메뉴 건너뛰기




Volumn 289, Issue 15, 2014, Pages 10843-10852

Structural and biochemical analyses of glycoside hydrolase family 26 β-mannanase from a symbiotic protist of the termite reticulitermes speratus

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMISTRY; BIOLOGY;

EID: 84898657935     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.555383     Document Type: Article
Times cited : (25)

References (38)
  • 1
    • 34249816507 scopus 로고    scopus 로고
    • Mitochondrial genomic comparisons of the subterranean termites from the genus Reticulitermes (Insecta: Isoptera: Rhinotermitidae)
    • Cameron, S. L., and Whiting, M. F. (2007) Mitochondrial genomic comparisons of the subterranean termites from the genus Reticulitermes (Insecta: Isoptera: Rhinotermitidae). Genome 50, 188-202
    • (2007) Genome , vol.50 , pp. 188-202
    • Cameron, S.L.1    Whiting, M.F.2
  • 3
    • 0037364788 scopus 로고    scopus 로고
    • Termite symbiotic systems: Efficient bio-recycling of lignocellulose
    • Ohkuma, M. (2003) Termite symbiotic systems: efficient bio-recycling of lignocellulose. Appl. Microbiol. Biotechnol. 61, 1-9
    • (2003) Appl. Microbiol. Biotechnol. , vol.61 , pp. 1-9
    • Ohkuma, M.1
  • 5
    • 77449097393 scopus 로고    scopus 로고
    • Cellulolytic systems in insects
    • Watanabe, H., and Tokuda, G. (2010) Cellulolytic systems in insects. Annu. Rev. Entomol. 55, 609-632
    • (2010) Annu. Rev. Entomol. , vol.55 , pp. 609-632
    • Watanabe, H.1    Tokuda, G.2
  • 6
    • 0002956082 scopus 로고
    • Studies on the nutrition of zootermopsis II: The relative Importance of the termite and the protozoa in wood digestion
    • Hungate, R. E. (1938) Studies on the nutrition of zootermopsis II: The relative Importance of the termite and the protozoa in wood digestion. Ecology 19, 1-25
    • (1938) Ecology , vol.19 , pp. 1-25
    • Hungate, R.E.1
  • 7
    • 74549126675 scopus 로고    scopus 로고
    • An overview of second generation biofuel technologies
    • Sims, R. E., Mabee, W., Saddler, J. N., and Taylor, M. (2010) An overview of second generation biofuel technologies. Bioresour. Technol. 101, 1570-1580
    • (2010) Bioresour. Technol. , vol.101 , pp. 1570-1580
    • Sims, R.E.1    Mabee, W.2    Saddler, J.N.3    Taylor, M.4
  • 8
    • 24044550811 scopus 로고
    • Cellulose digestion system in the termite, Reticulitermes speratus (Kolbe). II. Ultra-structural changes related to the ingestion and digestion of cellulose by the flagellate, Trichonympha agilis
    • Yamaoka, I., and Nagatani, Y. (1977) Cellulose digestion system in the termite, Reticulitermes speratus (Kolbe). II. Ultra-structural changes related to the ingestion and digestion of cellulose by the flagellate, Trichonympha agilis. Zool. Mag. 86, 34-42
    • (1977) Zool. Mag. , vol.86 , pp. 34-42
    • Yamaoka, I.1    Nagatani, Y.2
  • 9
    • 0002973531 scopus 로고
    • Acetogenesis from carbon dioxide in termite guts in
    • Springer US, New York
    • Breznak, J. A. (1994) Acetogenesis from carbon dioxide in termite guts in Acetogenesis, pp. 551-565 Springer US, New York
    • (1994) Acetogenesis , pp. 551-565
    • Breznak, J.A.1
  • 10
    • 79953688970 scopus 로고    scopus 로고
    • Toward the functional analysis of uncultivable, symbiotic microorganisms in the termite gut
    • Hongoh, Y. (2011) Toward the functional analysis of uncultivable, symbiotic microorganisms in the termite gut. Cell Mol. Life Sci. 68, 1311-1325
    • (2011) Cell Mol. Life Sci. , vol.68 , pp. 1311-1325
    • Hongoh, Y.1
  • 11
    • 33847700188 scopus 로고    scopus 로고
    • Environmental cDNA analysis of the genes involved in lignocellulose digestion in the symbiotic protist community of Reticulitermes speratus
    • Todaka, N., Moriya, S., Saita, K., Hondo, T., Kiuchi, I., Takasu, H., Ohkuma, M., Piero, C., Hayashizaki, Y., and Kudo, T. (2007) Environmental cDNA analysis of the genes involved in lignocellulose digestion in the symbiotic protist community of Reticulitermes speratus. FEMS Microbiol. Ecol. 59, 592-599
    • (2007) FEMS Microbiol. Ecol. , vol.59 , pp. 592-599
    • Todaka, N.1    Moriya, S.2    Saita, K.3    Hondo, T.4    Kiuchi, I.5    Takasu, H.6    Ohkuma, M.7    Piero, C.8    Hayashizaki, Y.9    Kudo, T.10
  • 12
    • 42649129680 scopus 로고    scopus 로고
    • An overview of mannan structure and mannan-degrading enzyme systems
    • Moreira, L. R., and Filho, E. X. (2008) An overview of mannan structure and mannan-degrading enzyme systems. Appl. Microbiol. Biotechnol. 79, 165-178
    • (2008) Appl. Microbiol. Biotechnol. , vol.79 , pp. 165-178
    • Moreira, L.R.1    Filho, E.X.2
  • 14
    • 0037436543 scopus 로고    scopus 로고
    • Isolation and characterization of O-acetylated glucomannans from aspen and birch wood
    • Teleman, A., Nordström, M., Tenkanen, M., Jacobs, A., and Dahlman, O. (2003) Isolation and characterization of O-acetylated glucomannans from aspen and birch wood. Carbohydr. Res. 338, 525-534
    • (2003) Carbohydr. Res. , vol.338 , pp. 525-534
    • Teleman, A.1    Nordström, M.2    Tenkanen, M.3    Jacobs, A.4    Dahlman, O.5
  • 16
    • 25444475768 scopus 로고    scopus 로고
    • The structure and characterization of a modular endo-β-1,4-mannanase from Cellulomonas fimi
    • Le Nours, J., Anderson, L., Stoll, D., Stalbrand, H., and Lo Leggio, L. (2005) The structure and characterization of a modular endo-β-1,4-mannanase from Cellulomonas fimi. Biochemistry 44, 12700-12708
    • (2005) Biochemistry , vol.44 , pp. 12700-12708
    • Le Nours, J.1    Anderson, L.2    Stoll, D.3    Stalbrand, H.4    Lo Leggio, L.5
  • 17
    • 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
  • 18
    • 77955963083 scopus 로고    scopus 로고
    • Comparative analyses of two thermophilic enzymes exhibiting bothβ-1,4 mannosidic andβ-1,4 glucosidic cleavage activities from Caldanaerobius polysaccharolyticus
    • Han, Y., Dodd, D., Hespen, C. W., Ohene-Adjei, S., Schroeder, C. M., Mackie, R. I., and Cann, I. K. (2010) Comparative analyses of two thermophilic enzymes exhibiting bothβ-1,4 mannosidic andβ-1,4 glucosidic cleavage activities from Caldanaerobius polysaccharolyticus. J. Bacteriol. 192, 4111-4121
    • (2010) J. Bacteriol. , vol.192 , pp. 4111-4121
    • Han, Y.1    Dodd, D.2    Hespen, C.W.3    Ohene-Adjei, S.4    Schroeder, C.M.5    Mackie, R.I.6    Cann, I.K.7
  • 20
    • 0037008171 scopus 로고    scopus 로고
    • Substrate distortion by a-mannanase: Snapshots of the Michaelis and covalent-intermediate complexes suggest a B(2,5) conformation for the transition state
    • Ducros, V. M., Zechel, D. L., Murshudov, G. N., Gilbert, H. J., Szabó, L., Stoll, D., Withers, S. G., and Davies, G. J. (2002) Substrate distortion by a-mannanase: snapshots of the Michaelis and covalent-intermediate complexes suggest a B(2,5) conformation for the transition state. Angew. Chem. Int. Ed Engl. 41, 2824-2827
    • (2002) Angew. Chem. Int. Ed Engl. , vol.41 , pp. 2824-2827
    • Ducros, V.M.1    Zechel, D.L.2    Murshudov, G.N.3    Gilbert, H.J.4    Szabó, L.5    Stoll, D.6    Withers, S.G.7    Davies, G.J.8
  • 21
    • 57749089774 scopus 로고    scopus 로고
    • The Cellvibrio japonicus mannanase CjMan26C displays a unique exo-mode of action that is conferred by subtle changes to the distal region of the active site
    • Cartmell, A., Topakas, E., Ducros, V. M., Suits, M. D., Davies, G. J., and Gilbert, H. J. (2008) The Cellvibrio japonicus mannanase CjMan26C displays a unique exo-mode of action that is conferred by subtle changes to the distal region of the active site. J. Biol. Chem. 283, 34403-34413
    • (2008) J. Biol. Chem. , vol.283 , pp. 34403-34413
    • Cartmell, A.1    Topakas, E.2    Ducros, V.M.3    Suits, M.D.4    Davies, G.J.5    Gilbert, H.J.6
  • 22
    • 84857822424 scopus 로고    scopus 로고
    • Expression and one-step purification of recombinant proteins using an alternative episomal vector for the expression of N-tagged heterologous proteins in Pichia pastoris
    • Uchima, C. A., and Arioka, M. (2012) Expression and one-step purification of recombinant proteins using an alternative episomal vector for the expression of N-tagged heterologous proteins in Pichia pastoris. Biosci. Biotechnol. Biochem. 76, 368-371
    • (2012) Biosci. Biotechnol. Biochem. , vol.76 , pp. 368-371
    • Uchima, C.A.1    Arioka, M.2
  • 23
    • 0022255318 scopus 로고
    • Determination of reducing sugars in the nanomole range with tetrazolium blue
    • Jue, C. K., and Lipke, P. N. (1985) Determination of reducing sugars in the nanomole range with tetrazolium blue. J. Biochem. Biophys. Methods 11, 109-115
    • (1985) J. Biochem. Biophys. Methods , vol.11 , pp. 109-115
    • Jue, C.K.1    Lipke, P.N.2
  • 24
    • 0030806312 scopus 로고    scopus 로고
    • Cellulose and xylan utilisation in the lower termite Reticulitermes speratus
    • Inoue, T., Murashima, K., Azuma, J., Sugimoto, A., and Slaytor, M. (1997) Cellulose and xylan utilisation in the lower termite Reticulitermes speratus. J. Insect Physiol. 43, 235-242
    • (1997) J. Insect Physiol. , vol.43 , pp. 235-242
    • Inoue, T.1    Murashima, K.2    Azuma, J.3    Sugimoto, A.4    Slaytor, M.5
  • 25
    • 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
  • 28
  • 29
    • 84877890782 scopus 로고    scopus 로고
    • Structural and biochemical analyses of glycoside hydrolase families 5 and 26β-(1,4)-mannanases from Podospora anserina reveal differences upon manno-oligosaccharide catalysis
    • Couturier, M., Roussel, A., Rosengren, A., Leone, P., Stalbrand, H., and Berrin, J. G. (2013) Structural and biochemical analyses of glycoside hydrolase families 5 and 26β-(1,4)-mannanases from Podospora anserina reveal differences upon manno-oligosaccharide catalysis. J. Biol. Chem. 288, 14624-14635
    • (2013) J. Biol. Chem. , vol.288 , pp. 14624-14635
    • Couturier, M.1    Roussel, A.2    Rosengren, A.3    Leone, P.4    Stalbrand, H.5    Berrin, J.G.6
  • 30
    • 79251613225 scopus 로고    scopus 로고
    • Podospora anserina hemicellulases potentiate the Trichoderma reesei secretome for saccharification of lignocellulosic biomass
    • Couturier, M., Haon, M., Coutinho, P. M., Henrissat, B., Lesage-Meessen, L., and Berrin, J. G. (2011) Podospora anserina hemicellulases potentiate the Trichoderma reesei secretome for saccharification of lignocellulosic biomass. Appl. Environ. Microbiol. 77, 237-246
    • (2011) Appl. Environ. Microbiol. , vol.77 , pp. 237-246
    • Couturier, M.1    Haon, M.2    Coutinho, P.M.3    Henrissat, B.4    Lesage-Meessen, L.5    Berrin, J.G.6
  • 31
    • 84871881296 scopus 로고    scopus 로고
    • Expression and characterization of a bifidobacterium adolescentisβ- mannanase carrying mannan-binding and cell association motifs
    • Kulcinskaja, E., Rosengren, A., Ibrahim, R., Kolenová, K., and Stalbrand, H. (2013) Expression and characterization of a bifidobacterium adolescentisβ-mannanase carrying mannan-binding and cell association motifs. Appl. Environ. Microbiol. 79, 133-140
    • (2013) Appl. Environ. Microbiol. , vol.79 , pp. 133-140
    • Kulcinskaja, E.1    Rosengren, A.2    Ibrahim, R.3    Kolenová, K.4    Stalbrand, H.5
  • 32
    • 77950682492 scopus 로고    scopus 로고
    • Efficient recombinant expression and secretion of a thermostable GH26 mannan endo-1,4-β-mannosidase from Bacillus licheniformis in Escherichia coli
    • Songsiriritthigul, C., Buranabanyat, B., Haltrich, D., and Yamabhai, M. (2010) Efficient recombinant expression and secretion of a thermostable GH26 mannan endo-1,4-β-mannosidase from Bacillus licheniformis in Escherichia coli. Microb. Cell Fact. 9, 20-2859-9-20
    • (2010) Microb. Cell Fact. , vol.9 , pp. 202859-202920
    • Songsiriritthigul, C.1    Buranabanyat, B.2    Haltrich, D.3    Yamabhai, M.4
  • 33
    • 8744220594 scopus 로고    scopus 로고
    • The crystal structure of an oxidatively stable subtilisin-like alkaline serine protease, KP-43, with a C-terminalβ-barrel domain
    • Nonaka, T., Fujihashi, M., Kita, A., Saeki, K., Ito, S., Horikoshi, K., and Miki, K. (2004) The crystal structure of an oxidatively stable subtilisin-like alkaline serine protease, KP-43, with a C-terminalβ-barrel domain. J. Biol. Chem. 279, 47344-47351
    • (2004) J. Biol. Chem. , vol.279 , pp. 47344-47351
    • Nonaka, T.1    Fujihashi, M.2    Kita, A.3    Saeki, K.4    Ito, S.5    Horikoshi, K.6    Miki, K.7
  • 34
    • 0029039266 scopus 로고
    • The termite gut microflora as an oxygen sink: Microelectrode determination of oxygen and pH gradients in guts of lower and higher termites
    • Brune, A., Emerson, D., and Breznak, J. A. (1995) The termite gut microflora as an oxygen sink: microelectrode determination of oxygen and pH gradients in guts of lower and higher termites. Appl. Environ. Microbiol. 61, 2681-2687
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 2681-2687
    • Brune, A.1    Emerson, D.2    Breznak, J.A.3
  • 35
    • 0002125451 scopus 로고
    • Cellulose digestion system in the termite, Reticulitermes speratus (Kolbe). I. Producing sites and physiological significance of two kinds of cellulase in the worker
    • Yamaoka, I., and Nagatani, Y. (1975) Cellulose digestion system in the termite, Reticulitermes speratus (Kolbe). I. Producing sites and physiological significance of two kinds of cellulase in the worker. Zool. Mag. 84, 23-29
    • (1975) Zool. Mag. , vol.84 , pp. 23-29
    • Yamaoka, I.1    Nagatani, Y.2
  • 36
    • 17044412101 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a cellulase gene from a symbiotic protist of the lower termite, Coptotermes formosanus
    • Inoue, T., Moriya, S., Ohkuma, M., and Kudo, T. (2005) Molecular cloning and characterization of a cellulase gene from a symbiotic protist of the lower termite, Coptotermes formosanus. Gene 349, 67-75
    • (2005) Gene , vol.349 , pp. 67-75
    • Inoue, T.1    Moriya, S.2    Ohkuma, M.3    Kudo, T.4
  • 37
    • 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
  • 38
    • 43449132076 scopus 로고    scopus 로고
    • From structure to function: Insights into the catalytic substrate specificity and thermostability displayed by Bacillus subtilis mannanase BCman
    • Yan, X. X., An, X. M., Gui, L. L., and Liang, D. C. (2008) From structure to function: insights into the catalytic substrate specificity and thermostability displayed by Bacillus subtilis mannanase BCman. J. Mol. Biol. 379, 535-544
    • (2008) J. Mol. Biol. , vol.379 , pp. 535-544
    • Yan, X.X.1    An, X.M.2    Gui, L.L.3    Liang, D.C.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.