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Volumn 64, Issue 7, 1998, Pages 2357-2360

Thermotoga neapolitana homotetrameric xylose isomerase is expressed as a catalytically active and thermostable dimer in Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

RECOMBINANT ENZYME; TETRAMER; XYLOSE ISOMERASE;

EID: 0031814109     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/aem.64.7.2357-2360.1998     Document Type: Article
Times cited : (25)

References (30)
  • 1
    • 0344343192 scopus 로고
    • Biocatalysis near and above 100°C by sulfur-dependent extremely thermophilic organisms
    • M. W. W. Adams and R. M. Kelly (ed.), Biocatalysis at extreme temperatures. American Chemical Society, Washington, D.C.
    • Adams, M. W. W., J. B. Park, S. Mukund, J. Blamey, and R. M. Kelly. 1992. Biocatalysis near and above 100°C by sulfur-dependent extremely thermophilic organisms, p. 4-22. In M. W. W. Adams and R. M. Kelly (ed.), Biocatalysis at extreme temperatures. ACS Symposium Series no. 498. American Chemical Society, Washington, D.C.
    • (1992) ACS Symposium Series No. 498 , pp. 4-22
    • Adams, M.W.W.1    Park, J.B.2    Mukund, S.3    Blamey, J.4    Kelly, R.M.5
  • 2
    • 0029055215 scopus 로고
    • Extremozymes: Expanding the limits of biocatalysis
    • Adams, M. W. W., F. B. Perler, and R. M. Kelly. 1995. Extremozymes: expanding the limits of biocatalysis. Bio/Technology 13:662-668.
    • (1995) Bio/Technology , vol.13 , pp. 662-668
    • Adams, M.W.W.1    Perler, F.B.2    Kelly, R.M.3
  • 3
    • 0025017683 scopus 로고
    • Identification of essential histidine residues in the active site of Escherichia coli xylose (glucose) isomerase
    • Batt, C. A., A. C. Jamieson, and M. A. Vandeyar. 1990. Identification of essential histidine residues in the active site of Escherichia coli xylose (glucose) isomerase. Proc. Natl. Acad. Sci. USA 87:618-622.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 618-622
    • Batt, C.A.1    Jamieson, A.C.2    Vandeyar, M.A.3
  • 4
    • 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
  • 5
    • 0027587611 scopus 로고
    • Purification and characterization of a highly thermostable glucose isomerase produced by the extremely thermophilic eubacterium Thermotoga maritima
    • Brown, S. H., C. Sjoholm, and R. M. Kelly. 1993. Purification and characterization of a highly thermostable glucose isomerase produced by the extremely thermophilic eubacterium Thermotoga maritima. Biotechnol. Bioeng. 41:878-886.
    • (1993) Biotechnol. Bioeng. , vol.41 , pp. 878-886
    • Brown, S.H.1    Sjoholm, C.2    Kelly, R.M.3
  • 6
    • 0001304049 scopus 로고
    • X-ray analysis of D-xylose isomerase at 1.9 Å: Native enzyme in complex with substrate and with a mechanism-designed inactivator
    • Carrell, J. P., V. Glusker, F. Berger, D. Tritsch, and J. P. Biellman. 1989. X-ray analysis of D-xylose isomerase at 1.9 Å: native enzyme in complex with substrate and with a mechanism-designed inactivator. Proc. Natl. Acad. Sci. USA 86:4440-4444.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 4440-4444
    • Carrell, J.P.1    Glusker, V.2    Berger, F.3    Tritsch, D.4    Biellman, J.P.5
  • 7
    • 0028070761 scopus 로고
    • Perturbing the metal site in D-xylose isomerase. Effect of mutations of His-220 on enzyme stability
    • Cha, J., Y. Cho, R. D. Whitaker, H. L. Carrell, J. P. Glusker, P. A. Karplus, and C. A. Batt. 1994. Perturbing the metal site in D-xylose isomerase. Effect of mutations of His-220 on enzyme stability. J. Biol. Chem. 269:2687-2694.
    • (1994) J. Biol. Chem. , vol.269 , pp. 2687-2694
    • Cha, J.1    Cho, Y.2    Whitaker, R.D.3    Carrell, H.L.4    Glusker, J.P.5    Karplus, P.A.6    Batt, C.A.7
  • 8
    • 0029822814 scopus 로고    scopus 로고
    • Tetrameric and octameric lactate dehydrogenase from the hyperthermophilic bacterium Thermotoga maritima
    • Dams, T., R. Ostendorp, M. Ott, K. Rutkat, and R. Jaenicke. 1996. Tetrameric and octameric lactate dehydrogenase from the hyperthermophilic bacterium Thermotoga maritima. Eur. J. Biochem. 240:274-279.
    • (1996) Eur. J. Biochem. , vol.240 , pp. 274-279
    • Dams, T.1    Ostendorp, R.2    Ott, M.3    Rutkat, K.4    Jaenicke, R.5
  • 9
    • 0000795089 scopus 로고
    • Refinement of glucose isomerase from Streptomyces albus at 1.65 Å with data from an imaging plate
    • Dauter, Z., H. Terry, H. Witzel, and K. S. Wilson. 1990. Refinement of glucose isomerase from Streptomyces albus at 1.65 Å with data from an imaging plate. Acta Crystallogr. Sect. B 46:833-841.
    • (1990) Acta Crystallogr. Sect. B , vol.46 , pp. 833-841
    • Dauter, Z.1    Terry, H.2    Witzel, H.3    Wilson, K.S.4
  • 10
    • 0025765288 scopus 로고
    • Xylose (glucose) isomerase gene from the thermophile Thermus thermophilus: Cloning, sequencing, and comparison with other thermostable xylose isomerases
    • Dekker, K. A., H. Yagamata, K. Sakaguchi, and S. Udaka. 1991. Xylose (glucose) isomerase gene from the thermophile Thermus thermophilus: cloning, sequencing, and comparison with other thermostable xylose isomerases. J. Bacteriol. 173:3078-3083.
    • (1991) J. Bacteriol. , vol.173 , pp. 3078-3083
    • Dekker, K.A.1    Yagamata, H.2    Sakaguchi, K.3    Udaka, S.4
  • 11
    • 0023530081 scopus 로고
    • The 3 Å crystal structure of xylose isomerase from Streptomyces olivochromogenes
    • Farber, G. K., G. A. Petsko, and D. Ringe. 1987. The 3 Å crystal structure of xylose isomerase from Streptomyces olivochromogenes. Protein Eng. 1:459-466.
    • (1987) Protein Eng. , vol.1 , pp. 459-466
    • Farber, G.K.1    Petsko, G.A.2    Ringe, D.3
  • 12
    • 0024362334 scopus 로고
    • Structures of D-xylose isomerase from Arthrobacter strain B3728 containing the inhibitors xylitol and D-sorbitol at 2.5 Å and 2.3 Å resolution, respectively
    • Henrik, K., C. A. Collyer, and D. M. Blow. 1989. Structures of D-xylose isomerase from Arthrobacter strain B3728 containing the inhibitors xylitol and D-sorbitol at 2.5 Å and 2.3 Å resolution, respectively. J. Mol. Biol. 208:129-147.
    • (1989) J. Mol. Biol. , vol.208 , pp. 129-147
    • Henrik, K.1    Collyer, C.A.2    Blow, D.M.3
  • 13
    • 0028849606 scopus 로고
    • Dimeric 3-phosphoglycerate kinases from hyperthermophilic Archaea
    • Hess, D., K. Kruger, A. Knappik, P. Palm, and R. Hensel. 1995. Dimeric 3-phosphoglycerate kinases from hyperthermophilic Archaea. Eur. J. Biochem. 233:227-237.
    • (1995) Eur. J. Biochem. , vol.233 , pp. 227-237
    • Hess, D.1    Kruger, K.2    Knappik, A.3    Palm, P.4    Hensel, R.5
  • 15
    • 0013647027 scopus 로고
    • Characterization of enzymes from high temperature bacteria
    • M. W. W. Adams and R. M. Kelly (ed.), Biocatalysis at extreme temperatures. American Chemical Society, Washington, D.C.
    • Kelly, R. M., S. H. Brown, I. I. Blumentals, and M. W. W. Adams. 1992. Characterization of enzymes from high temperature bacteria, p. 23-41. In M. W. W. Adams and R. M. Kelly (ed.), Biocatalysis at extreme temperatures. ACS Symposium Series no. 498. American Chemical Society, Washington, D.C.
    • (1992) ACS Symposium Series No. 498 , pp. 23-41
    • Kelly, R.M.1    Brown, S.H.2    Blumentals, I.I.3    Adams, M.W.W.4
  • 16
    • 0029936794 scopus 로고    scopus 로고
    • Protein purification, and cloning and characterization of the cDNA and gene for xylose isomerase of barley
    • Kristo, P., R. Saarelainen, R. Fagerstrom, S. Aho, and M. Korhola. 1996. Protein purification, and cloning and characterization of the cDNA and gene for xylose isomerase of barley. Eur. J. Biochem. 237:240-246.
    • (1996) Eur. J. Biochem. , vol.237 , pp. 240-246
    • Kristo, P.1    Saarelainen, R.2    Fagerstrom, R.3    Aho, S.4    Korhola, M.5
  • 17
    • 14744299296 scopus 로고
    • Thermal stabilization of xylose isomerase from Thermoanaerobacterium thermosulfurigenes
    • Meng, M., M. Bagdasarian, and J. G. Zeikus. 1993. Thermal stabilization of xylose isomerase from Thermoanaerobacterium thermosulfurigenes. Bio/Technology 11:1157-1161.
    • (1993) Bio/Technology , vol.11 , pp. 1157-1161
    • Meng, M.1    Bagdasarian, M.2    Zeikus, J.G.3
  • 18
    • 0000585947 scopus 로고
    • Industrial aspects of immobilized glucose isomerase
    • T. Kobayeashi, A. Tanaka, and T. Tosa (ed.), Marcel Dekker Inc., New York, N.Y.
    • Pedersen, S. 1993. Industrial aspects of immobilized glucose isomerase, p. 185-208. In T. Kobayeashi, A. Tanaka, and T. Tosa (ed.), Industrial applications of immobilized biocatalysts. Marcel Dekker Inc., New York, N.Y.
    • (1993) Industrial Applications of Immobilized Biocatalysts , pp. 185-208
    • Pedersen, S.1
  • 19
    • 0026760851 scopus 로고
    • Stability of Arthrobacter D-xylose isomerase to denaturants and heat
    • Rangarajan, M., B. Asboth, and B. S. Hartley. 1992. Stability of Arthrobacter D-xylose isomerase to denaturants and heat. Biochem. J. 285:889-898.
    • (1992) Biochem. J. , vol.285 , pp. 889-898
    • Rangarajan, M.1    Asboth, B.2    Hartley, B.S.3
  • 20
    • 0028119786 scopus 로고
    • Structure determination of glucose isomerase from Streptomyces murinus at 2.6 Å resolution
    • Rasmussen, H., T. L. Cour, J. Nyborg, and M. Schulein. 1994. Structure determination of glucose isomerase from Streptomyces murinus at 2.6 Å resolution. Acta Crystallogr. Sect. D 50:124-131.
    • (1994) Acta Crystallogr. Sect. D , vol.50 , pp. 124-131
    • Rasmussen, H.1    Cour, T.L.2    Nyborg, J.3    Schulein, M.4
  • 22
    • 0029959528 scopus 로고    scopus 로고
    • Growth physiology of the hyperthermophilic archaeon Thermococcus litoralis: Development of a sulfur-free defined medium, characterization of an exopolysaccharide, and evidence of biofilm formation
    • Rinker, K. D., and R. M. Kelly. 1996. Growth physiology of the hyperthermophilic archaeon Thermococcus litoralis: development of a sulfur-free defined medium, characterization of an exopolysaccharide, and evidence of biofilm formation. Appl. Environ. Microbiol. 62:4478-4485.
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 4478-4485
    • Rinker, K.D.1    Kelly, R.M.2
  • 24
    • 0028912631 scopus 로고
    • Octameric enolase from the hyperthermophilic bacterium T. maritima: Purification, characterization, and image processing
    • Schurig, H., K. Rutkat, R. Rachel, and R. Jaenicke. 1995. Octameric enolase from the hyperthermophilic bacterium T. maritima: purification, characterization, and image processing. Protein Sci. 4:228-236.
    • (1995) Protein Sci. , vol.4 , pp. 228-236
    • Schurig, H.1    Rutkat, K.2    Rachel, R.3    Jaenicke, R.4
  • 25
    • 84989039101 scopus 로고
    • Towards a new generation of glucose isomerases through genetic engineering
    • Sicard, P. J., J.-B. Leleu, and G. Tiraby. 1990. Towards a new generation of glucose isomerases through genetic engineering. Starke 42:23-27.
    • (1990) Starke , vol.42 , pp. 23-27
    • Sicard, P.J.1    Leleu, J.-B.2    Tiraby, G.3
  • 27
    • 0344781708 scopus 로고    scopus 로고
    • Unpublished results
    • 26a. Tchernajenko, V. Unpublished results.
    • Tchernajenko, V.1
  • 29
    • 0029018981 scopus 로고
    • XylA cloning and sequencing, and biochemical characterization of xylose isomerase from Thermotoga neapolitana
    • Vieille, C., J. M. Hess, R. M. Kelly, and J. G. Zeikus. 1995. xylA cloning and sequencing, and biochemical characterization of xylose isomerase from Thermotoga neapolitana. Appl. Environ. Microbiol. 61:1867-1875.
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 1867-1875
    • Vieille, C.1    Hess, J.M.2    Kelly, R.M.3    Zeikus, J.G.4
  • 30
    • 0025974544 scopus 로고
    • A metal-mediated hydride shift mechanism for xylose isomerase based on the 1.6 Å Streptomyces rubiginosus structures with xylitol and D-xylose
    • Whitlow, M., A. J. Howard, B. C. Finzel, T. L. Poulos, E. Winborne, and G. L. Gilliland. 1991. A metal-mediated hydride shift mechanism for xylose isomerase based on the 1.6 Å Streptomyces rubiginosus structures with xylitol and D-xylose. Proteins Struct. Funct. Genet. 9:153-173.
    • (1991) Proteins Struct. Funct. Genet. , vol.9 , pp. 153-173
    • Whitlow, M.1    Howard, A.J.2    Finzel, B.C.3    Poulos, T.L.4    Winborne, E.5    Gilliland, G.L.6


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