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Volumn 189, Issue 24, 2007, Pages 8901-8913

Unusual starch degradation pathway via cyclodextrins in the hyperthermophilic sulfate-reducing archaeon Archaeoglobus fulgidus strain 7324

Author keywords

[No Author keywords available]

Indexed keywords

AMYLASE; AMYLOPULLULANASE; BETA CYCLODEXTRIN; CYCLODEXTRIN; CYCLODEXTRINASE; CYCLOMALTODEXTRIN GLUCANOTRANSFERASE; DEXTRIN; ENZYME; GLUCOSE 6 PHOSPHATE; MALTODEXTRIN PHOSPHORYLASE; MALTOOLIGODEXTRIN; STARCH; SULFATE; UNCLASSIFIED DRUG;

EID: 37449008528     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.01136-07     Document Type: Article
Times cited : (33)

References (76)
  • 1
    • 24644491356 scopus 로고    scopus 로고
    • Characterization of a thermostable enzyme with phosphomannomutase/phosphoglucomutase activities from the hyperthermophilic archaeon Pyrococcus horikoshii OT3
    • Akutsu, J., Z. Zhang, M. Tsujimura, M. Sasaki, M. Yohda, and Y. Kawarabayasi. 2005. Characterization of a thermostable enzyme with phosphomannomutase/phosphoglucomutase activities from the hyperthermophilic archaeon Pyrococcus horikoshii OT3. J. Biochem. 138:159-166.
    • (2005) J. Biochem , vol.138 , pp. 159-166
    • Akutsu, J.1    Zhang, Z.2    Tsujimura, M.3    Sasaki, M.4    Yohda, M.5    Kawarabayasi, Y.6
  • 5
    • 0017413485 scopus 로고
    • Cyclodextrin glucanotransferase from Klebsiella pneumoniae. 2. Significance of the enzyme for the metabolism of cyclodextrins by Klebsiella pneumoniae M 5
    • Bender, H. 1977. Cyclodextrin glucanotransferase from Klebsiella pneumoniae. 2. Significance of the enzyme for the metabolism of cyclodextrins by Klebsiella pneumoniae M 5. Arch. Microbiol. 113:49-56.
    • (1977) Arch. Microbiol , vol.113 , pp. 49-56
    • Bender, H.1
  • 6
    • 0036525719 scopus 로고    scopus 로고
    • Starch-hydrolyzing enzymes from thermophilic archaea and bacteria
    • Bertoldo, C., and G. Antranikian. 2002. Starch-hydrolyzing enzymes from thermophilic archaea and bacteria. Curr. Opin. Chem. Biol. 6:151-160.
    • (2002) Curr. Opin. Chem. Biol , vol.6 , pp. 151-160
    • Bertoldo, C.1    Antranikian, G.2
  • 8
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254.
    • (1976) Anal. Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 9
    • 0025325482 scopus 로고
    • Characterization of amylolytic enzyme activities associated with the hyperthermophilic archaebacterium Pyrococcus furiosus
    • Brown, S. H., H. R. Costantino, and R. M. Kelly. 1990. Characterization of amylolytic enzyme activities associated with the hyperthermophilic archaebacterium Pyrococcus furiosus. Appl. Environ. Microbiol. 56:1985-1991.
    • (1990) Appl. Environ. Microbiol , vol.56 , pp. 1985-1991
    • Brown, S.H.1    Costantino, H.R.2    Kelly, R.M.3
  • 10
    • 0000388337 scopus 로고
    • Fructose degradation by Desulfovibrio sp. in pure culture and in coculture with Methanospirillum hungatei
    • Cord-Ruwisch, R., B. Ollivier, and J. Garcia. 1986. Fructose degradation by Desulfovibrio sp. in pure culture and in coculture with Methanospirillum hungatei. Curr. Microbiol. 13:285-289.
    • (1986) Curr. Microbiol , vol.13 , pp. 285-289
    • Cord-Ruwisch, R.1    Ollivier, B.2    Garcia, J.3
  • 13
    • 0029965735 scopus 로고    scopus 로고
    • Metabolism of cyclodextrins by Klebsiella oxytoca m5a1: Purification and characterization of a cytoplasmically located cyclodextrinase
    • Feederle, R., M. Pajatsch, E. Kremmer, and A. Bock. 1996. Metabolism of cyclodextrins by Klebsiella oxytoca m5a1: purification and characterization of a cytoplasmically located cyclodextrinase. Arch. Microbiol. 165:206-212.
    • (1996) Arch. Microbiol , vol.165 , pp. 206-212
    • Feederle, R.1    Pajatsch, M.2    Kremmer, E.3    Bock, A.4
  • 14
    • 0022445886 scopus 로고
    • Pyrococcus furiosus sp. nov. represents a novel genus of marine heterotrophic archaebacteria growing optimally at 100°C
    • Fiala, G., and K. O. Stetter. 1986. Pyrococcus furiosus sp. nov. represents a novel genus of marine heterotrophic archaebacteria growing optimally at 100°C. Arch. Microbiol. 145:56-61.
    • (1986) Arch. Microbiol , vol.145 , pp. 56-61
    • Fiala, G.1    Stetter, K.O.2
  • 15
    • 0029919677 scopus 로고    scopus 로고
    • Genetics of a novel starch utilization pathway present in Klebsiella oxytoca
    • Fiedler, G., M. Pajatsch, and A. Bock. 1996. Genetics of a novel starch utilization pathway present in Klebsiella oxytoca. J. Mol. Biol. 256:279-291.
    • (1996) J. Mol. Biol , vol.256 , pp. 279-291
    • Fiedler, G.1    Pajatsch, M.2    Bock, A.3
  • 16
    • 0028038878 scopus 로고
    • Purification and characterization of phosphoglucomutase from peas
    • Galloway, C. M., and W. M. Dugger. 1994. Purification and characterization of phosphoglucomutase from peas. Physiologia Plantarium 92:479-486.
    • (1994) Physiologia Plantarium , vol.92 , pp. 479-486
    • Galloway, C.M.1    Dugger, W.M.2
  • 17
    • 29144498155 scopus 로고    scopus 로고
    • Mutagenesis of catalytically important residues of cupin type phosphoglucose isomerase from Archaeoglobus fulgidus
    • Hansen, T., B. Schlichting, J. Grötzinger, M. K. Swan, C. Davies, and P. Schönheit. 2005. Mutagenesis of catalytically important residues of cupin type phosphoglucose isomerase from Archaeoglobus fulgidus. FEBS J. 272:6266-6275.
    • (2005) FEBS J , vol.272 , pp. 6266-6275
    • Hansen, T.1    Schlichting, B.2    Grötzinger, J.3    Swan, M.K.4    Davies, C.5    Schönheit, P.6
  • 18
    • 0028576948 scopus 로고
    • Metabolism of sulfate-reducing prokaryotes
    • Hansen, T. A. 1994. Metabolism of sulfate-reducing prokaryotes. Antonie Leeuwenhoek 66:165-185.
    • (1994) Antonie Leeuwenhoek , vol.66 , pp. 165-185
    • Hansen, T.A.1
  • 19
    • 0000703464 scopus 로고
    • Starch gel for gel filtration
    • Hanus, J., and J. Kucera. 1974. Starch gel for gel filtration. J. Chromatogr. 97:270-272.
    • (1974) J. Chromatogr , vol.97 , pp. 270-272
    • Hanus, J.1    Kucera, J.2
  • 20
    • 0034889240 scopus 로고    scopus 로고
    • Extracellular synthesis, specific recognition, and intracellular degradation of cyclomaltodextrins by the hyperthermophilic archaeon Thermococcus sp. strain B1001
    • Hashimoto, Y., T. Yamamoto, S. Fujiwara, M. Takagi, and T. Imanaka. 2001. Extracellular synthesis, specific recognition, and intracellular degradation of cyclomaltodextrins by the hyperthermophilic archaeon Thermococcus sp. strain B1001. J. Bacteriol. 183:5050-5057.
    • (2001) J. Bacteriol , vol.183 , pp. 5050-5057
    • Hashimoto, Y.1    Yamamoto, T.2    Fujiwara, S.3    Takagi, M.4    Imanaka, T.5
  • 21
    • 0026055308 scopus 로고
    • A classification of glycosyl hydrolases based on amino acid sequence similarities
    • Henrissat, B. 1991. A classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem. J. 280(Pt. 2):309-316.
    • (1991) Biochem. J , vol.280 , Issue.PART. 2 , pp. 309-316
    • Henrissat, B.1
  • 22
    • 0035899987 scopus 로고    scopus 로고
    • Identification of the catalytic residue of Thermococcus litoralis 4-α-glucano-transferase through mechanism-based labeling
    • Imamura, H., S. Fushinobu, B. S. Jeon, T. Wakagi, and H. Matsuzawa. 2001. Identification of the catalytic residue of Thermococcus litoralis 4-α-glucano-transferase through mechanism-based labeling. Biochemistry 40:12400-12406.
    • (2001) Biochemistry , vol.40 , pp. 12400-12406
    • Imamura, H.1    Fushinobu, S.2    Jeon, B.S.3    Wakagi, T.4    Matsuzawa, H.5
  • 23
    • 0024485990 scopus 로고
    • Pattern of action of Bacillus stearother-mophilus neopullulanase on pullulan
    • Imanaka, T., and T. Kuriki. 1989. Pattern of action of Bacillus stearother-mophilus neopullulanase on pullulan. J. Bacteriol. 171:369-374.
    • (1989) J. Bacteriol , vol.171 , pp. 369-374
    • Imanaka, T.1    Kuriki, T.2
  • 24
    • 0030738673 scopus 로고    scopus 로고
    • 4-α-Glucanotransferase from the hyperthermophilic archaeon Thermococcus litoralis: Enzyme purification and characterization and gene cloning, sequencing, and expression in Escherichia coli
    • Jeon, B. S., H. Taguchi, H. Sakai, T. Ohshima, T. Wakagi, and H. Matsuzawa. 1997. 4-α-Glucanotransferase from the hyperthermophilic archaeon Thermococcus litoralis: enzyme purification and characterization and gene cloning, sequencing, and expression in Escherichia coli. Eur. J. Biochem. 248:171-178.
    • (1997) Eur. J. Biochem , vol.248 , pp. 171-178
    • Jeon, B.S.1    Taguchi, H.2    Sakai, H.3    Ohshima, T.4    Wakagi, T.5    Matsuzawa, H.6
  • 25
    • 0037477763 scopus 로고    scopus 로고
    • Comparative analysis of pyruvate kinases from the hyperthermophilic archaea Archaeoglobus fulgidus, Aeropyrum pernix, and Pyrobaculum aerophilum and the hyperthermophilic bacterium Thermotoga maritima: Unusual regulatory properties in hyperthermophilic archaea
    • Johnsen, U., T. Hansen, and P. Schönheit. 2003. Comparative analysis of pyruvate kinases from the hyperthermophilic archaea Archaeoglobus fulgidus, Aeropyrum pernix, and Pyrobaculum aerophilum and the hyperthermophilic bacterium Thermotoga maritima: unusual regulatory properties in hyperthermophilic archaea. J. Biol. Chem. 278:25417-25427.
    • (2003) J. Biol. Chem , vol.278 , pp. 25417-25427
    • Johnsen, U.1    Hansen, T.2    Schönheit, P.3
  • 26
    • 0036304348 scopus 로고    scopus 로고
    • Crystal structures and structural comparison of Thermoactinomyces vulgaris R-47 alpha-amylase 1 (TVAI) at 1.6 Åresolution and alpha-amylase 2 (TVAII) at 2.3 Åresolution
    • Kamitori, S., A. Abe, A. Ohtaki, A. Kaji, T. Tonozuka, and Y. Sakano. 1999. Crystal structures and structural comparison of Thermoactinomyces vulgaris R-47 alpha-amylase 1 (TVAI) at 1.6 Åresolution and alpha-amylase 2 (TVAII) at 2.3 Åresolution. J. Mol. Biol. 318:443-453.
    • (1999) J. Mol. Biol , vol.318 , pp. 443-453
    • Kamitori, S.1    Abe, A.2    Ohtaki, A.3    Kaji, A.4    Tonozuka, T.5    Sakano, Y.6
  • 27
    • 6344229684 scopus 로고    scopus 로고
    • Identification of an alkaline-tolerant cyclodextrin-metabolizing bacterium and characterization of its cyclodextrinase gene
    • Kaulpiboon, J., V. Rimphanitchayakit, and P. Pongsawasdi. 2004. Identification of an alkaline-tolerant cyclodextrin-metabolizing bacterium and characterization of its cyclodextrinase gene. J. Basic Microbiol. 44:374-382.
    • (2004) J. Basic Microbiol , vol.44 , pp. 374-382
    • Kaulpiboon, J.1    Rimphanitchayakit, V.2    Pongsawasdi, P.3
  • 28
    • 0031458333 scopus 로고    scopus 로고
    • Klenk, H. P., R. A. Clayton, J. F. Tomb, O. White, K. E. Nelson, K. A. Ketchum, R. J. Dodson, M. Gwinn, E. K. Hickey, J. D. Peterson, D. L. Richardson, A. R. Kerlavage, D. E. Graham, N. C. Kyrpides, R. D. Fleischmann, J. Quackenbush, N. H. Lee, G. G. Sutton, S. Gill, E. F. Kirkness, B. A. Dougherty, K. McKenney, M. D. Adams, B. Loftus, and J. C. Venter. 1997. The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus. Nature 390:364-370.
    • Klenk, H. P., R. A. Clayton, J. F. Tomb, O. White, K. E. Nelson, K. A. Ketchum, R. J. Dodson, M. Gwinn, E. K. Hickey, J. D. Peterson, D. L. Richardson, A. R. Kerlavage, D. E. Graham, N. C. Kyrpides, R. D. Fleischmann, J. Quackenbush, N. H. Lee, G. G. Sutton, S. Gill, E. F. Kirkness, B. A. Dougherty, K. McKenney, M. D. Adams, B. Loftus, and J. C. Venter. 1997. The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus. Nature 390:364-370.
  • 29
    • 0025061657 scopus 로고
    • Extremely thermostable amylolytic enzyme from the archaebacterium Pyrococcus furiosus
    • Koch, R., R. Zablowski, A. Spreinat, and G. Antranikian. 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, R.2    Spreinat, A.3    Antranikian, G.4
  • 30
    • 0034749172 scopus 로고    scopus 로고
    • 2 via a modified Embden-Meyerhof pathway and acetyl-CoA synthetase (ADP-forming)
    • 2 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
  • 31
    • 0038781007 scopus 로고    scopus 로고
    • ADP-dependent glucokinase from the hyperthermophilic sulfate-reducing archaeon Archaeoglobus fulgidus strain 7324
    • Labes, A., and P. Schönheit. 2003. ADP-dependent glucokinase from the hyperthermophilic sulfate-reducing archaeon Archaeoglobus fulgidus strain 7324. Arch. Microbiol. 180:69-75.
    • (2003) Arch. Microbiol , vol.180 , pp. 69-75
    • Labes, A.1    Schönheit, P.2
  • 32
    • 0027496724 scopus 로고
    • The purification and characterization of an extremely thermostable alpha-amylase from the hyperthermophilic archaebacterium Pyrococcus furiosus
    • Laderman, K. A., B. R. Davis, H. C. Krutzsch, M. S. Lewis, Y. V. Griko, P. L. Privalov, and C. B. Anlinsen. 1993. The purification and characterization of an extremely thermostable alpha-amylase from the hyperthermophilic archaebacterium Pyrococcus furiosus. J. Biol. Chem. 268:24394-24401.
    • (1993) J. Biol. Chem , vol.268 , pp. 24394-24401
    • Laderman, K.A.1    Davis, B.R.2    Krutzsch, H.C.3    Lewis, M.S.4    Griko, Y.V.5    Privalov, P.L.6    Anlinsen, C.B.7
  • 35
    • 33644520519 scopus 로고    scopus 로고
    • Liolios, K., N. Tavernarakis, P. Hugenholtz, and N. C. Kyrpides. 2006. The Genomes On Line Database (GOLD) v.2: a monitor of genome projects worldwide. Nucleic Acids Res. 34:D332-D334.
    • Liolios, K., N. Tavernarakis, P. Hugenholtz, and N. C. Kyrpides. 2006. The Genomes On Line Database (GOLD) v.2: a monitor of genome projects worldwide. Nucleic Acids Res. 34:D332-D334.
  • 36
    • 0347926551 scopus 로고    scopus 로고
    • The influence of cytosolic phosphoglucomutase on photosynthetic carbohydrate metabolism
    • Lytovchenko, A., L. Sweetlove, M. Pauly, and A. R. Fernie. 2002. The influence of cytosolic phosphoglucomutase on photosynthetic carbohydrate metabolism. Planta 215:1013-1021.
    • (2002) Planta , vol.215 , pp. 1013-1021
    • Lytovchenko, A.1    Sweetlove, L.2    Pauly, M.3    Fernie, A.R.4
  • 37
    • 0035831255 scopus 로고    scopus 로고
    • Relationship of sequence and structure to specificity in the α-amylase family of enzymes
    • MacGregor, E. A., S. Janecek, and B. Svensson. 2001. Relationship of sequence and structure to specificity in the α-amylase family of enzymes. Biochim. Biophys. Acta 1546:1-20.
    • (2001) Biochim. Biophys. Acta , vol.1546 , pp. 1-20
    • MacGregor, E.A.1    Janecek, S.2    Svensson, B.3
  • 38
    • 0016265063 scopus 로고
    • Regulation of glucosylation of teichoic acid. I. Isolation of phosphoglucomutase in Bacillus subtilis 168
    • Maino, V. C., and F. E. Young. 1974. Regulation of glucosylation of teichoic acid. I. Isolation of phosphoglucomutase in Bacillus subtilis 168. J. Biol. Chem. 249:5169-5175.
    • (1974) J. Biol. Chem , vol.249 , pp. 5169-5175
    • Maino, V.C.1    Young, F.E.2
  • 39
    • 0029900104 scopus 로고    scopus 로고
    • Purification and partial sequencing of high-affinity progesterone-binding site(s) from porcine liver membranes
    • Meyer, C., R. Schmid, P. C. Scriba, and M. Wehling. 1996. Purification and partial sequencing of high-affinity progesterone-binding site(s) from porcine liver membranes. Eur. J. Biochem. 239:726-731.
    • (1996) Eur. J. Biochem , vol.239 , pp. 726-731
    • Meyer, C.1    Schmid, R.2    Scriba, P.C.3    Wehling, M.4
  • 40
    • 33747333106 scopus 로고
    • Use of dinitrosalicylic acid reagent for determination of reducing sugar
    • Miller, G. L. 1959. Use of dinitrosalicylic acid reagent for determination of reducing sugar. Anal. Chem. 31:426.
    • (1959) Anal. Chem , vol.31 , pp. 426
    • Miller, G.L.1
  • 41
    • 0004696687 scopus 로고
    • Inhibition of phosphoglucomutase by trace metals
    • Milstein, C. 1961. Inhibition of phosphoglucomutase by trace metals. Biochem. J. 79:591-596.
    • (1961) Biochem. J , vol.79 , pp. 591-596
    • Milstein, C.1
  • 43
    • 0025117681 scopus 로고
    • 2 by Archaeoglobus fulgidus via the carbon monoxide dehydrogenase pathway: Demonstration of the acetyl-CoA carbon-carbon cleavage reaction in cell extracts
    • 2 by Archaeoglobus fulgidus via the carbon monoxide dehydrogenase pathway: demonstration of the acetyl-CoA carbon-carbon cleavage reaction in cell extracts. Arch. Microbiol. 153:215-218.
    • (1990) Arch. Microbiol , vol.153 , pp. 215-218
    • Möller-Zinkhan, D.1    Thauer, R.K.2
  • 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 P. Schönheit. 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
    • 0002193576 scopus 로고
    • Phosphoglucomutase from muscle
    • Academic Press, Inc, New York, NY
    • Najjar, V. A. 1955. Phosphoglucomutase from muscle, p. 294-299. In Methods in enzymology. Academic Press, Inc., New York, NY.
    • (1955) Methods in enzymology , pp. 294-299
    • Najjar, V.A.1
  • 46
    • 0035584063 scopus 로고    scopus 로고
    • Kinetic mechanism and pH dependence of the kinetic parameters of Pseudomonas aeruginosa phosphoman-nomutase/phosphoglucomutase
    • Naught, L. E., and P. A. Tipton. 2001. Kinetic mechanism and pH dependence of the kinetic parameters of Pseudomonas aeruginosa phosphoman-nomutase/phosphoglucomutase. Arch. Biochem. Biophys. 396:111-118.
    • (2001) Arch. Biochem. Biophys , vol.396 , pp. 111-118
    • Naught, L.E.1    Tipton, P.A.2
  • 48
    • 0032004274 scopus 로고    scopus 로고
    • 14C]maltose using amylomaltase, cyclodextrin glucosyltransferase and cyclodextrinase
    • 14C]maltose using amylomaltase, cyclodextrin glucosyltransferase and cyclodextrinase. Carbohydr. Res. 307:375-379.
    • (1998) Carbohydr. Res , vol.307 , pp. 375-379
    • Pajatsch, M.1    Bock, A.2    Boos, W.3
  • 49
    • 0021964124 scopus 로고
    • Evolution of catalytic and regulatory sites in phosphorylases
    • Palm, D., R. Goerl, and K. J. Burger. 1985. Evolution of catalytic and regulatory sites in phosphorylases. Nature 313:500-502.
    • (1985) Nature , vol.313 , pp. 500-502
    • Palm, D.1    Goerl, R.2    Burger, K.J.3
  • 50
    • 0034705064 scopus 로고    scopus 로고
    • Structure, specificity and function of cyclomaltodextrinase, a multispecific enzyme of the α-amylase family
    • Park, K. H., T. J. Kim, T. K. Cheong, J. W. Kim, B. H. Oh, and B. Svensson. 2000. Structure, specificity and function of cyclomaltodextrinase, a multispecific enzyme of the α-amylase family. Biochim. Biophys. Acta 1478:165-185.
    • (2000) Biochim. Biophys. Acta , vol.1478 , pp. 165-185
    • Park, K.H.1    Kim, T.J.2    Cheong, T.K.3    Kim, J.W.4    Oh, B.H.5    Svensson, B.6
  • 51
    • 0036181524 scopus 로고    scopus 로고
    • Characterization of an archaeal cyclodextrin glucanotransferase with a novel C-terminal domain
    • Rashid, N., J. Cornista, S. Ezaki, T. Fukui, H. Atomi, and T. Imanaka. 2002. Characterization of an archaeal cyclodextrin glucanotransferase with a novel C-terminal domain. J. Bacteriol. 184:777-784.
    • (2002) J. Bacteriol , vol.184 , pp. 777-784
    • Rashid, N.1    Cornista, J.2    Ezaki, S.3    Fukui, T.4    Atomi, H.5    Imanaka, T.6
  • 52
    • 4444268422 scopus 로고    scopus 로고
    • Among multiple phosphomannomutase gene orthologues, only one gene encodes a protein with phosphoglucomutase and phosphomannomutase activities in Thermococcus kodakaraensis
    • Rashid, N., T. Kanai, H. Atomi, and T. Imanaka. 2004. Among multiple phosphomannomutase gene orthologues, only one gene encodes a protein with phosphoglucomutase and phosphomannomutase activities in Thermococcus kodakaraensis. J. Bacteriol. 186:6070-6076.
    • (2004) J. Bacteriol , vol.186 , pp. 6070-6076
    • Rashid, N.1    Kanai, T.2    Atomi, H.3    Imanaka, T.4
  • 53
    • 0025348046 scopus 로고
    • Characterization of vanadate-based transition-state-analogue complexes of phosphoglucomutase by spectral and NMR techniques
    • Ray, W. J., Jr., J. W. Burgner, and C. B. Post. 1990. Characterization of vanadate-based transition-state-analogue complexes of phosphoglucomutase by spectral and NMR techniques. Biochemistry 29:2770-2778.
    • (1990) Biochemistry , vol.29 , pp. 2770-2778
    • Ray Jr., W.J.1    Burgner, J.W.2    Post, C.B.3
  • 54
    • 77956895189 scopus 로고    scopus 로고
    • Ray, W. J., Jr., and E. J. Peck, Jr. 1972. Phosphomutase, p. 407-477. In P. D. Boyer (ed.), The enzymes, VI. Academic Press, Inc., New York, NY.
    • Ray, W. J., Jr., and E. J. Peck, Jr. 1972. Phosphomutase, p. 407-477. In P. D. Boyer (ed.), The enzymes, vol. VI. Academic Press, Inc., New York, NY.
  • 55
    • 0025194947 scopus 로고
    • The oxyvanadium constellation in transition-state-analogue complexes of phosphoglucomutase and ribonuclease: Structural deductions from electron-transfer spectra
    • Ray, W. J., Jr., and C. B. Post. 1990. The oxyvanadium constellation in transition-state-analogue complexes of phosphoglucomutase and ribonuclease: structural deductions from electron-transfer spectra. Biochemistry 29:2779-2789.
    • (1990) Biochemistry , vol.29 , pp. 2779-2789
    • Ray Jr., W.J.1    Post, C.B.2
  • 56
    • 0025344523 scopus 로고
    • Characterization of a vanadate-based transition-state-analogue complex of phosphoglucomutase by kinetic and equilibrium binding studies: Mechanistic implications
    • Ray, W. J., Jr., and J. M. Puvathingal. 1990. Characterization of a vanadate-based transition-state-analogue complex of phosphoglucomutase by kinetic and equilibrium binding studies: mechanistic implications. Biochemistry 29:2790-2801.
    • (1990) Biochemistry , vol.29 , pp. 2790-2801
    • Ray Jr., W.J.1    Puvathingal, J.M.2
  • 57
    • 0001311609 scopus 로고
    • A kinetic study of the phosphoglucomutase pathway
    • Ray, W. J., Jr., and G. A. Roscelli. 1964. A kinetic study of the phosphoglucomutase pathway. J. Biol. Chem. 239:1228-1236.
    • (1964) J. Biol. Chem , vol.239 , pp. 1228-1236
    • Ray Jr., W.J.1    Roscelli, G.A.2
  • 58
    • 0014010755 scopus 로고
    • Activation and inhibition in the phosphoglucomutase system
    • Ray, W. J., Jr., and G. A. Roscelli. 1966. Activation and inhibition in the phosphoglucomutase system. J. Biol. Chem. 241:2596- 2602.
    • (1966) J. Biol. Chem , vol.241 , pp. 2596-2602
    • Ray Jr., W.J.1    Roscelli, G.A.2
  • 59
    • 0028859745 scopus 로고
    • Isolation and characterization of a heat-stable pullulanase from the hyperthermophilic archaeon Pyrococcus woesei after cloning and expression of its gene in Escherichia coli
    • Rüdiger, A., P. L. Jorgensen, and G. Antranikian. 1995. Isolation and characterization of a heat-stable pullulanase from the hyperthermophilic archaeon Pyrococcus woesei after cloning and expression of its gene in Escherichia coli. Appl. Environ. Microbiol. 61:567-575.
    • (1995) Appl. Environ. Microbiol , vol.61 , pp. 567-575
    • Rüdiger, A.1    Jorgensen, P.L.2    Antranikian, G.3
  • 60
    • 0032966504 scopus 로고    scopus 로고
    • Bacterial alpha-glucan phosphorylases
    • Schinzel, R., and B. Nidetzky. 1999. Bacterial alpha-glucan phosphorylases. FEMS Microbiol. Lett. 171:73-79.
    • (1999) FEMS Microbiol. Lett , vol.171 , pp. 73-79
    • Schinzel, R.1    Nidetzky, B.2
  • 61
    • 27844507018 scopus 로고    scopus 로고
    • Unusual pathways and enzymes of central carbohydrate metabolism in archaea
    • Siebers, B., and P. Schönheit. 2005. Unusual pathways and enzymes of central carbohydrate metabolism in archaea. Curr. Opin. Microbiol. 8:695-705.
    • (2005) Curr. Opin. Microbiol , vol.8 , pp. 695-705
    • Siebers, B.1    Schönheit, P.2
  • 62
    • 33746804854 scopus 로고
    • Archaeoglobus fulgidus gen. nov., sp. nov.: A new taxon of extremely thermophilic archaebacteria
    • Stetter, K. O. 1988. Archaeoglobus fulgidus gen. nov., sp. nov.: a new taxon of extremely thermophilic archaebacteria. Syst. Appl. Microbiol. 10:172-173.
    • (1988) Syst. Appl. Microbiol , vol.10 , pp. 172-173
    • Stetter, K.O.1
  • 64
    • 0023159558 scopus 로고
    • Isolation of extremely thermophilic sulfate reducers: Evidence for a novel branch of archaebacteria
    • Stetter, K. O., G. Lauerer, M. Thomm, and A. Neuner. 1987. Isolation of extremely thermophilic sulfate reducers: evidence for a novel branch of archaebacteria. Science 236:822-824.
    • (1987) Science , vol.236 , pp. 822-824
    • Stetter, K.O.1    Lauerer, G.2    Thomm, M.3    Neuner, A.4
  • 65
    • 0032899816 scopus 로고    scopus 로고
    • Purification and characterization of an extremely thermostable cyclomaltodextrin glucanotransferase from a newly isolated hyperthermophilic archaeon, a Thermococcus sp
    • Tachibana, Y., A. Kuramura, N. Shirasaka, Y. Suzuki, T. Yamamoto, S. Fujiwara, M. Takagi, and T. Imanaka. 1999. Purification and characterization of an extremely thermostable cyclomaltodextrin glucanotransferase from a newly isolated hyperthermophilic archaeon, a Thermococcus sp. Appl. Environ. Microbiol. 65:1991-1997.
    • (1999) Appl. Environ. Microbiol , vol.65 , pp. 1991-1997
    • Tachibana, Y.1    Kuramura, A.2    Shirasaka, N.3    Suzuki, Y.4    Yamamoto, T.5    Fujiwara, S.6    Takagi, M.7    Imanaka, T.8
  • 66
    • 0001890066 scopus 로고
    • Sulfate-reducing archaea
    • N. Clark ed, Plenum Publishing Company, Ltd, London, England
    • Thauer, R. K., and J. Kunow. 1995. Sulfate-reducing archaea, p. 33-48. In N. Clark (ed.), Biotechnology handbook. Plenum Publishing Company, Ltd., London, England.
    • (1995) Biotechnology handbook , pp. 33-48
    • Thauer, R.K.1    Kunow, J.2
  • 67
    • 5544280269 scopus 로고    scopus 로고
    • Characterization of a thermoalkali-stable cyclodextrin glycosyltransferase from the anaerobic thermoalkaliphilic bacterium Anaerobranca gottschalkii
    • Thiemann, V., C. Donges, S. G. Prowe, R. Sterner, and G. Antranikian. 2004. Characterization of a thermoalkali-stable cyclodextrin glycosyltransferase from the anaerobic thermoalkaliphilic bacterium Anaerobranca gottschalkii. Arch. Microbiol. 182:226-235.
    • (2004) Arch. Microbiol , vol.182 , pp. 226-235
    • Thiemann, V.1    Donges, C.2    Prowe, S.G.3    Sterner, R.4    Antranikian, G.5
  • 68
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL_X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson, J. D., T. J. Gibson, F. Plewniak, F. Jeanmougin, and D. G. Higgins. 1997. The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res. 25:4876-4882.
    • (1997) Nucleic Acids Res , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 69
    • 0032103189 scopus 로고    scopus 로고
    • Bacterial cyclodextrin glucanotransferase
    • Tonkova, A. 1998. Bacterial cyclodextrin glucanotransferase. Enzyme Microb. Technol. 22:678-686.
    • (1998) Enzyme Microb. Technol , vol.22 , pp. 678-686
    • Tonkova, A.1
  • 70
    • 31844451922 scopus 로고    scopus 로고
    • Two novel cyclodextrin-degrading enzymes isolated from thermophilic bacteria have similar domain structures but differ in oligomeric state and activity profile
    • Turner, P., A. Labes, O. H. Fridjonsson, G. O. Hreggvidson, P. Schönheit, J. K. Kristjansson, O. Hoist, and E. N. Karlsson. 2005. Two novel cyclodextrin-degrading enzymes isolated from thermophilic bacteria have similar domain structures but differ in oligomeric state and activity profile. J. Biosci. Bioeng. 100:380-390.
    • (2005) J. Biosci. Bioeng , vol.100 , pp. 380-390
    • Turner, P.1    Labes, A.2    Fridjonsson, O.H.3    Hreggvidson, G.O.4    Schönheit, P.5    Kristjansson, J.K.6    Hoist, O.7    Karlsson, E.N.8
  • 71
    • 0001515809 scopus 로고
    • The enzymatic oxidation of pyridoxine and pyridoxamine phosphates
    • Wada, H., and E. E. Snell. 1961. The enzymatic oxidation of pyridoxine and pyridoxamine phosphates. J. Biol. Chem. 236:2089-2095.
    • (1961) J. Biol. Chem , vol.236 , pp. 2089-2095
    • Wada, H.1    Snell, E.E.2
  • 72
    • 0033003021 scopus 로고    scopus 로고
    • Maltose metabolism in the hyperthermophilic archaeon Thermococcus litoralis: Purification and characterization of key enzymes
    • Xavier, K. B., R. Peist, M. Kossmann, W. Boos, and H. Santos. 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
  • 73
    • 30744439834 scopus 로고    scopus 로고
    • Enzymatic preparation of maltohexaose, maltoheptaose, and maltooctaose by the preferential cyclomaltooligosaccharide (cyclodextrin) ring-opening reaction of Pyrococcus furiosus thermostable amylase
    • Yang, S. J., H. S. Lee, J. W. Kim, M. H. Lee, J. H. Auh, B. H. Lee, and K. H. Park. 2006. Enzymatic preparation of maltohexaose, maltoheptaose, and maltooctaose by the preferential cyclomaltooligosaccharide (cyclodextrin) ring-opening reaction of Pyrococcus furiosus thermostable amylase. Carbohydr. Res. 341:420-424.
    • (2006) Carbohydr. Res , vol.341 , pp. 420-424
    • Yang, S.J.1    Lee, H.S.2    Kim, J.W.3    Lee, M.H.4    Auh, J.H.5    Lee, B.H.6    Park, K.H.7
  • 74
    • 0028123664 scopus 로고
    • Pathway of glycogen metabolism in Methanococcus maripaludis
    • Yu, J. P., J. Ladapo, and W. B. Whitman. 1994. Pathway of glycogen metabolism in Methanococcus maripaludis. J. Bacteriol. 176:325-332.
    • (1994) J. Bacteriol , vol.176 , pp. 325-332
    • Yu, J.P.1    Ladapo, J.2    Whitman, W.B.3
  • 75
    • 0000967346 scopus 로고
    • Desulfovibrio simplex sp. nov., a new sulfate-reducing bacteria from a sour whey digester
    • Zellner, G., P. Messner, H. Kneifel, and J. Winter. 1989. Desulfovibrio simplex sp. nov., a new sulfate-reducing bacteria from a sour whey digester. Arch. Microbiol. 152:329-334.
    • (1989) Arch. Microbiol , vol.152 , pp. 329-334
    • Zellner, G.1    Messner, P.2    Kneifel, H.3    Winter, J.4


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