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Volumn 78, Issue 2, 2010, Pages 496-500

Structure of hyperthermophilie endocellulase from Pyrococcus horikoshii

Author keywords

Active site; Cellulase; Endoglucanase; Hyperthermophile; Pyrococcus horikoshii

Indexed keywords

CELLULASE;

EID: 77449087500     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.22602     Document Type: Article
Times cited : (30)

References (24)
  • 1
    • 50049107012 scopus 로고    scopus 로고
    • Significant contribution of Archaea to extant biomass in marine subsurface sediments
    • Lipp JS, Morono Y, Inagaki F, Hinrichs KU. Significant contribution of Archaea to extant biomass in marine subsurface sediments. Nature 2008;454:991-994.
    • (2008) Nature , vol.454 , pp. 991-994
    • Lipp, J.S.1    Morono, Y.2    Inagaki, F.3    Hinrichs, K.U.4
  • 3
    • 0032590072 scopus 로고    scopus 로고
    • An endoglucanase. Egl A, from the hyperthermophilic archaeon Pyrococcus furiosus hydrolyzes beta-1,4 bonds in mixed-linkage (1>3),(1->4)-beta-D- glucans and cellulose
    • Bauer MW, Driskill LE, Callen W, Snead MA, Mathur EJ, Kelly RM. An endoglucanase. Egl A, from the hyperthermophilic archaeon Pyrococcus furiosus hydrolyzes beta-1,4 bonds in mixed-linkage (1>3),(1->4)-beta-D-glucans and cellulose. J Bacteriol 1999;181:284-290.
    • (1999) J Bacteriol , vol.181 , pp. 284-290
    • Bauer, M.W.1    Driskill, L.E.2    Callen, W.3    Snead, Ma.4    Mathur, E.J.5    Kelly, R.M.6
  • 5
    • 14644419633 scopus 로고    scopus 로고
    • Analysis of the function of a hyperthermophilic endoglucanase from Pyrococcus horikoshii that hydrolyzes crystalline cellulose
    • Kashima Y, Mori K, Fukada H, Ishikawa K. Analysis of the function of a hyperthermophilic endoglucanase from Pyrococcus horikoshii that hydrolyzes crystalline cellulose, Extremophiles 2005;9:37-43.
    • (2005) Extremophiles , vol.9 , pp. 37-43
    • Kashima, Y.1    Mori, K.2    Fukada, H.3    Ishikawa, K.4
  • 6
    • 0030061364 scopus 로고    scopus 로고
    • Catalytical potency of beta-glucosidase from the extremophile Pyrococcus furiosus in glucoconjugate synthesis
    • DOI 10.1038/nbt0196-88
    • 6. Fischer L, Bromann R, Kengen SW, de Vos WM, Wagner F. Catalyticai potency of beta-glucosidase from the extremophile Pyrococcus furiosus in glucoconjugate synthesis. Biotechnology (N Y) 1996;14:88-91. (Pubitemid 3016631)
    • (1996) Bio/Technology , vol.14 , Issue.1 , pp. 88-91
    • Fischer, L.1    Bromann, R.2    Kengen, S.W.3    De Vos, W.M.4    Wagner, F.5
  • 7
    • 0040776974 scopus 로고    scopus 로고
    • Comparative structural analysis and substrate specificity engineering of the hyperthermostable beta-glucosidase CelB from Pyrococcus furiosus
    • Kaper T, Lebbink JH, Pouwels J, et al. Comparative structural analysis and substrate specificity engineering of the hyperthermostable beta-glucosidase CelB from Pyrococcus furiosus. Biochemistry 2000;39:4963-4970.
    • (2000) Biochemistry , vol.39 , pp. 4963-4970
    • Kaper, T.1    Lebbink, J.H.2    Pouwels, J.3
  • 8
    • 0034603740 scopus 로고    scopus 로고
    • Improving low-temperature catalysis in the hyperthermostable Pyrococcus furiosus beta-glucosidase CelB by directed evolution
    • Lebbink JH, Kaper T, Bron P, van der Oost J, de Vos WM. Improving low-temperature catalysis in the hyperthermostable Pyrococcus furiosus beta-glucosidase CelB by directed evolution. Biochemistry 2000;39:3656-3665.
    • (2000) Biochemistry , vol.39 , pp. 3656-3665
    • Lebbink, J.H.1    Kaper, T.2    Bron, P.3    Van Der Oost, J.4    De Vos, W.M.5
  • 9
    • 0035143560 scopus 로고    scopus 로고
    • Beta-Glucosidase CelB from Pyrococcus furiosus: Production by Escherichia coli, purification, and in vitro evolution
    • Lebbink JH, Kaper T, Kengen SW, van der Oost J, de Vos WM. beta-Glucosidase CelB from Pyrococcus furiosus: production by Escherichia coli, purification, and in vitro evolution. Methods Enzymol 2001; 330: 364-379.
    • (2001) Methods Enzymol , vol.330 , pp. 364-379
    • Lebbink, J.H.1    Kaper, T.2    Kengen, S.W.3    Van Der Oost, J.4    De Vos, W.M.5
  • 10
    • 0028876332 scopus 로고
    • Characterization of the celB gene coding for beta-glucosidase from the hyperthermophilic archaeon Pyrococcus furiosus and its expression and site-directed mutation in Escherichia coll
    • Voorhorst WG, Eggen. RI, Luesink EJ, de Vos WM, Characterization of the celB gene coding for beta-glucosidase from the hyperthermophilic archaeon Pyrococcus furiosus and its expression and site-directed mutation in Escherichia coll. J Bacteriol 1995;177:7105-7111.
    • (1995) J Bacteriol , vol.177 , pp. 7105-7111
    • Voorhorst, W.G.1    Eggen, R.I.2    Luesink, E.J.3    De Vos, W.M.4
  • 11
    • 57349124144 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray analysis of endoglucanase from Pyrococcus horikoshii
    • Kim HW, Mino K, Ishikawa K. Crystallization and preliminary X-ray analysis of endoglucanase from Pyrococcus horikoshii. Acta Crystallogr Sect F Struct Biol Cryst Commun 2008;64:1169-1171.
    • (2008) Acta Crystallogr Sect F Struct Biol Cryst Commun , vol.64 , pp. 1169-1171
    • Kim, H.W.1    Mino, K.2    Ishikawa, K.3
  • 12
    • 34548500137 scopus 로고    scopus 로고
    • Analysis of active center in hyperthermophilic cellulase from Pyrococcus horikoshii
    • 12. Kang HJ, Ishikawa K. Analysis of active center in hyperthermophilic cellulase from Pyrococcus horikoshii. J Microbiol Biotechnol 2007;17:1249-1253. (Pubitemid 47377390)
    • (2007) Journal of Microbiology and Biotechnology , vol.17 , Issue.8 , pp. 1249-1253
    • Kang, H.-J.1    Ishikawa, K.2
  • 13
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • The CCP4 suite: programs for protein crystallography. Acta Crystallogr D Biol Crystallogr 1994;50:760-763.
    • (1994) Acta Crystallogr D Biol Crystallogr , vol.50 , pp. 760-763
  • 15
  • 16
    • 4644366388 scopus 로고    scopus 로고
    • Hkl2map: A graphical user interface for macromolecular phasing with shelx programs
    • Pape T, Schneider TR. Hkl2map: a graphical user interface for macromolecular phasing with shelx programs. J Appl Cryst 2004;37: 843-844.
    • (2004) J Appl Cryst , vol.37 , pp. 843-844
    • Pape, T.1    Schneider, T.R.2
  • 17
    • 0029740205 scopus 로고    scopus 로고
    • Crystal structure of thermostable family 5 endocellulase E1 from Acidothermus cellulolyticus in complex with cellotetraose
    • Sakon J, Adney WS, Himmel ME, Thomas SR, Karplus PA. Crystal structure of thermostable family 5 endocellulase E1 from Acidothermus cellulolyticus in complex with cellotetraose. Biochemistry 1996; 35:10648-10660.
    • (1996) Biochemistry , vol.35 , pp. 10648-10660
    • Sakon, J.1    Adney, W.S.2    Himmel, M.E.3    Thomas, S.R.4    Karplus, P.A.5
  • 18
    • 33847258778 scopus 로고    scopus 로고
    • Improvement of the enzymatic activity of the hyperthermophilic cellulase from Pyrococcus horikoshii
    • Rang HJ, Uegaki K, Fukada H, Ishikawa K, Improvement of the enzymatic activity of the hyperthermophilic cellulase from Pyrococcus horikoshii. Extremophiles 2007;11:251-256.
    • (2007) Extremophiles , vol.11 , pp. 251-256
    • Rang, H.J.1    Uegaki, K.2    Fukada, H.3    Ishikawa, K.4
  • 19
    • 0029993491 scopus 로고    scopus 로고
    • The crystal structure of a family 5 endoglucanase mutant in complexed and uncomplexed forms reveals an induced fit activation mechanism
    • Dominguez R, Souchon H, Lascombe M, Alzan PM. The crystal structure of a family 5 endoglucanase mutant in complexed and uncomplexed forms reveals an induced fit activation mechanism. J Mol Biol 1996;257:1042-1051.
    • (1996) J Mol Biol , vol.257 , pp. 1042-1051
    • Dominguez, R.1    Souchon, H.2    Lascombe, M.3    Alzan, P.M.4
  • 20
    • 0029166485 scopus 로고
    • Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases
    • Henrissat B, Callebaut I, Fabrega S, Lehn P, Mornon JP, Davies G. Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases. Proc Natl Acad Sci USA 1995;92:7090-7094.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 7090-7094
    • Henrissat, B.1    Callebaut, I.2    Fabrega, S.3    Lehn, P.4    Mornon, J.P.5    Davies, G.6
  • 21
    • 0028956984 scopus 로고
    • Beta-glucosidase, beta-galactosidase, family A cellulases, family F xylanases and two barley glycanases form a superfamily of enzymes with 8-fold beta/ alpha architecture and with two conserved glutamates near the carboxy-terminal ends of beta-strands four and seven
    • Jenkins J, Lo Leggio L, Harris G, Pickersgill R. Beta-glucosidase, beta-galactosidase, family A cellulases, family F xylanases and two barley glycanases form a superfamily of enzymes with 8-fold beta/ alpha architecture and with two conserved glutamates near the carboxy-terminal ends of beta-strands four and seven. FEBS Lett 1995;362:281-285.
    • (1995) FEBS Lett , vol.362 , pp. 281-285
    • Jenkins, J.1    Lo Leggio, L.2    Harris, G.3    Pickersgill, R.4
  • 22
    • 84979146389 scopus 로고
    • Stereochemistry and the mechanism of enzymatic reactions
    • Koshland DEJ. Stereochemistry and the mechanism of enzymatic reactions. Biol Rev 1953;28:416-436.
    • (1953) Biol Rev , vol.28 , pp. 416-436
    • Koshland, D.E.J.1
  • 23
    • 0025354545 scopus 로고
    • Calcium binding in alpha-amylases: An X-ray diffraction study at 2.1-A resolution of two enzymes from Aspergillus
    • Boel E, Brady L, Brzozowski AM, et al. Calcium binding in alpha-amylases: an X-ray diffraction study at 2.1-A resolution of two enzymes from Aspergillus. Biochemistry 1990;29:6244-6249.
    • (1990) Biochemistry , vol.29 , pp. 6244-6249
    • Boel, E.1    Brady, L.2    Brzozowski, A.M.3
  • 24
    • 0034737321 scopus 로고    scopus 로고
    • Insights into ligand-induced conformational change in Cel5A from Bacillus agaradhaerens revealed by a catalytically active crystal form
    • Varrot A, Schulein M, Davies GJ. Insights into ligand-induced conformational change in Cel5A from Bacillus agaradhaerens revealed by a catalytically active crystal form, J Mol Biol 2000;297: 819-828.
    • (2000) J Mol Biol , vol.297 , pp. 819-828
    • Varrot, A.1    Schulein, M.2    Davies, G.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.