메뉴 건너뛰기




Volumn 9, Issue 3, 2000, Pages 466-475

An additional aromatic interaction improves the thermostability and thermophilicity of a mesophilic family 11 xylanase: Structural basis and molecular study

Author keywords

Aromatic interaction; Endo 1,4 xylanase; Molecular modeling; Site directed mutagenesis; Structural analysis; Thermophilicity; Thermostability

Indexed keywords

XYLAN ENDO 1,3 BETA XYLOSIDASE;

EID: 0343293808     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.9.3.466     Document Type: Article
Times cited : (166)

References (30)
  • 1
    • 0027209738 scopus 로고
    • Hydrophobic core repacking and aromatic-aromatic interaction in the thermostable mutant of T4 lysozyme ser117 → phe
    • Anderson DE, Hurley JH, Nicholson H, Baase WA, Matthews BW. 1993. Hydrophobic core repacking and aromatic-aromatic interaction in the thermostable mutant of T4 lysozyme Ser117 → Phe. Protein Sci 8:1285-1290.
    • (1993) Protein Sci , vol.8 , pp. 1285-1290
    • Anderson, D.E.1    Hurley, J.H.2    Nicholson, H.3    Baase, W.A.4    Matthews, B.W.5
  • 4
    • 0030772482 scopus 로고    scopus 로고
    • Family-10 and family-11 xylanases differ in their capacity to enhance the bleach-ability of hardwood and softwood paper pulps
    • Clarke JH, Rixon JE, Ciruela A, Gilbert HJ, Hazlewood GP. 1997. Family-10 and Family-11 xylanases differ in their capacity to enhance the bleach-ability of hardwood and softwood paper pulps. Appl Microbiol Biot 48: 177-183.
    • (1997) Appl Microbiol Biot , vol.48 , pp. 177-183
    • Clarke, J.H.1    Rixon, J.E.2    Ciruela, A.3    Gilbert, H.J.4    Hazlewood, G.P.5
  • 5
    • 0031873691 scopus 로고    scopus 로고
    • Scan rate dependence in protein calorimetry: The irreversible transitions of Bacillus circulans xylanase and a disulfide-bridge mutant
    • Davoodi J, Wakarchuck WW, Surewicz WK, Carey PR. 1998. Scan rate dependence in protein calorimetry: The irreversible transitions of Bacillus circulans xylanase and a disulfide-bridge mutant. Protein Sci 7:1538-1544.
    • (1998) Protein Sci , vol.7 , pp. 1538-1544
    • Davoodi, J.1    Wakarchuck, W.W.2    Surewicz, W.K.3    Carey, P.R.4
  • 8
    • 0028949132 scopus 로고
    • Evidence for a general role for non-catalytic 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 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
    • 0033952763 scopus 로고    scopus 로고
    • Purification and properties of three endo-β-1,4-xylanases produced by Streptomyces sp. Strain S38 which differ in their capacity to enhance the bleaching of kraft pulp
    • Georis J, Giannotta F, De Buyl E, Granier B, Frère JM. 2000. Purification and properties of three endo-β-1,4-xylanases produced by Streptomyces sp. strain S38 which differ in their capacity to enhance the bleaching of kraft pulp. Enzyme Microb Technol 26.
    • (2000) Enzyme Microb Technol , vol.26
    • Georis, J.1    Giannotta, F.2    De Buyl, E.3    Granier, B.4    Frère, J.M.5
  • 10
    • 0032865133 scopus 로고    scopus 로고
    • Sequence, overproduction and purification of the endo-β-1,4-xylanase encoded by the xylI gene of Streptomyces sp. S38
    • Georis J, Giannotta F, Lamotte-Brasseur J, Devreese B, Van Beeumen J, Granier B, Frère JM. 1999. Sequence, overproduction and purification of the endo-β-1,4-xylanase encoded by the xylI gene of Streptomyces sp. S38. Gene 237:123-133.
    • (1999) Gene , vol.237 , pp. 123-133
    • Georis, J.1    Giannotta, F.2    Lamotte-Brasseur, J.3    Devreese, B.4    Van Beeumen, J.5    Granier, B.6    Frère, J.M.7
  • 11
    • 0032578420 scopus 로고    scopus 로고
    • Thermophilic xylanase from Thermomyces lanuginosus: High-resolution X-ray structure and modeling studies
    • Gruber K, Klintschar G, Hayn M, Schlacher A, Steiner W, Kratky C. 1998. Thermophilic xylanase from Thermomyces lanuginosus: High-resolution X-ray structure and modeling studies. Biochemistry 37:13475-13485.
    • (1998) Biochemistry , vol.37 , pp. 13475-13485
    • Gruber, K.1    Klintschar, G.2    Hayn, M.3    Schlacher, A.4    Steiner, W.5    Kratky, C.6
  • 13
    • 0027225980 scopus 로고
    • New families in the classification of glycosyl hydrolases based on amino acid sequence similarities
    • Henrissat B, Bairoch A. 1993. New families in the classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem J 293:781-788.
    • (1993) Biochem J , vol.293 , pp. 781-788
    • Henrissat, B.1    Bairoch, A.2
  • 14
    • 0028294637 scopus 로고
    • Characterization and sequence of a Thermomonospora fusca xylanase
    • Irwin D, Jung ED, Wilson DB. 1994. Characterization and sequence of a Thermomonospora fusca xylanase. Appl Environ Microb 60(3):763-770.
    • (1994) Appl Environ Microb , vol.60 , Issue.3 , pp. 763-770
    • Irwin, D.1    Jung, E.D.2    Wilson, D.B.3
  • 15
    • 0023430560 scopus 로고
    • Enhanced protein thermostability from site-directed mutations that decrease the entropy of unfolding
    • Matthews BW, Nicholson H, Becktel WJ. 1987. Enhanced protein thermostability from site-directed mutations that decrease the entropy of unfolding. Proc Natl Acad Sci USA 84:6663-6667.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 6663-6667
    • Matthews, B.W.1    Nicholson, H.2    Becktel, W.J.3
  • 17
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls A, Sharp K, Honig B. 1991. Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 11:281-296.
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.2    Honig, B.3
  • 19
    • 0028786876 scopus 로고
    • Sequence and expression of a xylanase gene from the hyperthermophile Thermotoga sp. Strain FjSS3-B1 and characterization of the recombinant enzyme and its activity on kraft pulp
    • Saul DJ, Williams LC, Reeves RA, Gibbs MD, Bergquist PL. 1995. Sequence and expression of a xylanase gene from the hyperthermophile Thermotoga sp. strain FjSS3-B1 and characterization of the recombinant enzyme and its activity on Kraft pulp. Appl Environ Microb 61:4110-4113.
    • (1995) Appl Environ Microb , vol.61 , pp. 4110-4113
    • Saul, D.J.1    Williams, L.C.2    Reeves, R.A.3    Gibbs, M.D.4    Bergquist, P.L.5
  • 20
    • 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
  • 22
    • 0001433241 scopus 로고
    • Knowledge based modeling of homologous proteins, part I: Three-dimensional frameworks derived from the simultaneous superposition of multiple structures
    • Sutcliffe MJ, Haneef I, Carney D, Blundell TL. 1987a. Knowledge based modeling of homologous proteins, part I: Three-dimensional frameworks derived from the simultaneous superposition of multiple structures. Protein Eng 1:377-384.
    • (1987) Protein Eng , vol.1 , pp. 377-384
    • Sutcliffe, M.J.1    Haneef, I.2    Carney, D.3    Blundell, T.L.4
  • 23
    • 0000179199 scopus 로고
    • Knowledge based modelling of homologous proteins, part II: Rules for the conformations of substituted side chains
    • Sutcliffe MJ, Hayes FRF, Blundell TL. 1987b. Knowledge based modelling of homologous proteins, part II: Rules for the conformations of substituted side chains. Protein Ens 1:385-392.
    • (1987) Protein Ens , vol.1 , pp. 385-392
    • Sutcliffe, M.J.1    Hayes, F.R.F.2    Blundell, T.L.3
  • 24
    • 0028338985 scopus 로고
    • Three-dimensional structure of endo-1,4-β-xylanase II from Trichoderma reesei: Two functional states in the active site
    • Törrönen A, Harkki J, Rouvinen J. 1994. Three-dimensional structure of endo-1,4-β-xylanase II from Trichoderma reesei: Two functional states in the active site. EMBO J 13:2493-2501.
    • (1994) EMBO J , vol.13 , pp. 2493-2501
    • Törrönen, A.1    Harkki, J.2    Rouvinen, J.3
  • 25
    • 0028911057 scopus 로고
    • Structural comparison of two major endo-1,4-xylanases from Trichoderma reesei
    • Törrönen A, Rouvinen J. 1995. Structural comparison of two major endo-1,4-xylanases from Trichoderma reesei. Biochemistry 34:847-856.
    • (1995) Biochemistry , vol.34 , pp. 847-856
    • Törrönen, A.1    Rouvinen, J.2
  • 26
    • 0040003315 scopus 로고    scopus 로고
    • Structural and functional properties of low molecular weight endo-1,4-β-xylanases
    • Törrönen A, Rouvinen J. 1997. Structural and functional properties of low molecular weight endo-1,4-β-xylanases. J Biotechnol 57:137-149.
    • (1997) J Biotechnol , vol.57 , pp. 137-149
    • Törrönen, A.1    Rouvinen, J.2
  • 29
    • 0029008857 scopus 로고
    • Two extremely thermostable xylanases of the hyperthermophilic bacterium Thermotoga maritima MSB8
    • Winterhalter C, Liebl W. 1995. Two extremely thermostable xylanases of the hyperthermophilic bacterium Thermotoga maritima MSB8. Appl Environ Microb 15-3:1810-1815.
    • (1995) Appl Environ Microb , vol.15 , Issue.3 , pp. 1810-1815
    • Winterhalter, C.1    Liebl, W.2
  • 30
    • 0029916417 scopus 로고    scopus 로고
    • The multidomain xylanase A of hyperthermophilic bacterium Thermotoga neapolitana is extremely thermoresistant
    • Zverlov V, Piotukh K, Dakhova O, Velikodvorskaya G, Borris R. 1996. The multidomain xylanase A of hyperthermophilic bacterium Thermotoga neapolitana is extremely thermoresistant. Appl Microbiol Biotech 45:245-247.
    • (1996) Appl Microbiol Biotech , vol.45 , pp. 245-247
    • Zverlov, V.1    Piotukh, K.2    Dakhova, O.3    Velikodvorskaya, G.4    Borris, R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.