메뉴 건너뛰기




Volumn 290, Issue 46, 2015, Pages 27438-27450

Sph3 is a glycoside hydrolase required for the biosynthesis of galactosaminogalactan in aspergillus fumigatus

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMISTRY; BIOSYNTHESIS; ENCODING (SYMBOLS); ENZYME ACTIVITY; GENES; HYDROLASES; PROTEINS; SUGARS;

EID: 84946944902     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M115.679050     Document Type: Article
Times cited : (75)

References (70)
  • 1
    • 84942087410 scopus 로고    scopus 로고
    • Biofilm formation by aspergillus fumigatus
    • Kaur, S., and Singh, S. (2014) Biofilm formation by Aspergillus fumigatus. Med. Mycol. 52, 2-9
    • (2014) Med. Mycol. , vol.52 , pp. 2-9
    • Kaur, S.1    Singh, S.2
  • 11
  • 12
    • 48849094142 scopus 로고    scopus 로고
    • In vivo analysis of aspergillus fumigatus developmental gene expression determined by real time reverse transcription-PCR
    • Gravelat, F. N., Doedt, T., Chiang, L. Y., Liu, H., Filler, S. G., Patterson, T. F., and Sheppard, D. C. (2008) In vivo analysis of Aspergillus fumigatus developmental gene expression determined by real time reverse transcription-PCR. Infect. Immun. 76, 3632-3639
    • (2008) Infect. Immun. , vol.76 , pp. 3632-3639
    • Gravelat, F.N.1    Doedt, T.2    Chiang, L.Y.3    Liu, H.4    Filler, S.G.5    Patterson, T.F.6    Sheppard, D.C.7
  • 13
    • 84873107819 scopus 로고    scopus 로고
    • Synthase-dependent exopolysaccharide secretion in gram-negative bacteria
    • Whitney, J. C., and Howell, P. L. (2013) Synthase-dependent exopolysaccharide secretion in Gram-negative bacteria. Trends Microbiol. 21, 63-72
    • (2013) Trends Microbiol. , vol.21 , pp. 63-72
    • Whitney, J.C.1    Howell, P.L.2
  • 14
    • 11144237620 scopus 로고    scopus 로고
    • A crucial role for exopolysaccharide modification in bacterial biofilm formation, immune evasion, and virulence
    • Vuong, C., Kocianova, S., Voyich, J. M., Yao, Y., and Fischer, E. R., DeLeo, F. R., and Otto, M. (2004) A crucial role for exopolysaccharide modification in bacterial biofilm formation, immune evasion, and virulence. J. Biol. Chem. 279, 54881-54886
    • (2004) J. Biol. Chem. , vol.279 , pp. 54881-54886
    • Vuong, C.1    Kocianova, S.2    Voyich, J.M.3    Yao, Y.4    Fischer, E.R.5    DeLeo, F.R.6    Otto, M.7
  • 15
    • 0029888438 scopus 로고    scopus 로고
    • Molecular basis of intercellular adhesion in the biofilmforming staphylococcus epidermidis
    • Heilmann, C., Schweitzer, O., Gerke, C., Vanittanakom, N., Mack, D., and Götz, F. (1996) Molecular basis of intercellular adhesion in the biofilmforming Staphylococcus epidermidis. Mol. Microbiol. 20, 1083-1091
    • (1996) Mol. Microbiol. , vol.20 , pp. 1083-1091
    • Heilmann, C.1    Schweitzer, O.2    Gerke, C.3    Vanittanakom, N.4    Mack, D.5    Götz, F.6
  • 16
    • 73649119152 scopus 로고    scopus 로고
    • Structure, function and contribution of polysaccharide intercellular adhesin (PIA) to staphylococcus epidermidis biofilm formation and pathogenesis of biomaterial-associated infections
    • Rohde, H., Frankenberger, S., Zähringer, U., and Mack, D. (2010) Structure, function and contribution of polysaccharide intercellular adhesin (PIA) to Staphylococcus epidermidis biofilm formation and pathogenesis of biomaterial-associated infections. Eur. J. Cell Biol. 89, 103-111
    • (2010) Eur. J. Cell Biol. , vol.89 , pp. 103-111
    • Rohde, H.1    Frankenberger, S.2    Zähringer, U.3    Mack, D.4
  • 17
    • 33846603188 scopus 로고    scopus 로고
    • Role of a putative polysaccharide locus in bordetella biofilm development
    • Parise, G., Mishra, M., Itoh, Y., Romeo, T., and Deora, R. (2007) Role of a putative polysaccharide locus in Bordetella biofilm development. J. Bacteriol. 189, 750-760
    • (2007) J. Bacteriol. , vol.189 , pp. 750-760
    • Parise, G.1    Mishra, M.2    Itoh, Y.3    Romeo, T.4    Deora, R.5
  • 18
    • 36549050407 scopus 로고    scopus 로고
    • The bordetella bps polysaccharide is critical for biofilm development in the mouse respiratory tract
    • Sloan, G. P., and Love, C. F., Sukumar, N., Mishra, M., and Deora, R. (2007) The Bordetella Bps polysaccharide is critical for biofilm development in the mouse respiratory tract. J. Bacteriol. 189, 8270-8276
    • (2007) J. Bacteriol. , vol.189 , pp. 8270-8276
    • Sloan, G.P.1    Love, C.F.2    Sukumar, N.3    Mishra, M.4    Deora, R.5
  • 19
    • 0035152224 scopus 로고    scopus 로고
    • Biofilm exopolysaccharides: A strong and sticky framework
    • Sutherland, I. (2001) Biofilm exopolysaccharides: a strong and sticky framework. Microbiology 147, 3-9
    • (2001) Microbiology , vol.147 , pp. 3-9
    • Sutherland, I.1
  • 23
    • 84941591667 scopus 로고    scopus 로고
    • BpsB is a poly-β-1, 6-N-acetyl-D-glucosamine deacetylase required for biofilm formation in bordetella bronchiseptica
    • Little, D. J., Milek, S., Bamford, N. C., Ganguly, T., DiFrancesco, B. R., Nitz, M., Deora, R., and Howell, P. L. (2015) BpsB is a poly-β-1, 6-N-acetyl-D-glucosamine deacetylase required for biofilm formation in Bordetella bronchiseptica. J. Biol. Chem. 290, 22827-22840
    • (2015) J. Biol. Chem. , vol.290 , pp. 22827-22840
    • Little, D.J.1    Milek, S.2    Bamford, N.C.3    Ganguly, T.4    DiFrancesco, B.R.5    Nitz, M.6    Deora, R.7    Howell, P.L.8
  • 24
    • 47049129510 scopus 로고    scopus 로고
    • Roles of pgaABCD genes in synthesis, modification, and export of the Escherichia coli biofilm adhesin poly-β-1, 6-N-acetyl-D-glucosamine
    • Itoh, Y., and Rice, J. D., Goller, C., Pannuri, A., Taylor, J., Meisner, J., Beveridge, T. J., and Preston, J. F., 3rd, and Romeo, T. (2008) Roles of pgaABCD genes in synthesis, modification, and export of the Escherichia coli biofilm adhesin poly-β-1, 6-N-acetyl-D-glucosamine. J. Bacteriol. 190, 3670-3680
    • (2008) J. Bacteriol. , vol.190 , pp. 3670-3680
    • Itoh, Y.1    Rice, J.D.2    Goller, C.3    Pannuri, A.4    Taylor, J.5    Meisner, J.6    Beveridge, T.J.7    Preston, J.F.8    Romeo, T.9
  • 26
    • 84865222416 scopus 로고    scopus 로고
    • The structure- and metal-dependent activity of Escherichia coli PgaB provides insight into the partial de-N-acetylation of poly-β-1, 6-N-acetyl-D-glucosamine
    • Little, D. J., Poloczek, J., Whitney, J. C., Robinson, H., Nitz, M., and Howell, P. L. (2012) The structure- and metal-dependent activity of Escherichia coli PgaB provides insight into the partial de-N-acetylation of poly-β-1, 6-N-acetyl-D-glucosamine. J. Biol. Chem. 287, 31126-31137
    • (2012) J. Biol. Chem. , vol.287 , pp. 31126-31137
    • Little, D.J.1    Poloczek, J.2    Whitney, J.C.3    Robinson, H.4    Nitz, M.5    Howell, P.L.6
  • 27
    • 84877994854 scopus 로고    scopus 로고
    • PelA deacetylase activity is required for pel polysaccharide synthesis in pseudomonas aeruginosa
    • Colvin, K. M., Alnabelseya, N., Baker, P., Whitney, J. C., Howell, P. L., and Parsek, M. R. (2013) PelA deacetylase activity is required for Pel polysaccharide synthesis in Pseudomonas aeruginosa. J. Bacteriol. 195, 2329-2339
    • (2013) J. Bacteriol. , vol.195 , pp. 2329-2339
    • Colvin, K.M.1    Alnabelseya, N.2    Baker, P.3    Whitney, J.C.4    Howell, P.L.5    Parsek, M.R.6
  • 29
    • 28844451839 scopus 로고    scopus 로고
    • Role of the pseudomonas fluorescens alginate lyase (AlgL) in clearing the periplasm of alginates not exported to the extracellular environment
    • Bakkevig, K., Sletta, H., Gimmestad, M., Aune, R., Ertesvåg, H., Degnes, K., and Christensen, B. E., Ellingsen, T. E., and Valla, S. (2005) Role of the Pseudomonas fluorescens alginate lyase (AlgL) in clearing the periplasm of alginates not exported to the extracellular environment. J. Bacteriol. 187, 8375-8384
    • (2005) J. Bacteriol. , vol.187 , pp. 8375-8384
    • Bakkevig, K.1    Sletta, H.2    Gimmestad, M.3    Aune, R.4    Ertesvåg, H.5    Degnes, K.6    Christensen, B.E.7    Ellingsen, T.E.8    Valla, S.9
  • 30
    • 25444481824 scopus 로고    scopus 로고
    • Role of an alginate lyase for alginate transport in mucoid pseudomonas aeruginosa
    • Jain, S., and Ohman, D. E. (2005) Role of an alginate lyase for alginate transport in mucoid Pseudomonas aeruginosa. Infection and immunity 73, 6429-6436
    • (2005) Infection and Immunity , vol.73 , pp. 6429-6436
    • Jain, S.1    Ohman, D.E.2
  • 31
    • 84873569415 scopus 로고    scopus 로고
    • Allosteric activation of exopolysaccharide synthesis through cyclic di-GMP-stimulated protein-protein interaction
    • Steiner, S., Lori, C., Boehm, A., and Jenal, U. (2013) Allosteric activation of exopolysaccharide synthesis through cyclic di-GMP-stimulated protein-protein interaction. EMBO J. 32, 354-368
    • (2013) EMBO J. , vol.32 , pp. 354-368
    • Steiner, S.1    Lori, C.2    Boehm, A.3    Jenal, U.4
  • 32
    • 0032540949 scopus 로고    scopus 로고
    • Characterization of the N-acetylglucosaminyltransferase activity involved in the biosynthesis of the staphylococcus epidermidis polysaccharide intercellular adhesin
    • Gerke, C., Kraft, A., Süssmuth, R., Schweitzer, O., and Götz, F. (1998) Characterization of the N-acetylglucosaminyltransferase activity involved in the biosynthesis of the Staphylococcus epidermidis polysaccharide intercellular adhesin. J. Biol. Chem. 273, 18586-18593
    • (1998) J. Biol. Chem. , vol.273 , pp. 18586-18593
    • Gerke, C.1    Kraft, A.2    Süssmuth, R.3    Schweitzer, O.4    Götz, F.5
  • 33
    • 0024967696 scopus 로고
    • Developmentally regulated late mRNAs in the encystment of physarum polycephalum plasmodia
    • Savard, L., Laroche, A., Lemieux, G., and Pallotta, D. (1989) Developmentally regulated late mRNAs in the encystment of Physarum polycephalum plasmodia. Biochim. Biophys. Acta 1007, 264-269
    • (1989) Biochim. Biophys. Acta , vol.1007 , pp. 264-269
    • Savard, L.1    Laroche, A.2    Lemieux, G.3    Pallotta, D.4
  • 34
    • 80053345905 scopus 로고    scopus 로고
    • SignalP 4.0: Discriminating signal peptides from transmembrane regions
    • Petersen, T. N., Brunak, S., von Heijne, G., and Nielsen, H. (2011) SignalP 4.0: discriminating signal peptides from transmembrane regions. Nat. Methods 8, 785-786
    • (2011) Nat. Methods , vol.8 , pp. 785-786
    • Petersen, T.N.1    Brunak, S.2    Von Heijne, G.3    Nielsen, H.4
  • 36
    • 63849246525 scopus 로고    scopus 로고
    • Protein structure prediction on the web: A case study using the phyre server
    • Kelley, L. A., and Sternberg, M. J. (2009) Protein structure prediction on the Web: a case study using the Phyre server. Nat. Protoc. 4, 363-371
    • (2009) Nat. Protoc. , vol.4 , pp. 363-371
    • Kelley, L.A.1    Sternberg, M.J.2
  • 37
    • 0035910270 scopus 로고    scopus 로고
    • Predicting transmembrane protein topology with a hidden Markov model: Application to complete genomes
    • Krogh, A., Larsson, B., von Heijne, G., and Sonnhammer, E. L. (2001) Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes. J. Mol. Biol. 305, 567-580
    • (2001) J. Mol. Biol. , vol.305 , pp. 567-580
    • Krogh, A.1    Larsson, B.2    Von Heijne, G.3    Sonnhammer, E.L.4
  • 38
    • 2142657817 scopus 로고    scopus 로고
    • A combined transmembrane topology and signal peptide prediction method
    • Käll, L., Krogh, A., and Sonnhammer, E. L. (2004) A combined transmembrane topology and signal peptide prediction method. J. Mol. Biol. 338, 1027-1036
    • (2004) J. Mol. Biol. , vol.338 , pp. 1027-1036
    • Käll, L.1    Krogh, A.2    Sonnhammer, E.L.3
  • 41
    • 84858131811 scopus 로고    scopus 로고
    • Targeted gene deletion in aspergillus fumigatus using the hygromycin-resistance split-marker approach
    • Gravelat, F. N., Askew, D. S., and Sheppard, D. C. (2012) Targeted gene deletion in Aspergillus fumigatus using the hygromycin-resistance split-marker approach. Methods Mol. Biol. 845, 119-130
    • (2012) Methods Mol. Biol. , vol.845 , pp. 119-130
    • Gravelat, F.N.1    Askew, D.S.2    Sheppard, D.C.3
  • 42
    • 0034793650 scopus 로고    scopus 로고
    • Structure of E. Coli 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase reveals similarity to the purine nucleoside phosphorylases
    • Lee, J. E., and Cornell, K. A., Riscoe, M. K., and Howell, P. L. (2001) Structure of E. coli 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase reveals similarity to the purine nucleoside phosphorylases. Structure 9, 941-953
    • (2001) Structure , vol.9 , pp. 941-953
    • Lee, J.E.1    Cornell, K.A.2    Riscoe, M.K.3    Howell, P.L.4
  • 43
    • 0031059866 scopus 로고    scopus 로고
    • Processing of x-ray diffraction data collection in oscillation mode
    • Otwinowski, Z., and Minor, W. (1997) Processing of x-ray diffraction data collection in oscillation mode. Methods Enzymol. 276, 307-326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 47
  • 48
    • 77954288774 scopus 로고    scopus 로고
    • Dali server: Conservation mapping in 3D
    • Holm, L., and Rosenström, P. (2010) Dali server: conservation mapping in 3D. Nucleic Acids Res. 38, W545-W549
    • (2010) Nucleic Acids Res. , vol.38 , pp. W545-W549
    • Holm, L.1    Rosenström, P.2
  • 49
    • 77954257799 scopus 로고    scopus 로고
    • ConSurf 2010: Calculating evolutionary conservation in sequence and structure of proteins and nucleic acids
    • Ashkenazy, H., Erez, E., Martz, E., Pupko, T., and Ben-Tal, N. (2010) ConSurf 2010: calculating evolutionary conservation in sequence and structure of proteins and nucleic acids. Nucleic Acids Res. 38, W529-W533
    • (2010) Nucleic Acids Res. , vol.38 , pp. W529-W533
    • Ashkenazy, H.1    Erez, E.2    Martz, E.3    Pupko, T.4    Ben-Tal, N.5
  • 50
    • 2542445427 scopus 로고    scopus 로고
    • ConSurf: Identification of functional regions in proteins by surface-mapping of phylogenetic information
    • Glaser, F., Pupko, T., Paz, I., Bell, R. E., Bechor-Shental, D., Martz, E., and Ben-Tal, N. (2003) ConSurf: identification of functional regions in proteins by surface-mapping of phylogenetic information. Bioinformatics 19, 163-164
    • (2003) Bioinformatics , vol.19 , pp. 163-164
    • Glaser, F.1    Pupko, T.2    Paz, I.3    Bell, R.E.4    Bechor-Shental, D.5    Martz, E.6    Ben-Tal, N.7
  • 51
    • 23144448512 scopus 로고    scopus 로고
    • ConSurf 2005: The projection of evolutionary conservation scores of residues on protein structures
    • Landau, M., Mayrose, I., Rosenberg, Y., Glaser, F., Martz, E., Pupko, T., and Ben-Tal, N. (2005) ConSurf 2005: the projection of evolutionary conservation scores of residues on protein structures. Nucleic Acids Res. 33, W299-W302
    • (2005) Nucleic Acids Res. , vol.33 , pp. W299-W302
    • Landau, M.1    Mayrose, I.2    Rosenberg, Y.3    Glaser, F.4    Martz, E.5    Pupko, T.6    Ben-Tal, N.7
  • 53
    • 0035137275 scopus 로고    scopus 로고
    • Colorimetric method for the determination of lipoxygenase activity
    • Anthon, G. E., and Barrett, D. M. (2001) Colorimetric method for the determination of lipoxygenase activity. J. Agric. Food Chem. 49, 32-37
    • (2001) J. Agric. Food Chem. , vol.49 , pp. 32-37
    • Anthon, G.E.1    Barrett, D.M.2
  • 54
    • 78149297086 scopus 로고    scopus 로고
    • CAZymes analysis toolkit (CAT): Web service for searching and analyzing carbohydrate-active enzymes in a newly sequenced organism using CAZy database
    • Park, B. H., Karpinets, T. V., and Syed., M. H., Leuze, M. R., and Uberbacher, E. C. (2010) CAZymes Analysis Toolkit (CAT): web service for searching and analyzing carbohydrate-active enzymes in a newly sequenced organism using CAZy database. Glycobiology 20, 1574-1584
    • (2010) Glycobiology , vol.20 , pp. 1574-1584
    • Park, B.H.1    Karpinets, T.V.2    Syed, M.H.3    Leuze, M.R.4    Uberbacher, E.C.5
  • 55
    • 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
  • 56
    • 0030733350 scopus 로고    scopus 로고
    • Structural and sequence-based classification of glycoside hydrolases
    • Henrissat, B., and Davies, G. (1997) Structural and sequence-based classification of glycoside hydrolases. Curr. Opin. Struct. Biol. 7, 637-644
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 637-644
    • Henrissat, B.1    Davies, G.2
  • 57
    • 0035949643 scopus 로고    scopus 로고
    • High resolution structural analyses of mutant chitinase A complexes with substrates provide new insight into the mechanism of catalysis
    • Papanikolau, Y., Prag, G., Tavlas, G., Vorgias, C. E., and Oppenheim, A. B., and Petratos, K. (2001) High resolution structural analyses of mutant chitinase A complexes with substrates provide new insight into the mechanism of catalysis. Biochemistry 40, 11338-11343
    • (2001) Biochemistry , vol.40 , pp. 11338-11343
    • Papanikolau, Y.1    Prag, G.2    Tavlas, G.3    Vorgias, C.E.4    Oppenheim, A.B.5    Petratos, K.6
  • 59
    • 33645735070 scopus 로고    scopus 로고
    • Structural insights into the mechanism and inhibition of eukaryotic O-glcnac hydrolysis
    • Rao, F. V., Dorfmueller, H. C., Villa, F., Allwood, M., Eggleston, I. M., and van Aalten, D. M. (2006) Structural insights into the mechanism and inhibition of eukaryotic O-GlcNAc hydrolysis. EMBO J. 25, 1569-1578
    • (2006) EMBO J. , vol.25 , pp. 1569-1578
    • Rao, F.V.1    Dorfmueller, H.C.2    Villa, F.3    Allwood, M.4    Eggleston, I.M.5    Van Aalten, D.M.6
  • 61
    • 0347683443 scopus 로고    scopus 로고
    • The crystal structure of the calystegia sepium agglutinin reveals a novel quaternary arrangement of lectin subunits with a β-prism fold
    • Bourne, Y., Roig-Zamboni, V., Barre, A., and Peumans, W. J., Astoul, C. H., Van Damme, E. J., and Rougé, P. (2004) The crystal structure of the Calystegia sepium agglutinin reveals a novel quaternary arrangement of lectin subunits with a β-prism fold. J. Biol. Chem. 279, 527-533
    • (2004) J. Biol. Chem. , vol.279 , pp. 527-533
    • Bourne, Y.1    Roig-Zamboni, V.2    Barre, A.3    Peumans, W.J.4    Astoul, C.H.5    Van Damme, E.J.6    Rougé, P.7
  • 62
    • 84861165112 scopus 로고    scopus 로고
    • Chapter 8: The crystallization and structural analysis of cellulases (and other glycoside hydrolases): Strategies and tactics
    • Roberts, S. M., and Davies, G. J. (2012) Chapter 8: The crystallization and structural analysis of cellulases (and other glycoside hydrolases): strategies and tactics. Methods Enzymol. 510, 141-168
    • (2012) Methods Enzymol. , vol.510 , pp. 141-168
    • Roberts, S.M.1    Davies, G.J.2
  • 63
    • 84929282872 scopus 로고    scopus 로고
    • Listeria monocytogenes exopolysaccharide: Origin, structure, biosynthetic machinery and c-di-GMP-dependent regulation
    • Köseoglu, V. K., Heiss, C., Azadi, P., Topchiy, E., Güvener, Z. T., Lehmann, T. E., and Miller, K. W., and Gomelsky, M. (2015) Listeria monocytogenes exopolysaccharide: origin, structure, biosynthetic machinery and c-di-GMP-dependent regulation. Mol. Microbiol. 96, 728-743
    • (2015) Mol. Microbiol. , vol.96 , pp. 728-743
    • Köseoglu, V.K.1    Heiss, C.2    Azadi, P.3    Topchiy, E.4    Güvener, Z.T.5    Lehmann, T.E.6    Miller, K.W.7    Gomelsky, M.8
  • 64
    • 79955969731 scopus 로고    scopus 로고
    • Apo- and cellopentaose-bound structures of the bacterial cellulose synthase subunit BcsZ
    • Mazur, O., and Zimmer, J. (2011) Apo- and cellopentaose-bound structures of the bacterial cellulose synthase subunit BcsZ. J. Biol. Chem. 286, 17601-17606
    • (2011) J. Biol. Chem. , vol.286 , pp. 17601-17606
    • Mazur, O.1    Zimmer, J.2
  • 65
    • 0031587296 scopus 로고    scopus 로고
    • The crystal structure of the catalytic core domain of endoglucanase I from trichoderma reesei at 3.6 A resolution, and a comparison with related enzymes
    • Kleywegt, G. J., and Zou, J. Y., Divne, C., and Davies, G. J., Sinning, I., Stâhlberg, J., Reinikainen, T., Srisodsuk, M., Teeri, T. T., and Jones, T. A. (1997) The crystal structure of the catalytic core domain of endoglucanase I from Trichoderma reesei at 3.6 A resolution, and a comparison with related enzymes. J. Mol. Biol. 272, 383-397
    • (1997) J. Mol. Biol. , vol.272 , pp. 383-397
    • Kleywegt, G.J.1    Zou, J.Y.2    Divne, C.3    Davies, G.J.4    Sinning, I.5    Stâhlberg, J.6    Reinikainen, T.7    Srisodsuk, M.8    Teeri, T.T.9    Jones, T.A.10
  • 67
    • 0029645404 scopus 로고
    • Structures and mechanisms of glycosyl hydrolases
    • Davies, G., and Henrissat, B. (1995) Structures and mechanisms of glycosyl hydrolases. Structure 3, 853-859
    • (1995) Structure , vol.3 , pp. 853-859
    • Davies, G.1    Henrissat, B.2
  • 68
    • 84860188732 scopus 로고    scopus 로고
    • Biosynthesis of the pseudomonas aeruginosa extracellular polysaccharides, alginate, pel, and psl
    • Franklin, M. J., and Nivens, D. E., Weadge, J. T., and Howell, P. L. (2011) Biosynthesis of the Pseudomonas aeruginosa extracellular polysaccharides, Alginate, Pel, and Psl. Front. Microbiol. 2, 167
    • (2011) Front. Microbiol. , vol.2 , pp. 167
    • Franklin, M.J.1    Nivens, D.E.2    Weadge, J.T.3    Howell, P.L.4
  • 69
    • 0036399960 scopus 로고    scopus 로고
    • Effects of endogenous endo-β-1, 4-glucanase on cellulose biosynthesis in acetobacterxylinum ATCC23769
    • Kawano, S., Tajima, K., Kono, H., Erata, T., Munekata, M., and Takai, M. (2002) Effects of endogenous endo-β-1, 4-glucanase on cellulose biosynthesis in Acetobacterxylinum ATCC23769. J. Biosci. Bioeng. 94, 275-281
    • (2002) J. Biosci. Bioeng. , vol.94 , pp. 275-281
    • Kawano, S.1    Tajima, K.2    Kono, H.3    Erata, T.4    Munekata, M.5    Takai, M.6
  • 70
    • 0032200058 scopus 로고    scopus 로고
    • Evidence that a β-1, 4-endoglucanase secreted by acetobacter xylinum plays an essential role for the formation of cellulose fiber
    • Koo, H. M., and Song, S. H., Pyun, Y. R., and Kim, Y. S. (1998) Evidence that a β-1, 4-endoglucanase secreted by Acetobacter xylinum plays an essential role for the formation of cellulose fiber. Biosci. Biotechnol. Biochem. 62, 2257-2259
    • (1998) Biosci. Biotechnol. Biochem. , vol.62 , pp. 2257-2259
    • Koo, H.M.1    Song, S.H.2    Pyun, Y.R.3    Kim, Y.S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.