메뉴 건너뛰기




Volumn 322, Issue 1, 2004, Pages 277-280

Principle component analysis in F/10 and G/11 xylanase

Author keywords

Classification; Computation; Principle component analysis; Structure; Xylanase

Indexed keywords

XYLAN ENDO 1,3 BETA XYLOSIDASE;

EID: 4143081403     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2004.07.116     Document Type: Article
Times cited : (5)

References (17)
  • 2
    • 0030334262 scopus 로고    scopus 로고
    • Xylanases: From biology to biotechnology
    • R.A. Prade Xylanases: from biology to biotechnology Biotechnol. Genet. Eng. Rev. 13 1996 101 131
    • (1996) Biotechnol. Genet. Eng. Rev. , vol.13 , pp. 101-131
    • Prade, R.A.1
  • 3
    • 0030822611 scopus 로고    scopus 로고
    • Enzymes: An important tool in the improvement of the quality of cereal foods
    • K. Poutanen Enzymes: an important tool in the improvement of the quality of cereal foods Trends Food Sci. Technol. 9 1997 300 306
    • (1997) Trends Food Sci. Technol. , vol.9 , pp. 300-306
    • Poutanen, K.1
  • 4
    • 0024087074 scopus 로고
    • Multiplicity of β-1,4-xylanase in microorganisms: Functions and applications
    • K.K. Wong, L.U. Tan, and J. Saddler Multiplicity of β-1,4-xylanase in microorganisms: functions and applications Microbiol. Mol. Biol. Rev 52 1988 305 317
    • (1988) Microbiol. Mol. Biol. Rev , vol.52 , pp. 305-317
    • Wong, K.K.1    Tan2    Saddler, J.L.U.3
  • 5
    • 0024419181 scopus 로고
    • Cellulase families revealed by hydrophobic cluster analysis
    • B. Henrissat, M. Claeyssens, P. Tomme, L. Lemesle, and J.P. Mornon Cellulase families revealed by hydrophobic cluster analysis Gene 81 1989 83 95
    • (1989) Gene , vol.81 , pp. 83-95
    • Henrissat, B.1    Claeyssens, M.2    Tomme, P.3    Lemesle4    Mornon, J.P.L.5
  • 6
    • 0025804758 scopus 로고
    • Domains in microbial B-1,4-glycanases: Sequence conservation, function, and enzyme families
    • N.R. Gilkes, D.G. Kilburn, R.C. Miller Jr., and J. Sundquist Domains in microbial B-1,4-glycanases: sequence conservation, function, and enzyme families Microbiol. Mol. Biol. Rev. 55 1991 303 315
    • (1991) Microbiol. Mol. Biol. Rev. , vol.55 , pp. 303-315
    • Gilkes, N.R.1    Kilburn, D.G.2    Miller Jr., R.C.3    Sundquist, J.4
  • 7
    • 0026055308 scopus 로고
    • A classification of glycosyl hydrolases based on amino acid sequence similarities
    • B. Henrissat A classification of glycosyl hydrolases based on amino acid sequence similarities Biochem. J. 280 1991 309 316
    • (1991) Biochem. J. , vol.280 , pp. 309-316
    • Henrissat, B.1
  • 8
    • 0027225980 scopus 로고
    • New families in the classification of glycosyl hydrolases based on amino acid sequence similarities
    • B. Henrissat, and A. Bairoch New families in the classification of glycosyl hydrolases based on amino acid sequence similarities Biochem. J. 293 1993 781 788
    • (1993) Biochem. J. , vol.293 , pp. 781-788
    • Henrissat1    Bairoch, A.B.2
  • 10
    • 0033527441 scopus 로고    scopus 로고
    • Xylanase II from an alkaliphilic thermophilic Bacillus with a distinctly different structure from other xylanases: Evolutionary relationship to alkaliphilic xylanases
    • N. Kulkarni, M. Lakshmikumaran, and M. Rao Xylanase II from an alkaliphilic thermophilic Bacillus with a distinctly different structure from other xylanases: evolutionary relationship to alkaliphilic xylanases Biochem. Biophys. Res. Commun. 263 1999 640 645
    • (1999) Biochem. Biophys. Res. Commun. , vol.263 , pp. 640-645
    • Kulkarni, N.1    Lakshmikumaran2    Rao, M.M.3
  • 11
    • 0032984477 scopus 로고    scopus 로고
    • Molecular and biotechnological aspects of xylanases
    • N. Kulkarni, A. Shendye, and M. Rao Molecular and biotechnological aspects of xylanases FEMS Microbiol. Rev. 23 1999 411 456
    • (1999) FEMS Microbiol. Rev. , vol.23 , pp. 411-456
    • Kulkarni, N.1    Shendye2    Rao, M.A.3
  • 13
    • 0017868338 scopus 로고
    • Empirical predictions of protein conformation
    • P.Y. Chou, and G.D. Fasman Empirical predictions of protein conformation Ann. Rev. Biochem. 47 1978 251 276
    • (1978) Ann. Rev. Biochem. , vol.47 , pp. 251-276
    • Chou1    Fasman, G.D.P.Y.2
  • 14
    • 0033567040 scopus 로고    scopus 로고
    • High resolution structure and sequence of T. aurantiacus xylanase I: Implication for the evolution of thermostability in family 10 xylanases and enzymes with Barrel architecture
    • L. Lo Leggio, S. Kalogiannis, M.K. Bhat, and R.W. Pickersgill High resolution structure and sequence of T. aurantiacus xylanase I: implication for the evolution of thermostability in family 10 xylanases and enzymes with Barrel architecture Proteins 36 1999 295 306
    • (1999) Proteins , vol.36 , pp. 295-306
    • Lo Leggio, L.1    Kalogiannis, S.2    Bhat3    Pickersgill, R.W.M.K.4
  • 15
    • 12244272407 scopus 로고    scopus 로고
    • Partial NMR assignments and secondary structure mapping of the isolated subunit of Escherichia coli tryptophan synthase a 29-kDa TIM barrel protein
    • R. Vadrevu, C.J. Falzone, and C.R. Matthews Partial NMR assignments and secondary structure mapping of the isolated subunit of Escherichia coli tryptophan synthase a 29-kDa TIM barrel protein Protein Sci. 12 2003 185 191
    • (2003) Protein Sci. , vol.12 , pp. 185-191
    • Vadrevu, R.1    Falzone2    Matthews, C.R.C.J.3
  • 16
    • 0028338985 scopus 로고
    • Three-dimensional structure of endo-1,4-beta-xylanase II from Trichoderma reesei: Two conformational states in the active site
    • A. Torronen, A. Harkki, and J. Rouvinen Three-dimensional structure of endo-1,4-beta-xylanase II from Trichoderma reesei: two conformational states in the active site EMBO J. 13 1994 2493 2501
    • (1994) EMBO J. , vol.13 , pp. 2493-2501
    • Torronen, A.1    Harkki2    Rouvinen, J.A.3
  • 17
    • 0030592470 scopus 로고    scopus 로고
    • Three-dimensional structure of endo-1,4-xylanase I from Aspergillus niger: Molecular basis for its low pH optimum
    • U. Krengel Three-dimensional structure of endo-1,4-xylanase I from Aspergillus niger: molecular basis for its low pH optimum J. Mol. Biol. 263 1996 70 78
    • (1996) J. Mol. Biol. , vol.263 , pp. 70-78
    • Krengel, U.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.