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Volumn 6, Issue 8, 1997, Pages 1718-1726

Xylanase XynA from the hyperthermophilic bacterium Thermotoga maritima: Structure and stability of the recombinant enzyme and its isolated cellulose- binding domain

Author keywords

Cellulose binding domain; Hyperthermophiles; Stability; Thermotoga maritima; Xylanase

Indexed keywords

XYLAN ENDO 1,3 BETA XYLOSIDASE;

EID: 0030861309     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560060812     Document Type: Article
Times cited : (45)

References (31)
  • 1
    • 0027161156 scopus 로고
    • The crusade against chlorine
    • Amato I. 1993. The crusade against chlorine. Science 261:152-154.
    • (1993) Science , vol.261 , pp. 152-154
    • Amato, I.1
  • 3
    • 0029824486 scopus 로고    scopus 로고
    • Evidence that linker sequences and cellulose-binding domains enhance the activity of hemicellulases against complex substrates
    • Black GW, Rixon JE, Clarke JH, Hazlewood GP, Theodorou MK, Morris P, Gilbert HJ. 1996. Evidence that linker sequences and cellulose-binding domains enhance the activity of hemicellulases against complex substrates. Biochem J 319:515-520.
    • (1996) Biochem J , vol.319 , pp. 515-520
    • Black, G.W.1    Rixon, J.E.2    Clarke, J.H.3    Hazlewood, G.P.4    Theodorou, M.K.5    Morris, P.6    Gilbert, H.J.7
  • 4
    • 0030012798 scopus 로고    scopus 로고
    • A modular xylanase from mesophilic Cellulomonas fimi contains the same cellulose-binding and thermostabilizing domains as xylanases from thermophilic bacteria
    • Clarke JH, Davidson K, Gilbert HJ, Fontes CMGA, Hazlewood GP. 1996. A modular xylanase from mesophilic Cellulomonas fimi contains the same cellulose-binding and thermostabilizing domains as xylanases from thermophilic bacteria. FEMS Microbiol Lett 139:27-35.
    • (1996) FEMS Microbiol Lett , vol.139 , pp. 27-35
    • Clarke, J.H.1    Davidson, K.2    Gilbert, H.J.3    Fontes, C.M.G.A.4    Hazlewood, G.P.5
  • 5
    • 0020484055 scopus 로고
    • Partial specific volume changes of proteins: Densimetric studies
    • Durchschlag H, Jaenicke R. 1982. Partial specific volume changes of proteins: Densimetric studies. Biochem Biophys Res Commun 108:1074-1079.
    • (1982) Biochem Biophys Res Commun , vol.108 , pp. 1074-1079
    • Durchschlag, H.1    Jaenicke, R.2
  • 7
    • 0015236352 scopus 로고
    • Electrophoretic analysis of the major polypeptides of the human erythrocyte membrane
    • Fairbanks G, Steck TL, Wallach DFH. 1971. Electrophoretic analysis of the major polypeptides of the human erythrocyte membrane. Biochemistry 10:2606-2617.
    • (1971) Biochemistry , vol.10 , pp. 2606-2617
    • Fairbanks, G.1    Steck, T.L.2    Wallach, D.F.H.3
  • 8
    • 0028949132 scopus 로고
    • Evidence for a general role for non-catalytic thermostabilizing domains in xylanases from thermophilic bacteria
    • Fontes CMGA, Hazlewood GP, Morag E, Hall J, Hirst BH, Gilbert HJ. 1995. Evidence for a general role for non-catalytic thermostabilizing domains in xylanases from thermophilic bacteria. Biochem J 307:151-158.
    • (1995) Biochem J , vol.307 , pp. 151-158
    • Fontes, C.M.G.A.1    Hazlewood, G.P.2    Morag, E.3    Hall, J.4    Hirst, B.H.5    Gilbert, H.J.6
  • 9
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • Gill SJ, von Hippel PH. 1989. Calculation of protein extinction coefficients from amino acid sequence data. Anal Biochem 182:319-326.
    • (1989) Anal Biochem , vol.182 , pp. 319-326
    • Gill, S.J.1    Von Hippel, P.H.2
  • 10
    • 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 280:309-316.
    • (1991) Biochem J , vol.280 , pp. 309-316
    • Henrissat, B.1
  • 11
    • 0023506457 scopus 로고
    • Folding and association of proteins
    • Jaenicke R. 1987. Folding and association of proteins. Prog Biophys Mol Biol 49:117-237.
    • (1987) Prog Biophys Mol Biol , vol.49 , pp. 117-237
    • Jaenicke, R.1
  • 12
    • 0029685460 scopus 로고    scopus 로고
    • Protein folding and association: In vitro studies for self-organization and targeting in the cell
    • Jaenicke R. 1996. Protein folding and association: In vitro studies for self-organization and targeting in the cell. Curr Top Cell Regul 34:209-314.
    • (1996) Curr Top Cell Regul , vol.34 , pp. 209-314
    • Jaenicke, R.1
  • 13
    • 0029786277 scopus 로고    scopus 로고
    • Structure and stability of "hyperstable proteins:" Glycolytic enzymes from the hyperthermophilic bacterium Thermotoga maritima
    • Jaenicke R, Schurig H, Beaucamp N, Ostendorp R. 1996. Structure and stability of "hyperstable proteins:" Glycolytic enzymes from the hyperthermophilic bacterium Thermotoga maritima. Adv Prot Chem 48:181-269.
    • (1996) Adv Prot Chem , vol.48 , pp. 181-269
    • Jaenicke, R.1    Schurig, H.2    Beaucamp, N.3    Ostendorp, R.4
  • 14
  • 15
    • 0021248179 scopus 로고
    • SDS-PAGE strongly overestimates the molecular masses of the neurofilament proteins
    • Kaufmann E, Geisler N, Weber K. 1984. SDS-PAGE strongly overestimates the molecular masses of the neurofilament proteins. FEBS Lett 170:81-84.
    • (1984) FEBS Lett , vol.170 , pp. 81-84
    • Kaufmann, E.1    Geisler, N.2    Weber, K.3
  • 16
    • 0014010861 scopus 로고
    • Viscosity and density of aqueous solutions of urea and guanidine hydrochloride
    • Kawahara K, Tanford C. 1966. Viscosity and density of aqueous solutions of urea and guanidine hydrochloride. J Biol Chem 241:3228-3232.
    • (1966) J Biol Chem , vol.241 , pp. 3228-3232
    • Kawahara, K.1    Tanford, C.2
  • 17
    • 0024593759 scopus 로고
    • On the origin of the positive band in the far-ultraviolet circular dichroic spectrum of fibronectin
    • Khan MY, Villanueva G, Newman SA. 1989. On the origin of the positive band in the far-ultraviolet circular dichroic spectrum of fibronectin. J Biol Chem 264:2139-2142.
    • (1989) J Biol Chem , vol.264 , pp. 2139-2142
    • Khan, M.Y.1    Villanueva, G.2    Newman, S.A.3
  • 18
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 19
    • 0027274760 scopus 로고
    • Characterization of the active site and thermostability regions of endoxylanase from Thermoanaerobacterium saccharolyticum B6A-RI
    • Lee YE, Lowe SE, Henrissat B, Zeikus G. 1993. Characterization of the active site and thermostability regions of endoxylanase from Thermoanaerobacterium saccharolyticum B6A-RI. J Bacteriol 175:5890-5898.
    • (1993) J Bacteriol , vol.175 , pp. 5890-5898
    • Lee, Y.E.1    Lowe, S.E.2    Henrissat, B.3    Zeikus, G.4
  • 21
    • 0028834548 scopus 로고
    • Novel cellulose-binding domains, NodB homologues, and conserved modular architecture in xylanases from the aerobic soil bacteria Pseudomonasfluorescens subsp. cellulosa and Cellvibrio mixtus
    • Millward-Sadler SJ, Davidson K, Hazlewood GP, Black GW, Gilbert HJ, Clarke JH. 1995. Novel cellulose-binding domains, NodB homologues, and conserved modular architecture in xylanases from the aerobic soil bacteria Pseudomonasfluorescens subsp. cellulosa and Cellvibrio mixtus. Biochem J 312:39-48.
    • (1995) Biochem J , vol.312 , pp. 39-48
    • Millward-Sadler, S.J.1    Davidson, K.2    Hazlewood, G.P.3    Black, G.W.4    Gilbert, H.J.5    Clarke, J.H.6
  • 22
    • 0022555885 scopus 로고
    • Determination and analysis of urea and guanidine hydrochloride denaturation curves
    • Pace CN. 1986. Determination and analysis of urea and guanidine hydrochloride denaturation curves. Methods Enzymol 131:266-280.
    • (1986) Methods Enzymol , vol.131 , pp. 266-280
    • Pace, C.N.1
  • 23
    • 0026628269 scopus 로고
    • Deconvolution of the circular dichroism spectra of proteins: The circular dichroism spectra of the antiparallel beta-sheet in proteins
    • Perczel A, Park K, Fasman GD. 1992. Deconvolution of the circular dichroism spectra of proteins: The circular dichroism spectra of the antiparallel beta-sheet in proteins. Proteins Struct Funct Genet 13:57-69.
    • (1992) Proteins Struct Funct Genet , vol.13 , pp. 57-69
    • Perczel, A.1    Park, K.2    Fasman, G.D.3
  • 24
    • 0025339471 scopus 로고
    • Folding of an all-β protein: Independent domain folding in γII-crystallin from calf eye lens
    • Rudolph R, Neßlauer G, Siebendritt R, Sharma AK, Jaenicke R. 1990. Folding of an all-β protein: Independent domain folding in γII-crystallin from calf eye lens. Proc Natl Acad Sci USA 87:4625-4629.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 4625-4629
    • Rudolph, R.1    Neßlauer, G.2    Siebendritt, R.3    Sharma, A.K.4    Jaenicke, R.5
  • 25
    • 0000722070 scopus 로고
    • Spectral methods of characterizing protein conformation and conformational changes
    • Creighton TE, ed. Oxford: IRL
    • Schmid FX. 1989. Spectral methods of characterizing protein conformation and conformational changes. In: Creighton TE, ed. Protein structure, a practical approach. Oxford: IRL. pp 251-285.
    • (1989) Protein Structure, a Practical Approach , pp. 251-285
    • Schmid, F.X.1
  • 27
    • 0024971067 scopus 로고
    • Folding of thermolysin fragments. Hydrodynamic properties of isolated domains and subdomains
    • Vita C, Fontana A, Jaenicke R. 1989. Folding of thermolysin fragments. Hydrodynamic properties of isolated domains and subdomains. Eur J Biochem 183:513-518.
    • (1989) Eur J Biochem , vol.183 , pp. 513-518
    • Vita, C.1    Fontana, A.2    Jaenicke, R.3
  • 29
    • 0028901697 scopus 로고
    • Identification of a novel cellulose-binding domain within the multidomain 120 kDa xylanase XynA of the hyperthermophilic bacterium Thermotoga maritima
    • Winterhalter C, Heinrich P, Candussio A, Wich G, Liebl W. 1995. Identification of a novel cellulose-binding domain within the multidomain 120 kDa xylanase XynA of the hyperthermophilic bacterium Thermotoga maritima. Mol Microbiol 15:431-444.
    • (1995) Mol Microbiol , vol.15 , pp. 431-444
    • Winterhalter, C.1    Heinrich, P.2    Candussio, A.3    Wich, G.4    Liebl, W.5
  • 30
    • 0028102759 scopus 로고
    • Contributions of tryptophan side chains to the far-ultraviolet circular dichroism of proteins
    • Woody RW. 1994. Contributions of tryptophan side chains to the far-ultraviolet circular dichroism of proteins. Eur Biophys J 23:253-262.
    • (1994) Eur Biophys J , vol.23 , pp. 253-262
    • Woody, R.W.1
  • 31
    • 0029916417 scopus 로고    scopus 로고
    • The multidomain xylanase A of the hyperthermophilic bacterium Thermotoga neapolitana is extremely thermoresistant
    • Zverlov V, Piotukh K, Dakhova O, Velikodvorskaya G, Borriss R. 1996. The multidomain xylanase A of the hyperthermophilic bacterium Thermotoga neapolitana is extremely thermoresistant. Appl Microbiol Biotechnol 45:245-247.
    • (1996) Appl Microbiol Biotechnol , vol.45 , pp. 245-247
    • Zverlov, V.1    Piotukh, K.2    Dakhova, O.3    Velikodvorskaya, G.4    Borriss, R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.