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Volumn 44, Issue 38, 2005, Pages 12700-12708

The structure and characterization of a modular endo-β-1,4-mannanase from Cellulomonas fimi

Author keywords

[No Author keywords available]

Indexed keywords

BONE; CHARACTERIZATION; ENZYMES; HYDROLYSIS; POLYSACCHARIDES; X RAY CRYSTALLOGRAPHY;

EID: 25444475768     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi050779v     Document Type: Article
Times cited : (66)

References (47)
  • 3
    • 84979146389 scopus 로고
    • Stereochemistry and the mechanism of enzymatic reactions
    • Koshland, D. E. (1953) Stereochemistry and the mechanism of enzymatic reactions, Biol. Rev. 28, 416-436.
    • (1953) Biol. Rev. , vol.28 , pp. 416-436
    • Koshland, D.E.1
  • 4
    • 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, J.-P., and Davies, G. J. (1995) Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases, Proc. Natl. Acad. Sci. U.S.A. 92, 7090-7094.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 7090-7094
    • Henrissat, B.1    Callebaut, I.2    Fabrega, S.3    Lehn, P.4    Mornon, J.-P.5    Davies, G.J.6
  • 5
    • 0028956984 scopus 로고
    • β-glucosidase, β-galactosidase, family a cellulases, family F xylanases and two barley glucanases form a superfamily of enzymes with 8-fold β/α architecture and with two conserved glutamates near the carboxy-terminal ends of β-strands four and seven
    • Jenkins, J., Lo Leggio, L., Harris, G., and Pickersgill, R. (1995) β-glucosidase, β-galactosidase, family A cellulases, family F xylanases and two barley glucanases form a superfamily of enzymes with 8-fold β/α architecture and with two conserved glutamates near the carboxy-terminal ends of β-strands four and seven, FEBS Lett. 362, 281-285.
    • (1995) FEBS Lett. , vol.362 , pp. 281-285
    • Jenkins, J.1    Lo Leggio, L.2    Harris, G.3    Pickersgill, R.4
  • 6
    • 0032533450 scopus 로고    scopus 로고
    • High-resolution native and complex structures of thermostable β-mannanase from Thermomonospora fusca-substrate specificity in glycosyl hydrolase family 5
    • Huge, M., Gloor, S. M., Rypniewski, W., Sauer, O., Heightman, T. D., Zimmermann, W., Winterhalter, K., and Piontek, K. (1998) High-resolution native and complex structures of thermostable β-mannanase from Thermomonospora fusca-substrate specificity in glycosyl hydrolase family 5, Structure 6, 1433-1444.
    • (1998) Structure , vol.6 , pp. 1433-1444
    • Huge, M.1    Gloor, S.M.2    Rypniewski, W.3    Sauer, O.4    Heightman, T.D.5    Zimmermann, W.6    Winterhalter, K.7    Piontek, K.8
  • 8
    • 17744391774 scopus 로고    scopus 로고
    • Three-dimensional structure of (1,4)-β-D-mannan mannanohydrolase from tomato fruit
    • Bourgault, R., Oakley, A. J., Bewley, J. D., Wilce, M. C. (2005) Three-dimensional structure of (1,4)-β-D-mannan mannanohydrolase from tomato fruit, Protein Sci. 14, 1233-1241.
    • (2005) Protein Sci. , vol.14 , pp. 1233-1241
    • Bourgault, R.1    Oakley, A.J.2    Bewley, J.D.3    Wilce, M.C.4
  • 10
    • 0030466871 scopus 로고    scopus 로고
    • Mannanase a from Pseudomonas fluorescens sp. Cellulosa is a retaining glycosyl hydrolase in which E212 and E230 are the putative catalytic residues
    • Bolam, D. N., Hughes, N., Virden, R., Lakey, J. H., Hazlewood, G. P., Henrissat, B., Braithwaite, K. L., and Gilbert, H. J. (1996) Mannanase A from Pseudomonas fluorescens sp. Cellulosa is a retaining glycosyl hydrolase in which E212 and E230 are the putative catalytic residues, Biochemistry 35, 16195-16204.
    • (1996) Biochemistry , vol.35 , pp. 16195-16204
    • Bolam, D.N.1    Hughes, N.2    Virden, R.3    Lakey, J.H.4    Hazlewood, G.P.5    Henrissat, B.6    Braithwaite, K.L.7    Gilbert, H.J.8
  • 11
    • 0035903165 scopus 로고    scopus 로고
    • Crystal structure of mannanase 26A from Pseudomonas cellulosa and analysis of residues involved in substrate binding
    • Hogg, D., Woo, E.-J., Bolam, D. N., McKie, V. A., Gilbert, H. J., and Pickersgill, R. W. (2001) Crystal structure of mannanase 26A from Pseudomonas cellulosa and analysis of residues involved in substrate binding, J. Biol. Chem. 276, 31186-31192.
    • (2001) J. Biol. Chem. , vol.276 , pp. 31186-31192
    • Hogg, D.1    Woo, E.-J.2    Bolam, D.N.3    McKie, V.A.4    Gilbert, H.J.5    Pickersgill, R.W.6
  • 13
    • 0028932041 scopus 로고
    • Cloning and expression in Saccharomyces cerevisiae of a Trichoderma reesei β-mannanase gene containing a cellulose binding domain
    • Stålbrand, H., Saloheimo, A., Vehmaanpera, J., Henrissat, B., Penttilä, M. (1995) Cloning and expression in Saccharomyces cerevisiae of a Trichoderma reesei β-mannanase gene containing a cellulose binding domain, Appl. Environ. Microbiol. 61, 1090-1097.
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 1090-1097
    • Stålbrand, H.1    Saloheimo, A.2    Vehmaanpera, J.3    Henrissat, B.4    Penttilä, M.5
  • 14
    • 0035875574 scopus 로고    scopus 로고
    • Identification of novel β-mannan- and β-glucan-binding modules: Evidence for a superfamily of carbohydrate-binding modules
    • Sunna, A., Gibbs, M. D., and Bergquist, P. L. (2001) Identification of novel β-mannan- and β-glucan-binding modules: evidence for a superfamily of carbohydrate-binding modules, Biochem. J. 356, 791-798.
    • (2001) Biochem. J. , vol.356 , pp. 791-798
    • Sunna, A.1    Gibbs, M.D.2    Bergquist, P.L.3
  • 15
    • 0029843079 scopus 로고    scopus 로고
    • Microbial hydrolysis of polysaccharides
    • Warren, R. A. J. (1996) Microbial hydrolysis of polysaccharides, Annu. Rev. Microbiol. 50, 183-212.
    • (1996) Annu. Rev. Microbiol. , vol.50 , pp. 183-212
    • Warren, R.A.J.1
  • 16
    • 0001973467 scopus 로고    scopus 로고
    • Carbohydrate-active enzymes: An integrated database approach
    • (Gilbert, H. J., Davies, G. J., Henrissat, B., and Svensson, B., Eds.), The Royal Society of Chemistry, Cambridge, England
    • Couthino, P. M., and Henrissat, B. (1999) Carbohydrate-active enzymes: an integrated database approach, in Recent advances in carbohydrate bioengineering (Gilbert, H. J., Davies, G. J., Henrissat, B., and Svensson, B., Eds.), pp 3 -12, The Royal Society of Chemistry, Cambridge, England.
    • (1999) Recent Advances in Carbohydrate Bioengineering , pp. 3-12
    • Couthino, P.M.1    Henrissat, B.2
  • 17
    • 4744368323 scopus 로고    scopus 로고
    • Carbohydrate-binding modules: Fine-tuning polysaccharide recognition
    • Boraston, A. B., Bolam, D. N., Gilbert, H. J., and Davies, G. J. (2004) Carbohydrate-binding modules: fine-tuning polysaccharide recognition, Biochem. J. 382, 769-781.
    • (2004) Biochem. J. , vol.382 , pp. 769-781
    • Boraston, A.B.1    Bolam, D.N.2    Gilbert, H.J.3    Davies, G.J.4
  • 20
    • 0027253195 scopus 로고
    • Purification and characterization of two β-mannanases from Trichoderma reesei
    • Stålbrand, H., Siika-aho, M., Tenkanen, M., and Viikari, L. (1993) Purification and characterization of two β-mannanases from Trichoderma reesei, J. Biotechnol. 29, 229-242.
    • (1993) J. Biotechnol. , vol.29 , pp. 229-242
    • Stålbrand, H.1    Siika-aho, M.2    Tenkanen, M.3    Viikari, L.4
  • 21
    • 0027109248 scopus 로고
    • Strategies in the crystallization of glycoproteins and protein complexes
    • Stura, E. S., Nemerow, G. R., and Wilson, I. A. (1992) Strategies in the crystallization of glycoproteins and protein complexes, J. Cryst. Growth 122, 273-285.
    • (1992) J. Cryst. Growth , vol.122 , pp. 273-285
    • Stura, E.S.1    Nemerow, G.R.2    Wilson, I.A.3
  • 23
    • 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
  • 24
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z., and Minor, W. (1997) Processing of X-ray diffraction data collected in oscillation mode, Methods Enzymol. 276, 307-326.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 25
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: An automated program for molecular replacement
    • Vagin, A., Teplyakov, A. (1997) MOLREP: An automated program for molecular replacement, J. Appl. Crystallogr. 30, 1022-1025.
    • (1997) J. Appl. Crystallogr. , vol.30 , pp. 1022-1025
    • Vagin, A.1    Teplyakov, A.2
  • 26
    • 0026597444 scopus 로고
    • Free R value: A novel statistical quantity for assessing the accuracy of crystal structures
    • Brünger, A. T. (1992) Free R value: a novel statistical quantity for assessing the accuracy of crystal structures, Nature 355, 472-475.
    • (1992) Nature , vol.355 , pp. 472-475
    • Brünger, A.T.1
  • 28
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and location of the errors in these models
    • Jones, T. A., Zou, J. Y., Cowan, S. W., and Kjeldgaard, M. (1991) Improved methods for building protein models in electron density maps and location of the errors in these models, Acta Crystallogr., Sect. A 47, 110-119.
    • (1991) Acta Crystallogr., Sect. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 29
    • 0346035834 scopus 로고    scopus 로고
    • A cellulose-binding module of the Trichoderma reesei beta-mannanase Man5A increases the mannan-hydrolysis of complex substrates
    • Hägglund, P., Eriksson, T., Collén, A., Nerinckx, W., Claeyssens, M., and Stålbrand, H. (2003) A cellulose-binding module of the Trichoderma reesei beta-mannanase Man5A increases the mannan-hydrolysis of complex substrates, J. Biotechnol. 101, 37-48.
    • (2003) J. Biotechnol. , vol.101 , pp. 37-48
    • Hägglund, P.1    Eriksson, T.2    Collén, A.3    Nerinckx, W.4    Claeyssens, M.5    Stålbrand, H.6
  • 30
    • 0027381121 scopus 로고
    • Stereochemistry, specificity and kinetics of the hydrolysis of reduced cellodextrins by nine cellulases
    • Schou, C., Rasmussen, G., Kaltoft, M. B., Henrissat, B., and Schulein, M. (1993) Stereochemistry, specificity and kinetics of the hydrolysis of reduced cellodextrins by nine cellulases, Eur. J. Biochem. 217, 947-953.
    • (1993) Eur. J. Biochem. , vol.217 , pp. 947-953
    • Schou, C.1    Rasmussen, G.2    Kaltoft, M.B.3    Henrissat, B.4    Schulein, M.5
  • 31
    • 0026540828 scopus 로고
    • Action pattern of xylo-oligosaccharide hydrolysis by Schizophyllum commune xylanase A
    • Bray, M. R., and Clarke, A. J. (1992) Action pattern of xylo-oligosaccharide hydrolysis by Schizophyllum commune xylanase A, Eur. J. Biochem. 204, 191-196.
    • (1992) Eur. J. Biochem. , vol.204 , pp. 191-196
    • Bray, M.R.1    Clarke, A.J.2
  • 32
    • 0030759920 scopus 로고    scopus 로고
    • Structure and mechanism of endo/exocellulase E4 from Thermomonospora fusca
    • Sakon, J., Irwin, D., Wilson, D. B., and Karplus, P. A. (1997) Structure and mechanism of endo/exocellulase E4 from Thermomonospora fusca, Nat. Struct. Biol. 10, 810-818.
    • (1997) Nat. Struct. Biol. , vol.10 , pp. 810-818
    • Sakon, J.1    Irwin, D.2    Wilson, D.B.3    Karplus, P.A.4
  • 33
    • 0027440362 scopus 로고
    • Protein structure comparison by alignment of distance matrices
    • Holm, L., and Sander, C. (1993) Protein structure comparison by alignment of distance matrices, J. Mol. Biol. 233, 123-138.
    • (1993) J. Mol. Biol. , vol.233 , pp. 123-138
    • Holm, L.1    Sander, C.2
  • 35
    • 0028961335 scopus 로고
    • SCOP: A structural classification of proteins database for the investigation of sequences and structures
    • Murzin, A. G., Brenner, S. E., Hubbard, T., and Chothia, C. (1995) SCOP: a structural classification of proteins database for the investigation of sequences and structures, J. Mol. Biol. 247, 536-540.
    • (1995) J. Mol. Biol. , vol.247 , pp. 536-540
    • Murzin, A.G.1    Brenner, S.E.2    Hubbard, T.3    Chothia, C.4
  • 36
    • 1542495429 scopus 로고    scopus 로고
    • Complex structures of Thermoactinomyces vulgaris R-47 alpha-amylase 1 with malto-oligosaccharides demonstrate the role of domain N acting as a starch-binding domain
    • Abe, A., Tonozuka, T., Sakano, Y., and Kamitori, S. (2004) Complex structures of Thermoactinomyces vulgaris R-47 alpha-amylase 1 with malto-oligosaccharides demonstrate the role of domain N acting as a starch-binding domain, J. Mol. Biol. 335, 811-822.
    • (2004) J. Mol. Biol. , vol.335 , pp. 811-822
    • Abe, A.1    Tonozuka, T.2    Sakano, Y.3    Kamitori, S.4
  • 37
    • 25444475386 scopus 로고    scopus 로고
    • Enzymology of endo-1,4-β-mannanases
    • (Whitaker, J. R., Voragen, A. G. J., and Wong, D. S. W., Eds.), Marcel Dekker, Inc., New York
    • Stålbrand, H. (2003) Enzymology of endo-1,4-β-mannanases, in Handbook of food enzymology (Whitaker, J. R., Voragen, A. G. J., and Wong, D. S. W., Eds.), pp 961-969, Marcel Dekker, Inc., New York.
    • (2003) Handbook of Food Enzymology , pp. 961-969
    • Stålbrand, H.1
  • 38
    • 0345389971 scopus 로고    scopus 로고
    • Softwood hemicellulose-degrading enzymes from Aspergillus niger: Purification and properties of a β-mannanase
    • Ademark, P., Varga, A., Medve, J., Harjunpää, V., Drakenberg, T., Tjerneld, F., and Stålbrand, H. (1998) Softwood hemicellulose- degrading enzymes from Aspergillus niger: purification and properties of a β-mannanase, J. Biotechnol. 63, 199-210.
    • (1998) J. Biotechnol. , vol.63 , pp. 199-210
    • Ademark, P.1    Varga, A.2    Medve, J.3    Harjunpää, V.4    Drakenberg, T.5    Tjerneld, F.6    Stålbrand, H.7
  • 39
    • 0028808905 scopus 로고
    • Kinetic and stereochemical studies of manno-oligosaccharide hydrolysis catalysed by β-mannanases from Trichoderma reesei
    • Harjunpää, V., Teleman, A., Siika-aho, M., and Drakenberg, T. (1995) Kinetic and stereochemical studies of manno-oligosaccharide hydrolysis catalysed by β-mannanases from Trichoderma reesei, Eur. J. Biochem. 234, 278-283.
    • (1995) Eur. J. Biochem. , vol.234 , pp. 278-283
    • Harjunpää, V.1    Teleman, A.2    Siika-aho, M.3    Drakenberg, T.4
  • 40
    • 0033040312 scopus 로고    scopus 로고
    • A comparative study of two retaining enzymes of Trichoderma reesei: Transglycosylation of oligosaccharides catalyzed by the cellobiohydrolase I, Cel7A, and the β-mannanase, Man5A
    • Harjunpää, V., Helin, J., Koivula, A., Siika-aho, M., and Drakenberg, T. (1999) A comparative study of two retaining enzymes of Trichoderma reesei: transglycosylation of oligosaccharides catalyzed by the cellobiohydrolase I, Cel7A, and the β-mannanase, Man5A, FEBS Lett. 443, 149-153.
    • (1999) FEBS Lett. , vol.443 , pp. 149-153
    • Harjunpää, V.1    Helin, J.2    Koivula, A.3    Siika-aho, M.4    Drakenberg, T.5
  • 42
    • 0037799892 scopus 로고    scopus 로고
    • The modular architecture of Cellvibrio japonicus mannanases in glycoside hydrolase families 5 and 26 points to differences in their role in mannan degradation
    • Hogg, D., Pell, G., Dupree, P., Goubet, F., Martìn-Orùe, S. M., Armand, S., and Gilbert, H. J. (2003) The modular architecture of Cellvibrio japonicus mannanases in glycoside hydrolase families 5 and 26 points to differences in their role in mannan degradation, Biochem. J. 371, 1027-1043.
    • (2003) Biochem. J. , vol.371 , pp. 1027-1043
    • Hogg, D.1    Pell, G.2    Dupree, P.3    Goubet, F.4    Martìn-Orùe, S.M.5    Armand, S.6    Gilbert, H.J.7
  • 43
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-Pdb viewer: An environment for comparative protein modelling
    • Guex, N., and Peitsch, M. C. (1997) SWISS-MODEL and the Swiss-Pdb viewer: An environment for comparative protein modelling, Electrophoresis 18, 2714-2723.
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 44
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P. J. (1991) MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures, J. Appl. Crystallogr. 24, 949-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 949-950
    • Kraulis, P.J.1
  • 45
    • 0030815133 scopus 로고    scopus 로고
    • RASTER3D version 2: Photorealistic molecular graphics
    • Merritt, E. A., and Bacon, D. J. (1997) RASTER3D version 2: photorealistic molecular graphics. Methods Enzymol. 277, 505-524.
    • (1997) Methods Enzymol. , vol.277 , pp. 505-524
    • Merritt, E.A.1    Bacon, D.J.2
  • 47
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R. A., MacArthur, M. W., Moss, D. S., and Thornton, J. M. (1993) PROCHECK: A program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26, 283-291.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4


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