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Volumn 272, Issue 4, 2005, Pages 1054-1062

Properties of the recombinant glucose/galactose dehydrogenase from the extreme thermoacidophile, Picrophilus torridus

Author keywords

Acidophile; Archaea; Entner Doudoroff pathway; Glucose dehydrogenase

Indexed keywords

GALACTOSE DEHYDROGENASE; GLUCOSE DEHYDROGENASE; NICOTINAMIDE ADENINE DINUCLEOTIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; RECOMBINANT ENZYME; ZINC;

EID: 14044272040     PISSN: 1742464X     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2004.04539.x     Document Type: Article
Times cited : (30)

References (21)
  • 1
    • 0028806517 scopus 로고
    • Picrophilus general nov., fam. nov. A novel aerobic, heterotrophic, thermoacidophilic genus and family comprising archaea capable of growth around pH 0
    • Schleper C, Puehler G, Holz I, Gambacorta A, Janekovic D, Santarius U, Klenk HP & Zillig W (1995) Picrophilus general nov., fam. nov. a novel aerobic, heterotrophic, thermoacidophilic genus and family comprising archaea capable of growth around pH 0. J Bacteriol 177, 7050-7059.
    • (1995) J Bacteriol , vol.177 , pp. 7050-7059
    • Schleper, C.1    Puehler, G.2    Holz, I.3    Gambacorta, A.4    Janekovic, D.5    Santarius, U.6    Klenk, H.P.7    Zillig, W.8
  • 2
    • 0032076479 scopus 로고    scopus 로고
    • Bioenergetics and cytoplasmic membrane stability of the extremely acidophilic, thermophilic archaeon Picrophilus oshimae
    • van Driessen AJ, Zillig W & Konings WN (1998) Bioenergetics and cytoplasmic membrane stability of the extremely acidophilic, thermophilic archaeon Picrophilus oshimae. Extremophiles 2, 67-74.
    • (1998) Extremophiles , vol.2 , pp. 67-74
    • Driessen, A.J.1    Zillig, W.2    Konings, W.N.3
  • 3
    • 0033215210 scopus 로고    scopus 로고
    • Pathway alignment: Application to the comparative analysis of glycolytic enzymes
    • Dandekar T, Schuster S, Snel B, Huynen M & 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
  • 4
    • 0021696802 scopus 로고
    • Glucose metabolism in the extreme thermoacidophilic archaebacterium Sulfolobus solfataricus
    • De Rosa M, Gambacorta A, Nicolaus B, Giardina P, Poerio E & 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
  • 5
    • 0024604672 scopus 로고
    • Central metabolism of the archaebacteria: An overview
    • Danson MJ (1989) Central metabolism of the archaebacteria: an overview. Can J Microbiol 35, 58-64.
    • (1989) Can J Microbiol , vol.35 , pp. 58-64
    • Danson, M.J.1
  • 7
    • 0016345760 scopus 로고
    • Chemical and biological evolution of nucleotide-binding protein
    • Rossmann MG, Moras D & Olsen KW (1974) Chemical and biological evolution of nucleotide-binding protein. Nature 250, 194-199.
    • (1974) Nature , vol.250 , pp. 194-199
    • Rossmann, M.G.1    Moras, D.2    Olsen, K.W.3
  • 8
    • 0028773470 scopus 로고
    • The crystal structure of glucose dehydrogenase from Thermoplasma acidophilum
    • John J, Crennell SJ, Hough DW, Danson MJ & Taylor GL (1994) The crystal structure of glucose dehydrogenase from Thermoplasma acidophilum. Structure 2, 385-393.
    • (1994) Structure , vol.2 , pp. 385-393
    • John, J.1    Crennell, S.J.2    Hough, D.W.3    Danson, M.J.4    Taylor, G.L.5
  • 9
    • 0026675661 scopus 로고
    • Importance of the structural zinc atom for the stability of yeast alcohol dehydrogenase
    • Magonet E, Hayen P, Delforge D, Delaive E & Remacle J (1992) Importance of the structural zinc atom for the stability of yeast alcohol dehydrogenase. Biochem J 287, 361-365.
    • (1992) Biochem J , vol.287 , pp. 361-365
    • Magonet, E.1    Hayen, P.2    Delforge, D.3    Delaive, E.4    Remacle, J.5
  • 11
    • 0029921869 scopus 로고    scopus 로고
    • Structural and sequence comparisons of quinone oxidoreductase, zeta-crystallin, and glucose and alcohol dehydrogenases
    • Edwards KJ, Barton JD, Rossjohn J, Thorn JM, Taylor GL & Ollis DL (1996) Structural and sequence comparisons of quinone oxidoreductase, zeta-crystallin, and glucose and alcohol dehydrogenases. Arch Biochem Biophys 328, 173-183.
    • (1996) Arch Biochem Biophys , vol.328 , pp. 173-183
    • Edwards, K.J.1    Barton, J.D.2    Rossjohn, J.3    Thorn, J.M.4    Taylor, G.L.5    Ollis, D.L.6
  • 12
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels
    • Shevchenko A, Wilm M, Vorm O & Mann M (1996) Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels. Anal Chem 68, 850-858.
    • (1996) Anal Chem , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 13
    • 0022893844 scopus 로고
    • Stability of NADPH: Effect of various factors on the kinetics of degradation
    • Wu JT, Wu LH & Knight JA (1986) Stability of NADPH: effect of various factors on the kinetics of degradation. Clin Chem 32, 314-319.
    • (1986) Clin Chem , vol.32 , pp. 314-319
    • Wu, J.T.1    Wu, L.H.2    Knight, J.A.3
  • 14
    • 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 VF & 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
  • 15
    • 12144290887 scopus 로고    scopus 로고
    • Reconstruction of the central carbohydrate metabolism of Thermoproteus tenax by use of genomic and biochemical data
    • Siebers B, Tjaden B, Michalke K et al. (2004) Reconstruction of the central carbohydrate metabolism of Thermoproteus tenax by use of genomic and biochemical data. J Bacteriol 186, 2179-2194.
    • (2004) J Bacteriol , vol.186 , pp. 2179-2194
    • Siebers, B.1    Tjaden, B.2    Michalke, K.3
  • 16
    • 0032878235 scopus 로고    scopus 로고
    • High level expression of Thermococcus litoralis 4-alpha- glucanotransferase in a soluble form in Escherichia coli with a novel expression system involving minor arginine tRNAs and GroELS
    • Imamura H, Jeon B, Wakagi T & Matsuzawa H (1999) High level expression of Thermococcus litoralis 4-alpha-glucanotransferase in a soluble form in Escherichia coli with a novel expression system involving minor arginine tRNAs and GroELS. FEBS Lett 457, 393-396.
    • (1999) FEBS Lett , vol.457 , pp. 393-396
    • Imamura, H.1    Jeon, B.2    Wakagi, T.3    Matsuzawa, H.4
  • 17
    • 0141483333 scopus 로고    scopus 로고
    • Metabolic pathway promiscuity in the archaeon Sulfolobus solfataricus revealed by studies on glucose dehydrogenase and 2-keto-3-deoxygluconate aldolase
    • Lamble HJ, Heyer NI, Bull SD, Hough DW & Danson MJ (2003) Metabolic pathway promiscuity in the archaeon Sulfolobus solfataricus revealed by studies on glucose dehydrogenase and 2-keto-3-deoxygluconate aldolase. J Biol Chem 278, 34066-34072.
    • (2003) J Biol Chem , vol.278 , pp. 34066-34072
    • Lamble, H.J.1    Heyer, N.I.2    Bull, S.D.3    Hough, D.W.4    Danson, M.J.5
  • 18
    • 0022839871 scopus 로고
    • Glucose dehydrogenase from the thermoacidophilic archaebacterium Sulfolobus solfataricus
    • Giardina P, de Biasi MG, de Rosa M, Gambacorta A & 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
  • 19
    • 0024709804 scopus 로고
    • Purification and characterization of glucose dehydrogenase from the thermoacidophilic archaebacterium Thermoplasma acidophilum
    • Smith LD, Budgen N, Bungard SJ, Danson MJ & Hough DW (1989) Purification and characterization of glucose dehydrogenase from the thermoacidophilic archaebacterium Thermoplasma acidophilum. Biochem J 261, 973-977.
    • (1989) Biochem J , vol.261 , pp. 973-977
    • Smith, L.D.1    Budgen, N.2    Bungard, S.J.3    Danson, M.J.4    Hough, D.W.5
  • 20
    • 0020482968 scopus 로고
    • Bovine liver glucose dehydrogenase: Isolation and characterization
    • Campbell DP, Carper WR & Thompson RE (1982) Bovine liver glucose dehydrogenase: isolation and characterization. Arch Biochem Biophys 215, 289-301.
    • (1982) Arch Biochem Biophys , vol.215 , pp. 289-301
    • Campbell, D.P.1    Carper, W.R.2    Thompson, R.E.3
  • 21
    • 0033229936 scopus 로고    scopus 로고
    • An extremely thermostable aldolase from Sulfolobus solfataricus with specificity for non-phosphorylated substrates
    • Buchanan CL, Connaris H, Danson MJ, Reeve CD & Hough DW (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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.