) Acetyl coenzyme A synthetase (ADP forming) from the hyperthermophilic Archaeon Pyrococcus furiosus: identification, cloning, separate expression of the encoding genes, acdAl and acdBl, in Escherichia coli, and in vitro reconstitution of the active heterotetrameric enzyme from its recombinant subunits. J. Bacteriol. 181, 5885-5888
    • (1999) J. Bacteriol. , vol.181 , pp. 5885-5888
    • Musfeldt, M.1    Selig, M.2    Schönheit, P.3
  • 44
    • 0036169401 scopus 로고    scopus 로고
    • Novel type of ADP-forming acetyl coenzyme a synthetase in hyperthermophilic archaea: Heterologous expression and characterization of isoenzymes from the sulfate reducer Archaeoglobus fulgidus and the methanogen Methanococcus jannaschii
    • Musfeldt, M. and Schönheit, P. (2002) Novel type of ADP-forming acetyl coenzyme A synthetase in hyperthermophilic archaea: heterologous expression and characterization of isoenzymes from the sulfate reducer Archaeoglobus fulgidus and the methanogen Methanococcus jannaschii. J. Bacteriol. 184, 636-644
    • (2002) J. Bacteriol. , vol.184 , pp. 636-644
    • Musfeldt, M.1    Schönheit, P.2
  • 45
    • 0033117895 scopus 로고    scopus 로고
    • An AMP-dependent (ATP-forming) kinase in the hyperthermophilic archaeon Pyrococcus furiosus: Characterization and novel physiological role
    • Sakuraba, H., Utsumi, E., Kujo, C. and Ohshima, T. (1999) An AMP-dependent (ATP-forming) kinase in the hyperthermophilic archaeon Pyrococcus furiosus: characterization and novel physiological role. Arch. Biochem. Biophys. 364, 125-128
    • (1999) Arch. Biochem. Biophys. , vol.364 , pp. 125-128
    • Sakuraba, H.1    Utsumi, E.2    Kujo, C.3    Ohshima, T.4
  • 46
    • 0033597824 scopus 로고    scopus 로고
    • Molecular and biochemical characterization of the ADP-dependent phosphofructokinase from the hyperthermophilic archaeon Pyrococcus furiosus
    • Tuininga, J. E., Verhees, C. H., van der Oost, J., Kengen, S. W., Stams, A. J. and de Vos, W. M. (1999) Molecular and biochemical characterization of the ADP-dependent phosphofructokinase from the hyperthermophilic archaeon Pyrococcus furiosus. J. Biol. Chem. 274, 21023-21028
    • (1999) J. Biol. Chem. , vol.274 , pp. 21023-21028
    • Tuininga, J.E.1    Verhees, C.H.2    Van Der Oost, J.3    Kengen, S.W.4    Stams, A.J.5    De Vos, W.M.6
  • 47
    • 0034529961 scopus 로고    scopus 로고
    • Biochemical characterization, cloning, and sequencing of ADP-dependent (AMP-forming) glucokinase from two hyperthermophilic archaea, Pyrococcus furiosus and Thermococcus litoralis
    • Tokyo
    • Koga, S., Yoshioka, I., Sakuraba, H., Takahashi, M., Sakasegawa, S., Shimizu, S. and Ohshima, T. (2000) Biochemical characterization, cloning, and sequencing of ADP-dependent (AMP-forming) glucokinase from two hyperthermophilic archaea, Pyrococcus furiosus and Thermococcus litoralis. J. Biochem. (Tokyo) 128, 1079-1085
    • (2000) J. Biochem. , vol.128 , pp. 1079-1085
    • Koga, S.1    Yoshioka, I.2    Sakuraba, H.3    Takahashi, M.4    Sakasegawa, S.5    Shimizu, S.6    Ohshima, T.7
  • 48
    • 0034749172 scopus 로고    scopus 로고
    • Sugar utilization in the hyperthermophilic, sulfate-reducing archaeon Archaeoglobus fulgidus strain 7324: Starch degradation to acetate and C02 via a modified Embden-Meyerhof pathway and acetyl-Coa synthetase (ADP-forming)
    • Labes, A. and Schönheit, P. (2001) Sugar utilization in the hyperthermophilic, sulfate-reducing archaeon Archaeoglobus fulgidus strain 7324: starch degradation to acetate and C02 via a modified Embden-Meyerhof pathway and acetyl-CoA synthetase (ADP-forming). Arch. Microbiol. 176, 329-338
    • (2001) Arch. Microbiol. , vol.176 , pp. 329-338
    • Labes, A.1    Schönheit, P.2
  • 49
    • 0036837983 scopus 로고    scopus 로고
    • The first archaeal ATP-dependent glucokinase, from the hyperthermophilic crenarchaeon Aeropyrum pernix, represents a monomeric, extremely thermophilic ROK glucokinase with broad hexose specificity
    • Hansen, T., Reichstein, B., Schmid, R. and Schönheit, P. (2002) The first archaeal ATP-dependent glucokinase, from the hyperthermophilic crenarchaeon Aeropyrum pernix, represents a monomeric, extremely thermophilic ROK glucokinase with broad hexose specificity. J. Bacteriol. 184, 5955-5965
    • (2002) J. Bacteriol. , vol.184 , pp. 5955-5965
    • Hansen, T.1    Reichstein, B.2    Schmid, R.3    Schönheit, P.4
  • 50
    • 18844478534 scopus 로고    scopus 로고
    • The hexokinase of the hyperthermophile Thermoproteus tenax: ATP-dependent hexokinases and ADP-dependent glucokinases, two alternatives for glucose phosphorylation in Archaea
    • Dorr, C., Zaparty, M., Tjaden, B., Brinkmann, H. and Siebers, B. (2003) The hexokinase of the hyperthermophile Thermoproteus tenax: ATP-dependent hexokinases and ADP-dependent glucokinases, two alternatives for glucose phosphorylation in Archaea. J. Biol. Chem. 278, 18744-18753
    • (2003) J. Biol. Chem. , vol.278 , pp. 18744-18753
    • Dorr, C.1    Zaparty, M.2    Tjaden, B.3    Brinkmann, H.4    Siebers, B.5
  • 51
    • 0035036956 scopus 로고    scopus 로고
    • Novel type of glucose-6-phosphate isomerase in the hyperthermophilic archaeon Pyrococcus furiosus
    • Hansen, T., Oehlmann, M. and Schönheit, P. (2001) Novel type of glucose-6-phosphate isomerase in the hyperthermophilic archaeon Pyrococcus furiosus. J. Bacteriol. 183, 3428-3435
    • (2001) J. Bacteriol. , vol.183 , pp. 3428-3435
    • Hansen, T.1    Oehlmann, M.2    Schönheit, P.3
  • 52
    • 0035798696 scopus 로고    scopus 로고
    • The phosphoglucose isomerase from the hyperthermophilic archaeon Pyrococcus furiosus is a unique glycolytic enzyme that belongs to the cupin superfamily
    • Verhees, C. H., Huynen, M. A., Ward, D. E., Schiltz, E., de Vos, W. M. and van der Oost, J. (2001) The phosphoglucose isomerase from the hyperthermophilic archaeon Pyrococcus furiosus is a unique glycolytic enzyme that belongs to the cupin superfamily. J. Biol. Chem. 276, 40926-40932
    • (2001) J. Biol. Chem. , vol.276 , pp. 40926-40932
    • Verhees, C.H.1    Huynen, M.A.2    Ward, D.E.3    Schiltz, E.4    De Vos, W.M.5    Van Der Oost, J.6
  • 53
    • 0037472632 scopus 로고    scopus 로고
    • Characterization of the cupin-type phosphoglucose isomerase from the hyperthermophilic archaeon Thermococcus litoralis
    • Jeong, J. J., Fushinobu, S., Ito, S., Jeon, B. S., Shoun, H. and Wakagi, T. (2003) Characterization of the cupin-type phosphoglucose isomerase from the hyperthermophilic archaeon Thermococcus litoralis. FEBS Lett. 535, 200-204
    • (2003) FEBS Lett. , vol.535 , pp. 200-204
    • Jeong, J.J.1    Fushinobu, S.2    Ito, S.3    Jeon, B.S.4    Shoun, H.5    Wakagi, T.6
  • 55
    • 0035212028 scopus 로고    scopus 로고
    • DNA microarray analysis of the hyperthermophilic archaeon Pyrococcus furiosus: Evidence for a new type of sulfur-reducing enzyme complex
    • Schut, G. J., Zhou, J. and Adams, M. W. (2001) DNA microarray analysis of the hyperthermophilic archaeon Pyrococcus furiosus: evidence for a new type of sulfur-reducing enzyme complex. J. Bacteriol. 183, 7027-7036
    • (2001) J. Bacteriol. , vol.183 , pp. 7027-7036
    • Schut, G.J.1    Zhou, J.2    Adams, M.W.3
  • 56
    • 0032932006 scopus 로고    scopus 로고
    • The SIS domain: A phosphosugar-binding domain
    • Bateman, A. (1999) The SIS domain: a phosphosugar-binding domain. Trends Biochem. Sci. 24, 94-95
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 94-95
    • Bateman, A.1
  • 57
    • 0033136901 scopus 로고    scopus 로고
    • Purification and characterization of an ADP-dependent phosphofructokinase from Thermococcus zilligii
    • Ronimus, R. S., Koning, J. and Morgan, H. W. (1999) Purification and characterization of an ADP-dependent phosphofructokinase from Thermococcus zilligii. Extremophiles 3, 121-129
    • (1999) Extremophiles , vol.3 , pp. 121-129
    • Ronimus, R.S.1    Koning, J.2    Morgan, H.W.3
  • 59
    • 0037066774 scopus 로고    scopus 로고
    • ADP-dependent glucokinase/ phosphofructokinase, a novel bifunctional enzyme from the hyperthermophilic archaeon Methanococcus jannaschii
    • Sakuraba, H., Yoshioka, I., Koga, S., Takahashi, M., Kitahama, Y., Satomura, T., Kawakami, R. and Ohshima, T. (2002) ADP-dependent glucokinase/ phosphofructokinase, a novel bifunctional enzyme from the hyperthermophilic archaeon Methanococcus jannaschii. J. Biol. Chem. 277, 12495-12498
    • (2002) J. Biol. Chem. , vol.277 , pp. 12495-12498
    • Sakuraba, H.1    Yoshioka, I.2    Koga, S.3    Takahashi, M.4    Kitahama, Y.5    Satomura, T.6    Kawakami, R.7    Ohshima, T.8
  • 60
    • 0035078573 scopus 로고    scopus 로고
    • Structural basis for the ADP-specificity of a novel glucokinase from a hyperthermophilic archaeon
    • Ito, S., Fushinobu, S., Yoshioka, I., Koga, S., Matsuzawa, H. and Wakagi, T. (2001) Structural basis for the ADP-specificity of a novel glucokinase from a hyperthermophilic archaeon. Struct. Fold Des. 9, 205-214
    • (2001) Struct. Fold Des. , vol.9 , pp. 205-214
    • Ito, S.1    Fushinobu, S.2    Yoshioka, I.3    Koga, S.4    Matsuzawa, H.5    Wakagi, T.6
  • 61
    • 0033961023 scopus 로고    scopus 로고
    • Purification and properties of the first-identified, archaeal, ATP-dependent 6-phosphofructokinase, an extremely thermophilic non-allosteric enzyme, from the hyperthermophile Desulfurococcus amylolyticus
    • Hansen, T. and Schönheit, P. (2000) Purification and properties of the first-identified, archaeal, ATP-dependent 6-phosphofructokinase, an extremely thermophilic non-allosteric enzyme, from the hyperthermophile Desulfurococcus amylolyticus. Arch. Microbiol. 173, 103-109
    • (2000) Arch. Microbiol. , vol.173 , pp. 103-109
    • Hansen, T.1    Schönheit, P.2
  • 62
    • 0031596609 scopus 로고    scopus 로고
    • i-dependent phosphofructokinase from Thermoproteus tenax, an archaeal descendant of an ancient line in phosphofructokinase evolution
    • i-dependent phosphofructokinase from Thermoproteus tenax, an archaeal descendant of an ancient line in phosphofructokinase evolution. J. Bacteriol. 180, 2137-2143
    • (1998) J. Bacteriol. , vol.180 , pp. 2137-2143
    • Siebers, B.1    Klenk, H.P.2    Hensel, R.3
  • 63
    • 0035800865 scopus 로고    scopus 로고
    • Archaeal fructose-1,6-bisphosphale aldolases constitute a new family of archaeal type class I aldolase
    • Siebers, B., Brinkmann, H., Dorr, C., Tjaden, B., Lilie, H., van der Oost, J. and Verhees, C. H. (2001) Archaeal fructose-1,6-bisphosphale aldolases constitute a new family of archaeal type class I aldolase. J. Biol. Chem. 276, 28710-28718
    • (2001) J. Biol. Chem. , vol.276 , pp. 28710-28718
    • Siebers, B.1    Brinkmann, H.2    Dorr, C.3    Tjaden, B.4    Lilie, H.5    Van Der Oost, J.6    Verhees, C.H.7
  • 64
    • 0033981705 scopus 로고    scopus 로고
    • Aldolases of the DhnA family: A possible solution to the problem of pentose and hexose biosynthesis in archaea
    • Galperin, M. Y., Aravind, L. and Koonin, E. V. (2000) Aldolases of the DhnA family: a possible solution to the problem of pentose and hexose biosynthesis in archaea. FEMS Microbiol. Lett. 183, 259-264
    • (2000) FEMS Microbiol. Lett. , vol.183 , pp. 259-264
    • Galperin, M.Y.1    Aravind, L.2    Koonin, E.V.3
  • 65
    • 0029976451 scopus 로고    scopus 로고
    • Tetrameric triosephosphate isomerase from hyperthermophilic Archaea
    • Kohlhoff, M., Dahm, A. and Hensel, R. (1996) Tetrameric triosephosphate isomerase from hyperthermophilic Archaea. FEBS Lett. 383, 245-250
    • (1996) FEBS Lett. , vol.383 , pp. 245-250
    • Kohlhoff, M.1    Dahm, A.2    Hensel, R.3
  • 66
  • 67
    • 0028927080 scopus 로고
    • Glyceraldehyde-3-phosphate ferredoxin oxidoreductase, a novel tungsten-containing enzyme with a potential glycolytic role in the hyperthermophilic archaeon Pyrococcus furiosus
    • Mukund, S. and Adams, M. W. (1995) Glyceraldehyde-3-phosphate ferredoxin oxidoreductase, a novel tungsten-containing enzyme with a potential glycolytic role in the hyperthermophilic archaeon Pyrococcus furiosus. J. Biol. Chem. 270, 8389-8392
    • (1995) J. Biol. Chem. , vol.270 , pp. 8389-8392
    • Mukund, S.1    Adams, M.W.2
  • 68
    • 0032561335 scopus 로고    scopus 로고
    • The ferredoxin-dependent conversion of glyceraldehyde 3-phosphate in the hyperthermophilic archaeon Pyrococcus furiosus represents a novel site of glycolytic regulation
    • van der Oost, J., Schut, G., Kengen, S. W., Hagen, W. R., Thomm, M. and de Vos, W. M. (1998) The ferredoxin-dependent conversion of glyceraldehyde 3-phosphate in the hyperthermophilic archaeon Pyrococcus furiosus represents a novel site of glycolytic regulation. J. Biol. Chem. 273, 28149-28154
    • (1998) J. Biol. Chem. , vol.273 , pp. 28149-28154
    • Van Der Oost, J.1    Schut, G.2    Kengen, S.W.3    Hagen, W.R.4    Thomm, M.5    De Vos, W.M.6
  • 69
    • 0035083111 scopus 로고    scopus 로고
    • Aldehyde oxidoreductases from Pyrococcus furiosus
    • Roy, R., Menon, A. L. and Adams, M. W. (2001) Aldehyde oxidoreductases from Pyrococcus furiosus. Methods Enzymol. 331, 132-144
    • (2001) Methods Enzymol. , vol.331 , pp. 132-144
    • Roy, R.1    Menon, A.L.2    Adams, M.W.3
  • 70
    • 0032513241 scopus 로고    scopus 로고
    • +-dependent glyceraldehyde-3-phosphate dehydrogenase from Thermoproteus tenax: The first identified archaeal member of the aldehyde dehydrogenase superfamily is a glycolytic enzyme with unusual regulatory properties
    • +-dependent glyceraldehyde-3-phosphate dehydrogenase from Thermoproteus tenax: the first identified archaeal member of the aldehyde dehydrogenase superfamily is a glycolytic enzyme with unusual regulatory properties. J. Biol. Chem. 273, 6149-6156
    • (1998) J. Biol. Chem. , vol.273 , pp. 6149-6156
    • Brunner, N.A.1    Brinkmann, H.2    Siebers, B.3    Hensel, R.4
  • 71
    • 0030868589 scopus 로고    scopus 로고
    • Comparison of archaeal and bacterial genomes: Computer analysis of protein sequences predicts novel functions and suggests a chimeric origin for the archaea
    • Koonin, E. V., Mushegian, A. R., Galperin, M. Y. and Walker, D. R. (1997) Comparison of archaeal and bacterial genomes: computer analysis of protein sequences predicts novel functions and suggests a chimeric origin for the archaea. Mol. Microbiol. 25, 619-637
    • (1997) Mol. Microbiol. , vol.25 , pp. 619-637
    • Koonin, E.V.1    Mushegian, A.R.2    Galperin, M.Y.3    Walker, D.R.4
  • 72
    • 0032461412 scopus 로고    scopus 로고
    • A superfamily of metalloenzymes unifies phosphopentomutase and cofactor-independent phosphoglycerate mutase with alkaline phosphatases and sulfatases
    • Galperin, M. Y., Bairoch, A. and Koonin, E. V. (1998) A superfamily of metalloenzymes unifies phosphopentomutase and cofactor-independent phosphoglycerate mutase with alkaline phosphatases and sulfatases. Protein Sci. 7, 1829-1835
    • (1998) Protein Sci. , vol.7 , pp. 1829-1835
    • Galperin, M.Y.1    Bairoch, A.2    Koonin, E.V.3
  • 73
    • 0037129849 scopus 로고    scopus 로고
    • Molecular characterization of phosphoglycerate mutase in archaea
    • van der Oost, J., Huynen, M. and Verhees, C. H. (2002) Molecular characterization of phosphoglycerate mutase in archaea. FEMS Microbiol. Lett. 212, 111-120
    • (2002) FEMS Microbiol. Lett. , vol.212 , pp. 111-120
    • Van Der Oost, J.1    Huynen, M.2    Verhees, C.H.3
  • 74
    • 0037165614 scopus 로고    scopus 로고
    • A divergent archaeal member of the alkaline phosphatase binuclear metalloenzyme superfamily has phosphoglycerate mutase activity
    • Graham, D. E., Xu, H. and White, R. H. (2002) A divergent archaeal member of the alkaline phosphatase binuclear metalloenzyme superfamily has phosphoglycerate mutase activity. FEBS Lett. 517, 190-194
    • (2002) FEBS Lett. , vol.517 , pp. 190-194
    • Graham, D.E.1    Xu, H.2    White, R.H.3
  • 75
    • 0028048307 scopus 로고
    • The hyperthermophilic glycolytic enzyme enolase in the archaeon, Pyrococcus furiosus: Comparison with mesophilic enolases
    • Peak, M. J., Peak, J. G., Stevens, F. J., Blamey, J., Mai, X., Zhou, Z. H. and Adams, M. W. (1994) The hyperthermophilic glycolytic enzyme enolase in the archaeon, Pyrococcus furiosus: comparison with mesophilic enolases. Arch. Biochem. Biophys. 313, 280-286
    • (1994) Arch. Biochem. Biophys. , vol.313 , pp. 280-286
    • Peak, M.J.1    Peak, J.G.2    Stevens, F.J.3    Blamey, J.4    Mai, X.5    Zhou, Z.H.6    Adams, M.W.7
  • 76
    • 0034707208 scopus 로고    scopus 로고
    • Evolutionary history of the enolase gene family
    • Tracy, M. R. and Hedges, S. B. (2000) Evolutionary history of the enolase gene family. Gene 259, 129-138
    • (2000) Gene , vol.259 , pp. 129-138
    • Tracy, M.R.1    Hedges, S.B.2
  • 77
    • 0035171348 scopus 로고    scopus 로고
    • Phosphoenolpyruvate synthetase from the hyperthermophilic archaeon Pyrococcus furiosus
    • Hutchins, A. M., Holden, J. F. and Adams, M. W. (2001) Phosphoenolpyruvate synthetase from the hyperthermophilic archaeon Pyrococcus furiosus. J. Bacteriol. 183, 709-715
    • (2001) J. Bacteriol. , vol.183 , pp. 709-715
    • Hutchins, A.M.1    Holden, J.F.2    Adams, M.W.3
  • 78
    • 0021696802 scopus 로고
    • Glucose metabolism in the extreme thermoacidophilic archaebacterium Sulfolobus solfataricus
    • De Rosa, M., Gambacorta, A., Nicolaus, B., Giardina, P., Poerio, E. and Buonocore, V. (1984) Glucose metabolism in the extreme thermoacidophilic archaebacterium Sulfolobus solfataricus. Biochem. J. 224, 407-414
    • (1984) Biochem. J. , vol.224 , pp. 407-414
    • De Rosa, M.1    Gambacorta, A.2    Nicolaus, B.3    Giardina, P.4    Poerio, E.5    Buonocore, V.6
  • 79
    • 0023837263 scopus 로고
    • Characterization of two D-glyceraldehyde-3-phosphate dehydrogenases from the extremely thermophilic archaebacterium Thermoproteus tenax
    • Hensel, R., Laumann, S., Lang, J., Heumann, H. and Lottspeich, F. (1987) Characterization of two D-glyceraldehyde-3-phosphate dehydrogenases from the extremely thermophilic archaebacterium Thermoproteus tenax. Eur. J. Biochem. 170, 325-333
    • (1987) Eur. J. Biochem. , vol.170 , pp. 325-333
    • Hensel, R.1    Laumann, S.2    Lang, J.3    Heumann, H.4    Lottspeich, F.5
  • 80
    • 0022549877 scopus 로고
    • Metabolism of glucose via a modified Entner-Doudoroff pathway in the thermoacidophilic archaeabacterium Thermoplasma acidophilum
    • Budgen, N. and Danson, M. J. (1986) Metabolism of glucose via a modified Entner-Doudoroff pathway in the thermoacidophilic archaeabacterium Thermoplasma acidophilum. FEBS Lett. 196, 207-210
    • (1986) FEBS Lett. , vol.196 , pp. 207-210
    • Budgen, N.1    Danson, M.J.2
  • 81
    • 0022839871 scopus 로고
    • Glucose dehydrogenase from the thermoacidophilic archaebacterium Sulfolobus solfataricus
    • Giardina, P., de Biasi, M. G., de Rosa, M., Gambacorta, A. and Buonocore, V. (1986) Glucose dehydrogenase from the thermoacidophilic archaebacterium Sulfolobus solfataricus. Biochem. J. 239, 517-522
    • (1986) Biochem. J. , vol.239 , pp. 517-522
    • Giardina, P.1    De Biasi, M.G.2    De Rosa, M.3    Gambacorta, A.4    Buonocore, V.5
  • 82
    • 0027462169 scopus 로고
    • Cloning, sequencing and expression of the gene encoding glucose dehydrogenase from the thermophilic archaeon Thermoplasma acidophilum
    • Bright, J. R., Bryom, D., Danson, M. J., Hough, D. W. and Towner, P. (1993) Cloning, sequencing and expression of the gene encoding glucose dehydrogenase from the thermophilic archaeon Thermoplasma acidophilum. Eur. J. Biochem. 211, 549-554
    • (1993) Eur. J. Biochem. , vol.211 , pp. 549-554
    • Bright, J.R.1    Bryom, D.2    Danson, M.J.3    Hough, D.W.4    Towner, P.5
  • 83
    • 0030871983 scopus 로고    scopus 로고
    • Carbohydrate metabolism in Thermoproteus tenax: In vivo utilization of the non-phosphorylative Entner-Doudoroff pathway and characterization of its first enzyme, glucose dehydrogenase
    • Siebers, B., Wendisch, V. F. and Hensel, R. (1997) Carbohydrate metabolism in Thermoproteus tenax: in vivo utilization of the non-phosphorylative Entner-Doudoroff pathway and characterization of its first enzyme, glucose dehydrogenase. Arch. Microbiol. 168, 120-127
    • (1997) Arch. Microbiol. , vol.168 , pp. 120-127
    • Siebers, B.1    Wendisch, V.F.2    Hensel, R.3
  • 84
    • 0029994972 scopus 로고    scopus 로고
    • Glucose dehydrogenase from the halophilic Archaeon Haloferax mediterranei: Enzyme purification, characterisation and N-terminal sequence
    • Bonete, M.-J., Pire, C., Llorca, F. I. and Camacho, M. L. (1996) Glucose dehydrogenase from the halophilic Archaeon Haloferax mediterranei: enzyme purification, characterisation and N-terminal sequence. FEBS Lett. 383, 227-229
    • (1996) FEBS Lett. , vol.383 , pp. 227-229
    • Bonete, M.-J.1    Pire, C.2    Llorca, F.I.3    Camacho, M.L.4
  • 85
    • 0035106495 scopus 로고    scopus 로고
    • Different glycolytic pathways for glucose and fructose in the halophilic archaeon Halococcus saccharolyticus
    • Johnsen, U., Selig, M., Xavier, K. B., Santos, H. and Schonheit, P. (2001) Different glycolytic pathways for glucose and fructose in the halophilic archaeon Halococcus saccharolyticus. Arch. Microbiol. 175, 52-61
    • (2001) Arch. Microbiol. , vol.175 , pp. 52-61
    • Johnsen, U.1    Selig, M.2    Xavier, K.B.3    Santos, H.4    Schonheit, P.5
  • 86
    • 0033229936 scopus 로고    scopus 로고
    • An extremely thermostable aldolase from Sulfolobus solfataricus with specificity for non-phosphorylated substrates
    • Buchanan, C. L., Connaris, H., Danson, M. J., Reeve, C. D. and Hough, D. W. (1999) An extremely thermostable aldolase from Sulfolobus solfataricus with specificity for non-phosphorylated substrates. Biochem. J. 343, 563-570
    • (1999) Biochem. J. , vol.343 , pp. 563-570
    • Buchanan, C.L.1    Connaris, H.2    Danson, M.J.3    Reeve, C.D.4    Hough, D.W.5
  • 88
    • 0024604672 scopus 로고
    • Central metabolism of the archaeabacteria: An overview
    • Danson, M. J. (1989) Central metabolism of the archaeabacteria: an overview. Can. J. Microbiol. 35, 58-63
    • (1989) Can. J. Microbiol. , vol.35 , pp. 58-63
    • Danson, M.J.1
  • 89
    • 0343488601 scopus 로고    scopus 로고
    • A reconstruction of the metabolism of Methanococcus jannaschii from sequence data
    • Selkov, E., Maltsev, N., Olsen, G. J., Overbeek, R. and Whitman, W. B. (1997) A reconstruction of the metabolism of Methanococcus jannaschii from sequence data. Gene 197, 11-26
    • (1997) Gene , vol.197 , pp. 11-26
    • Selkov, E.1    Maltsev, N.2    Olsen, G.J.3    Overbeek, R.4    Whitman, W.B.5
  • 90
    • 0032766490 scopus 로고    scopus 로고
    • Comparative genomics of the Archaea (Euryarchaeota): Evolution of conserved protein families, the stable core, and the variable shell
    • Makarova, K. S., Aravind, L., Galperin, M. Y., Grishin, N. V., Tatusov, R. L., Wolf, Y. I. and Koonin, E. V. (1999) Comparative genomics of the Archaea (Euryarchaeota): evolution of conserved protein families, the stable core, and the variable shell. Genome Res. 9, 608-628
    • (1999) Genome Res. , vol.9 , pp. 608-628
    • Makarova, K.S.1    Aravind, L.2    Galperin, M.Y.3    Grishin, N.V.4    Tatusov, R.L.5    Wolf, Y.I.6    Koonin, E.V.7
  • 91
    • 0037494947 scopus 로고    scopus 로고
    • Whole-genome DNA microarray analysis of a hyperthermophile and an archaeon: Pyrococcus furiosus grown on carbohydrates or peptides
    • Schut, G. J., Brehm, S. D., Datta, S. and Adams, M. W. (2003) Whole-genome DNA microarray analysis of a hyperthermophile and an archaeon: Pyrococcus furiosus grown on carbohydrates or peptides. J. Bacteriol. 185, 3935-3947
    • (2003) J. Bacteriol. , vol.185 , pp. 3935-3947
    • Schut, G.J.1    Brehm, S.D.2    Datta, S.3    Adams, M.W.4
  • 92
    • 0033905714 scopus 로고    scopus 로고
    • 13C-labeling experiments and nuclear magnetic resonance analysis
    • 13C-labeling experiments and nuclear magnetic resonance analysis. J. Bacteriol. 182, 4632-4636
    • (2000) J. Bacteriol. , vol.182 , pp. 4632-4636
    • Xavier, K.B.1    Da Costa, M.S.2    Santos, H.3
  • 93
    • 0020607444 scopus 로고
    • Carbohydrate metabolism in lactic acid bacteria
    • Kandler, O. (1983) Carbohydrate metabolism in lactic acid bacteria. Antonie van Leeuwenhoek 49, 209-224
    • (1983) Antonie Van Leeuwenhoek , vol.49 , pp. 209-224
    • Kandler, O.1
  • 94
    • 0020463405 scopus 로고
    • Glycogen in thermoacidophilic archaebacteria of the genera Sulfolobus, Thermoproteus, Desulfurococcus and Thermococcus
    • Konig, H., Skorko, R., Zillig, W. and Reiter, W. D. (1982) Glycogen in thermoacidophilic archaebacteria of the genera Sulfolobus, Thermoproteus, Desulfurococcus and Thermococcus. Arch. Microbiol. 132, 297-303
    • (1982) Arch. Microbiol. , vol.132 , pp. 297-303
    • Konig, H.1    Skorko, R.2    Zillig, W.3    Reiter, W.D.4
  • 95
    • 0036733379 scopus 로고    scopus 로고
    • The biochemistry and molecular biology of the glucose-6-phosphatase system
    • Maywood
    • Foster, J. D. and Nordlie, R. C. (2002) The biochemistry and molecular biology of the glucose-6-phosphatase system. Exp. Biol. Med. (Maywood) 227, 601-608
    • (2002) Exp. Biol. Med. , vol.227 , pp. 601-608
    • Foster, J.D.1    Nordlie, R.C.2
  • 96
    • 0028605844 scopus 로고
    • Isolation, sequence and characterization of the maltose-regulated mlrA gene from the hyperthermophilic archaeum Pyrococcus furiosus
    • Robinson, K. A. and Schreier, H. J. (1994) Isolation, sequence and characterization of the maltose-regulated mlrA gene from the hyperthermophilic archaeum Pyrococcus furiosus. Gene 151, 173-176
    • (1994) Gene , vol.151 , pp. 173-176
    • Robinson, K.A.1    Schreier, H.J.2
  • 97
    • 0035158352 scopus 로고    scopus 로고
    • Key role for sulfur in peptide metabolism and in regulation of three hydrogenases in the hyperthermophilic archaeon Pyrococcus furiosus
    • Adams, M. W., Holden, J. F., Menon, A. L., Schut, G. J., Grunden, A. M., Hou, C., Hutchins, A. M., Jenney, Jr, F. E., Kim, C., Ma, K. et al. (2001) Key role for sulfur in peptide metabolism and in regulation of three hydrogenases in the hyperthermophilic archaeon Pyrococcus furiosus. J. Bacteriol. 183, 716-724
    • (2001) J. Bacteriol. , vol.183 , pp. 716-724
    • Adams, M.W.1    Holden, J.F.2    Menon, A.L.3    Schut, G.J.4    Grunden, A.M.5    Hou, C.6    Hutchins, A.M.7    Jenney F.E., Jr.8    Kim, C.9    Ma, K.10
  • 98
    • 0033756225 scopus 로고    scopus 로고
    • MJ0109 is an enzyme that is both an inositol monophosphatase and the 'missing' archaeal fructose-1,6-bisphosphatase
    • Stec, B., Yang, H., Johnson, K. A., Chen, L. and Roberts, M. F. (2000) MJ0109 is an enzyme that is both an inositol monophosphatase and the 'missing' archaeal fructose-1,6-bisphosphatase. Nat. Struct. Biol. 7, 1046-1050
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 1046-1050
    • Stec, B.1    Yang, H.2    Johnson, K.A.3    Chen, L.4    Roberts, M.F.5
  • 99
    • 0036275509 scopus 로고    scopus 로고
    • Molecular and biochemical characterization of a distinct type of fructose-1,6-bisphosphatase from Pyrococcus furiosus
    • Verhees, C. H., Akerboom, J., Schiltz, E., de Vos, W. M. and van der Oost, J. (2002) Molecular and biochemical characterization of a distinct type of fructose-1,6-bisphosphatase from Pyrococcus furiosus. J. Bacteriol. 184, 3401-3405
    • (2002) J. Bacteriol. , vol.184 , pp. 3401-3405
    • Verhees, C.H.1    Akerboom, J.2    Schiltz, E.3    De Vos, W.M.4    Van Der Oost, J.5
  • 100
    • 0037163028 scopus 로고    scopus 로고
    • A novel candidate for the true fructose 1,6-bisphosphatase in archaea
    • Rashid, N., Imanaka, H., Kanai, T., Fukui, T., Atomi, H. and Imanaka, T. (2002) A novel candidate for the true fructose 1,6-bisphosphatase in archaea. J. Biol. Chem. 277, 30649-30655
    • (2002) J. Biol. Chem. , vol.277 , pp. 30649-30655
    • Rashid, N.1    Imanaka, H.2    Kanai, T.3    Fukui, T.4    Atomi, H.5    Imanaka, T.6
  • 101
    • 0037391699 scopus 로고    scopus 로고
    • Global metabolic regulation analysis for Escherichia coli K12 based on protein expression by 2-dimensional electrophoresis and enzyme activity measurement
    • Peng, L. and Shimizu, K. (2003) Global metabolic regulation analysis for Escherichia coli K12 based on protein expression by 2-dimensional electrophoresis and enzyme activity measurement. Appl. Microbiol. Biotechnol. 61, 163-178
    • (2003) Appl. Microbiol. Biotechnol. , vol.61 , pp. 163-178
    • Peng, L.1    Shimizu, K.2
  • 102
    • 0037066717 scopus 로고    scopus 로고
    • Global expression profiling of acetate-grown Escherichia coli
    • Oh, M. K., Rohlin, L., Kao, K. C. and Liao, J. C. (2002) Global expression profiling of acetate-grown Escherichia coli. J. Biol. Chem. 277, 13175-13183
    • (2002) J. Biol. Chem. , vol.277 , pp. 13175-13183
    • Oh, M.K.1    Rohlin, L.2    Kao, K.C.3    Liao, J.C.4
  • 103
    • 0029147255 scopus 로고
    • The global regulatory protein FruR modulates the direction of carbon flow in Escherichia coli
    • Ramseier, T. M., Bledig, S., Michotey, V., Feghali, R. and Saier, Jr, M. H. (1995) The global regulatory protein FruR modulates the direction of carbon flow in Escherichia coli. Mol. Microbiol. 16, 1157-1169
    • (1995) Mol. Microbiol. , vol.16 , pp. 1157-1169
    • Ramseier, T.M.1    Bledig, S.2    Michotey, V.3    Feghali, R.4    Saier M.H., Jr.5
  • 104
    • 0036217950 scopus 로고    scopus 로고
    • Regulation of gene expression in the PTS in Escherichia coli: The role and interactions of Mfc
    • Plumbridge, J. (2002) Regulation of gene expression in the PTS in Escherichia coli: the role and interactions of Mfc. Curr. Opin. Microbiol. 5, 187-193
    • (2002) Curr. Opin. Microbiol. , vol.5 , pp. 187-193
    • Plumbridge, J.1
  • 105
    • 0033118825 scopus 로고    scopus 로고
    • Interplay of global regulators and cell physiology in the general stress response of Escherichia coli
    • Hengge-Aronis, R. (1999) Interplay of global regulators and cell physiology in the general stress response of Escherichia coli. Curr. Opin. Microbiol. 2, 148-152
    • (1999) Curr. Opin. Microbiol. , vol.2 , pp. 148-152
    • Hengge-Aronis, R.1
  • 106
    • 0027193138 scopus 로고
    • Identification of a novel operon in Lactococcus lactis encoding three enzymes for lactic acid synthesis: Phosphofructokinase, pyruvate kinase, and lactate dehydrogenase
    • Llanos, R. M., Harris, C. J., Hillier, A. J. and Davidson, B. E. (1993) Identification of a novel operon in Lactococcus lactis encoding three enzymes for lactic acid synthesis: phosphofructokinase, pyruvate kinase, and lactate dehydrogenase. J. Bacteriol. 175, 2541-2551
    • (1993) J. Bacteriol. , vol.175 , pp. 2541-2551
    • Llanos, R.M.1    Harris, C.J.2    Hillier, A.J.3    Davidson, B.E.4
  • 107
    • 0031735564 scopus 로고    scopus 로고
    • Transcriptional activation of the glycolytic las operon and catabolite repression of the gal operon in Lactococcus lactis are mediated by the catabolite control protein CcpA
    • Luesink, E. J., van Herpen, R. E., Grossiord, B. P., Kuipers, O. P. and de Vos, W. M. (1998) Transcriptional activation of the glycolytic las operon and catabolite repression of the gal operon in Lactococcus lactis are mediated by the catabolite control protein CcpA. Mol. Microbiol. 30, 789-798
    • (1998) Mol. Microbiol. , vol.30 , pp. 789-798
    • Luesink, E.J.1    Van Herpen, R.E.2    Grossiord, B.P.3    Kuipers, O.P.4    De Vos, W.M.5
  • 109
    • 0022818244 scopus 로고
    • Glycolytic gene expression in Saccharomyces cerevisiae: Nucleotide sequence of GRC1, null mutations, and evidence for expression
    • Baker, H. V. (1986) Glycolytic gene expression in Saccharomyces cerevisiae: nucleotide sequence of GRC1, null mutations, and evidence for expression. Mol. Cell. Biol. 6, 3774-3784
    • (1986) Mol. Cell. Biol. , vol.6 , pp. 3774-3784
    • Baker, H.V.1
  • 110
    • 0026094551 scopus 로고
    • GCR1 of Saccharomyces cerevisiae encodes a DNA binding protein whose binding is abolished by mutations in the CTTCC sequence motif
    • Baker, H. V. (1991 ) GCR1 of Saccharomyces cerevisiae encodes a DNA binding protein whose binding is abolished by mutations in the CTTCC sequence motif. Proc. Natl. Acad. Sci. U.S.A. 88, 9443-9447
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 9443-9447
    • Baker, H.V.1
  • 111
    • 0027418935 scopus 로고
    • Gluconeogenesis from pyruvate in the hyperthermophilic archaeon Pyrococcus furiosus: Involvement of reactions of the Embden-Meyerhof pathway
    • Schäfer, T. and Schönheit, P. (1993) Gluconeogenesis from pyruvate in the hyperthermophilic archaeon Pyrococcus furiosus: involvement of reactions of the Embden-Meyerhof pathway. Arch. Microbiol. 159, 359-363
    • (1993) Arch. Microbiol. , vol.159 , pp. 359-363
    • Schäfer, T.1    Schönheit, P.2
  • 112
    • 0030956750 scopus 로고    scopus 로고
    • Multiple recruitment of class-I aldolase to chloroplasts and eubacterial origin of eukaryotic class-II aldolases revealed by cDNAs from Euglena gracilis
    • Plaumann, M., Pelzer-Reith, B., Martin, W. F. and Schnarrenberger, C. (1997) Multiple recruitment of class-I aldolase to chloroplasts and eubacterial origin of eukaryotic class-II aldolases revealed by cDNAs from Euglena gracilis. Curr. Genet. 31, 430-438
    • (1997) Curr. Genet. , vol.31 , pp. 430-438
    • Plaumann, M.1    Pelzer-Reith, B.2    Martin, W.F.3    Schnarrenberger, C.4
  • 113
    • 0030066139 scopus 로고    scopus 로고
    • Primary structure and phylogeny of the Calvin cycle enzymes transketolase and fructosebisphosphate aldolase of Xanthobacter flavus
    • van den Bergh, E. R., Baker, S. C., Raggers, R. J., Terpstra, P., Woudstra, E. C., Dijkhuizen, L. and Meijer, W. G. (1996) Primary structure and phylogeny of the Calvin cycle enzymes transketolase and fructosebisphosphate aldolase of Xanthobacter flavus. J. Bacteriol. 178, 888-893
    • (1996) J. Bacteriol. , vol.178 , pp. 888-893
    • Van Den Bergh, E.R.1    Baker, S.C.2    Raggers, R.J.3    Terpstra, P.4    Woudstra, E.C.5    Dijkhuizen, L.6    Meijer, W.G.7
  • 115
    • 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. and Hensel, R. (2000) Pyruvate kinase of the hyperthermophilic crenarchaeote Thermoproteus tenax: physiological role and phylogenetic aspects. J. Bacteriol. 182, 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
  • 116
    • 0035321642 scopus 로고    scopus 로고
    • Role of two different glyceraldehyde-3-phosphate dehydrogenases in controlling the reversible Embden-Meyerhof-Parnas pathway in Thermoproteus tenax: Regulation on protein and transcript level
    • Brunner, N. A., Siebers, B. and Hensel, R. (2001) Role of two different glyceraldehyde-3-phosphate dehydrogenases in controlling the reversible Embden-Meyerhof-Parnas pathway in Thermoproteus tenax: regulation on protein and transcript level. Extremophiles 5, 101-109
    • (2001) Extremophiles , vol.5 , pp. 101-109
    • Brunner, N.A.1    Siebers, B.2    Hensel, R.3
  • 118
    • 0035451127 scopus 로고    scopus 로고
    • Modularity in the gain and loss of genes: Applications for function prediction
    • Ettema, T., van der Oost, J. and Huynen, M. (2001) Modularity in the gain and loss of genes: applications for function prediction. Trends Genet. 17, 485-487
    • (2001) Trends Genet. , vol.17 , pp. 485-487
    • Ettema, T.1    Van Der Oost, J.2    Huynen, M.3
  • 120
    • 0020623423 scopus 로고
    • The archaeabacterium Thermococcus celer represents a novel genus within the thermophilic branch of the archaeabacteria
    • Zillig, W., Holz, I., Janekovic, D., Schäfer, T. and Reiter, W. D. (1983) The archaeabacterium Thermococcus celer represents a novel genus within the thermophilic branch of the archaeabacteria. Syst. Appl. Microbiol. 4, 88-94
    • (1983) Syst. Appl. Microbiol. , vol.4 , pp. 88-94
    • Zillig, W.1    Holz, I.2    Janekovic, D.3    Schäfer, T.4    Reiter, W.D.5
  • 121
    • 0030875412 scopus 로고    scopus 로고
    • The phylogenetic position of the Thermococcus isolate AN1 based on 16 S rRNA gene sequence analysis: A proposal that AN1 represents a new species, Thermococcus zilligii sp. nov.
    • Ronimus, R. S., Reysenbach, A., Musgrave, D. R. and Morgan, H. W. (1997) The phylogenetic position of the Thermococcus isolate AN1 based on 16 S rRNA gene sequence analysis: a proposal that AN1 represents a new species, Thermococcus zilligii sp. nov. Arch. Microbiol. 168, 245-248
    • (1997) Arch. Microbiol. , vol.168 , pp. 245-248
    • Ronimus, R.S.1    Reysenbach, A.2    Musgrave, D.R.3    Morgan, H.W.4
  • 122
    • 0033003021 scopus 로고    scopus 로고
    • Maltose metabolism in the hyperthermophilic archaeon Thermococcus litoralis: Purification and characterization of key enzymes
    • Xavier, K. B., Peist, R., Kossmann, M., Boos, W. and Santos, H. (1999) Maltose metabolism in the hyperthermophilic archaeon Thermococcus litoralis: purification and characterization of key enzymes. J. Bacteriol. 181, 3358-3367
    • (1999) J. Bacteriol. , vol.181 , pp. 3358-3367
    • Xavier, K.B.1    Peist, R.2    Kossmann, M.3    Boos, W.4    Santos, H.5
  • 124
    • 0031753314 scopus 로고    scopus 로고
    • Thermococcus guaymasensis sp. nov. and Thermococcus aggregans sp. nov., two novel thermophilic archaea isolated from the Guaymas Basin hydrothermal vent site
    • Canganella, F., Jones, W. J., Gambacorta, A. and Antranikian, G. (1998) Thermococcus guaymasensis sp. nov. and Thermococcus aggregans sp. nov., two novel thermophilic archaea isolated from the Guaymas Basin hydrothermal vent site. Int. J. Syst. Bacteriol. 48, 1181-1185
    • (1998) Int. J. Syst. Bacteriol. , vol.48 , pp. 1181-1185
    • Canganella, F.1    Jones, W.J.2    Gambacorta, A.3    Antranikian, G.4
  • 126
    • 0029817510 scopus 로고    scopus 로고
    • Thermococcus fumicolans sp. nov., a new hyperthermophilic archaeon isolated from a deep-sea hydrothermal vent in the north Fiji Basin
    • Godfroy, A., Meunier, J. R., Guezennec, J., Lesongeur, F., Raguenes, G., Rimbault, A. and Barbier, G. (1996) Thermococcus fumicolans sp. nov., a new hyperthermophilic archaeon isolated from a deep-sea hydrothermal vent in the north Fiji Basin. Int. J. Syst. Bacteriol. 46, 1113-1119
    • (1996) Int. J. Syst. Bacteriol. , vol.46 , pp. 1113-1119
    • Godfroy, A.1    Meunier, J.R.2    Guezennec, J.3    Lesongeur, F.4    Raguenes, G.5    Rimbault, A.6    Barbier, G.7
  • 127
    • 0029153768 scopus 로고
    • Properties of glutamate dehydrogenase and its involvement in alanine production in a hyperthermophilic archaeon, Thermococcus profundus
    • Tokyo
    • Kobayashi, T., Higuchi, S., Kimura, K., Kudo, T. and Horikoshi, K. (1995) Properties of glutamate dehydrogenase and its involvement in alanine production in a hyperthermophilic archaeon, Thermococcus profundus. J. Biochem. (Tokyo) 118, 587-592
    • (1995) J. Biochem. , vol.118 , pp. 587-592
    • Kobayashi, T.1    Higuchi, S.2    Kimura, K.3    Kudo, T.4    Horikoshi, K.5
  • 129
    • 0000549004 scopus 로고
    • Halobacterium mediterranei spec. nov., a new carbohydrate-utilizing extreme halophile
    • Rodriguez-Valera, F., Juez, G. and Kushner, D. J. (1983) Halobacterium mediterranei spec. nov., a new carbohydrate-utilizing extreme halophile. Syst. Appl. Microbiol. 4, 369-381
    • (1983) Syst. Appl. Microbiol. , vol.4 , pp. 369-381
    • Rodriguez-Valera, F.1    Juez, G.2    Kushner, D.J.3
  • 130
    • 0025355485 scopus 로고
    • Indication of a modifies EMP pathway for fructose breakdown in a halophilic archaebacterium
    • Altekar, W. and Rangaswamy, V. (1990) Indication of a modifies EMP pathway for fructose breakdown in a halophilic archaebacterium. FEBS Microbiol. Lett. 69, 139-143
    • (1990) FEBS Microbiol. Lett. , vol.69 , pp. 139-143
    • Altekar, W.1    Rangaswamy, V.2
  • 131
    • 0024150562 scopus 로고
    • Alternative routes of carbohydrate metabolism in halophilic archaebacteria
    • Rawal, N., Kelkar, S. M. and Altekar, W. (1988) Alternative routes of carbohydrate metabolism in halophilic archaebacteria. Indian J. Biochem. Biophys. 25, 674-686
    • (1988) Indian J. Biochem. Biophys. , vol.25 , pp. 674-686
    • Rawal, N.1    Kelkar, S.M.2    Altekar, W.3
  • 132
    • 0037103749 scopus 로고    scopus 로고
    • Biochemical adaptations of two sugar kinases from the hyperthermophilic archaeon Pyrococcus furiosus
    • Verhees, C. H., Koot, D. G. M., Ettema, T. J. G., Dijkema, C., de Vos, W. M. and van der Oost, J. (2002) Biochemical adaptations of two sugar kinases from the hyperthermophilic archaeon Pyrococcus furiosus. Biochem. J. 366, 121-127
    • (2002) Biochem. J. , vol.366 , pp. 121-127
    • Verhees, C.H.1    Koot, D.G.M.2    Ettema, T.J.G.3    Dijkema, C.4    De Vos, W.M.5    Van Der Oost, J.6
  • 133
    • 0028895142 scopus 로고
    • The PGK and glyceraldehyde-3-phosphate dehydrogenase genes from the thermophilic archaeon Sulfolobus solflataricus overlap by 8-bp: Isolation, sequencing of the genes and expression in Escherichia coli
    • Jones, C. E., Fleming, T. M., Cowan, D. A., Littlechild, J. A. and Piper, P. W. (1995) The PGK and glyceraldehyde-3-phosphate dehydrogenase genes from the thermophilic archaeon Sulfolobus solflataricus overlap by 8-bp: isolation, sequencing of the genes and expression in Escherichia coli. Eur. J. Biochem. 233, 800-808
    • (1995) Eur. J. Biochem. , vol.233 , pp. 800-808
    • Jones, C.E.1    Fleming, T.M.2    Cowan, D.A.3    Littlechild, J.A.4    Piper, P.W.5
  • 134
    • 0025279399 scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic archaebacterium Pyrococcus woesei: Characterization of the enzyme, cloning and sequencing of the gene, and expression in Escherichia coli
    • Zwickl, P., Fabry, S., Bogedain, C., Haas, A. and Hensel, R. (1990) Glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic archaebacterium Pyrococcus woesei: characterization of the enzyme, cloning and sequencing of the gene, and expression in Escherichia coli. J. Bacteriol. 172, 4329-4338
    • (1990) J. Bacteriol. , vol.172 , pp. 4329-4338
    • Zwickl, P.1    Fabry, S.2    Bogedain, C.3    Haas, A.4    Hensel, R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.