메뉴 건너뛰기




Volumn 31, Issue 6, 1998, Pages 600-603

A thermostable xylose isomerase from Thermus thermophilus: Biochemical characterization, crystallization, and preliminary x-ray analyses

Author keywords

Crystallization; Thermostable enzyme; Thermus thermopilus; Xylose isomerase

Indexed keywords


EID: 3042882508     PISSN: 12258687     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (3)

References (22)
  • 1
    • 0028953745 scopus 로고
    • Design, synthesis, and characterization of a potent xylose isomerase inhibitor, D-threonohydroxamic acid, and high-resolution X-ray crystallographic structure of the enzyme-inhibitor complex
    • Allen, K. N., Lavic, A., Petsko, G. A. and Ringe, D. (1995) Design, synthesis, and characterization of a potent xylose isomerase inhibitor, D-threonohydroxamic acid, and high-resolution X-ray crystallographic structure of the enzyme-inhibitor complex. Biochemistry 34, 3742-3749.
    • (1995) Biochemistry , vol.34 , pp. 3742-3749
    • Allen, K.N.1    Lavic, A.2    Petsko, G.A.3    Ringe, D.4
  • 2
    • 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, H. L., Glusker, J. P., Burger, V., Manfre, F., Tritsch, D. and Biellmann, J.-F. (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, H.L.1    Glusker, J.P.2    Burger, V.3    Manfre, F.4    Tritsch, D.5    Biellmann, J.-F.6
  • 3
    • 0021344650 scopus 로고
    • X-ray crystal structure of D-xylose isomerase at 4 Å resolution
    • Carrell, H. L., Rubin, B. H., Hurley, T. J. and Glusker, J. P. (1984) X-ray crystal structure of D-xylose isomerase at 4 Å resolution. J. Biol. Chem. 259, 3230-3236.
    • (1984) J. Biol. Chem. , vol.259 , pp. 3230-3236
    • Carrell, H.L.1    Rubin, B.H.2    Hurley, T.J.3    Glusker, J.P.4
  • 5
    • 0030933753 scopus 로고    scopus 로고
    • Crystallization and initial X-ray analysis of xylose isomerase from Thermotoga neapolitana
    • Chayen, N. E., Conti, E., Vieille, C. and Zeikus, J. G. (1997) Crystallization and initial X-ray analysis of xylose isomerase from Thermotoga neapolitana. Acta Crystallogr. D53, 229-230.
    • (1997) Acta Crystallogr. , vol.D53 , pp. 229-230
    • Chayen, N.E.1    Conti, E.2    Vieille, C.3    Zeikus, J.G.4
  • 6
    • 0000795089 scopus 로고
    • Refinement of glucose isomerase from Streptomyces albus at 1.65 Å with data from an imaging plate
    • Dauter, Z., Terry, H., Witzel, H. and Wilson, K. S. (1990) Refinement of glucose isomerase from Streptomyces albus at 1.65 Å with data from an imaging plate. Acta Crystallogr. B46, 833-841.
    • (1990) Acta Crystallogr. , vol.B46 , pp. 833-841
    • Dauter, Z.1    Terry, H.2    Witzel, H.3    Wilson, K.S.4
  • 7
    • 0025765288 scopus 로고
    • Xylose (Glucose) isomerase gene from the thermophile Thermus thermophilus: Cloning, sequencing, and comparison with other thermostable xylose isomerases
    • Dekker, K., Yamagata, H., Sakaguchi, K. and Udaka, S. (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.1    Yamagata, H.2    Sakaguchi, K.3    Udaka, S.4
  • 8
    • 0024962364 scopus 로고
    • Crystallographic studies of the mechanism of xylose isomerase
    • Farber, G. K., Glafeld, A., Tiraby, G., Ringe, D. and Petsko, G. A. (1989) Crystallographic studies of the mechanism of xylose isomerase. Biochemistry 28, 7289-7297.
    • (1989) Biochemistry , vol.28 , pp. 7289-7297
    • Farber, G.K.1    Glafeld, A.2    Tiraby, G.3    Ringe, D.4    Petsko, G.A.5
  • 9
    • 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
    • Henrick, K., Collyer, C. A. and Blow, D. M. (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, 129-157.
    • (1989) J. Mol. Biol. , vol.208 , pp. 129-157
    • Henrick, K.1    Collyer, C.A.2    Blow, D.M.3
  • 10
    • 0026206788 scopus 로고
    • Sparse matrix sampling: A screening method for crystallization of proteins
    • Jancarik, J. and Kim, S.-H. (1991) Sparse matrix sampling: A screening method for crystallization of proteins. J. Appl. Crystallogr. 24, 409-411.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 409-411
    • Jancarik, J.1    Kim, S.-H.2
  • 11
    • 0028225131 scopus 로고
    • X-ray crystallographic structures of D-xylose isomerase-substrate complexes position the substrate and provide evidence for metal movement during catalysis
    • Lavie, A., Allen, K. N., Petsko, G. A. and Ringe, D. (1994) X-ray crystallographic structures of D-xylose isomerase-substrate complexes position the substrate and provide evidence for metal movement during catalysis. Biochemistry 33, 5469-5480.
    • (1994) Biochemistry , vol.33 , pp. 5469-5480
    • Lavie, A.1    Allen, K.N.2    Petsko, G.A.3    Ringe, D.4
  • 12
    • 0028170334 scopus 로고
    • Crystallization and preliminary X-ray diffraction studies of xylose isomerase from Thermoanaerobacterium thermosulfurigenes strain 4B
    • Lloyd, L. F., Gallay, O. S., Akins, J. and Zeikus, J. G. (1994) Crystallization and preliminary X-ray diffraction studies of xylose isomerase from Thermoanaerobacterium thermosulfurigenes strain 4B. J. Mol. Biol. 240, 504-506.
    • (1994) J. Mol. Biol. , vol.240 , pp. 504-506
    • Lloyd, L.F.1    Gallay, O.S.2    Akins, J.3    Zeikus, J.G.4
  • 13
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • Matthews, B. W. (1968) Solvent content of protein crystals. J. Mol. Biol. 33, 491-497.
    • (1968) J. Mol. Biol. , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 14
    • 0025765854 scopus 로고
    • Switching substrate preference of thermophilic xylose isomerase from D-xylose to D-glucose by redesigning the substrate binding pocket
    • Meng, M., Lee, C., Bagdasarian, M. and Ziekus, J. G. (1991) Switching substrate preference of thermophilic xylose isomerase from D-xylose to D-glucose by redesigning the substrate binding pocket. Proc. Natl. Acad. Sci. USA 88, 4015-4019.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 4015-4019
    • Meng, M.1    Lee, C.2    Bagdasarian, M.3    Ziekus, J.G.4
  • 16
    • 0026603050 scopus 로고
    • Mechanism of D-fructose isomerization by Arthrobacter D-xylose isomerase
    • Rangarajan, M. and Hartley, B. S. (1992) Mechanism of D-fructose isomerization by Arthrobacter D-xylose isomerase. Biochem. J. 283, 223-233.
    • (1992) Biochem. J. , vol.283 , pp. 223-233
    • Rangarajan, M.1    Hartley, B.S.2
  • 17
    • 0028119786 scopus 로고
    • Structure determination of glucose isomerase from Streptomyces murinus at 2.6 Å resolution
    • Rasmussen, H., la Cour, T., Nyborg, J and Schülein, M. (1994) Structure determination of glucose isomerase from Streptomyces murinus at 2.6 Å resolution. Acta Crystallogr. D50, 124-131.
    • (1994) Acta Crystallogr. , vol.D50 , pp. 124-131
    • Rasmussen, H.1    La Cour, T.2    Nyborg, J.3    Schülein, M.4
  • 19
    • 0000293676 scopus 로고
    • A focusing Weissenberg camera with multilayer-screens for macromolecular crystallography
    • Sakabe, N. (1991). A focusing Weissenberg camera with multilayer-screens for macromolecular crystallography. Nucl. Instr. Meth. A303, 448-463.
    • (1991) Nucl. Instr. Meth. , vol.A303 , pp. 448-463
    • Sakabe, N.1
  • 21
    • 0025974544 scopus 로고
    • A metal-mediated hydride shift mechanism for xylose isomerase based on the 1.6 Å Streptomyces rubigiosus structures with xylitol and D-xylose
    • Whitlow, M., Howard, A. J., Finzel, B. C., Poulos, T. L., Winborne, E. and Gilliland, G. L. (1991) A metal-mediated hydride shift mechanism for xylose isomerase based on the 1.6 Å Streptomyces rubigiosus structures with xylitol and D-xylose. Proteins 9, 153-173.
    • (1991) Proteins , 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
  • 22
    • 77957202280 scopus 로고    scopus 로고
    • Molecular determinants of thermozyme activity and stability: Analysis of xylose isomerase and amylopullulanase
    • Enzymes for Carbohydrate Engineering, Park, K. H., Robyt, J. F. and Choi, Y.-D. (eds), Elsevier Science B. V., Amsterdam, The Netherlands
    • Zeikus, J. G. (1996). Molecular determinants of thermozyme activity and stability: Analysis of xylose isomerase and amylopullulanase; in Enzymes for Carbohydrate Engineering, Park, K. H., Robyt, J. F. and Choi, Y.-D. (eds), Progress in Biotechnology Vol 12, pp. 145-161, Elsevier Science B. V., Amsterdam, The Netherlands.
    • (1996) Progress in Biotechnology , vol.12 , pp. 145-161
    • Zeikus, J.G.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.