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Volumn 289, Issue 11, 2014, Pages 7335-7348

Characterization of all family-9 glycoside hydrolases synthesized by the cellulosome-producing bacterium Clostridium cellulolyticum

Author keywords

[No Author keywords available]

Indexed keywords

CELLULOSE; ESCHERICHIA COLI; PURIFICATION; SUBSTRATES;

EID: 84896276890     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.545046     Document Type: Article
Times cited : (71)

References (44)
  • 2
    • 84866500048 scopus 로고    scopus 로고
    • Evolution, substrate specificity and subfamily classification of glycoside hydrolase family-5 (GH5)
    • Aspeborg, H., Coutinho, P. M., Wang, Y., Brumer, H., 3rd, and Henrissat, B. (2012) Evolution, substrate specificity and subfamily classification of glycoside hydrolase family-5 (GH5). BMC Evol. Biol. 12, 186
    • (2012) BMC Evol. Biol. , vol.12 , pp. 186
    • Aspeborg, H.1    Coutinho, P.M.2    Wang, Y.3    Brumer III, H.4    Henrissat, B.5
  • 3
    • 0024419181 scopus 로고
    • Cellulase families revealed by hydrophobic cluster analysis
    • DOI 10.1016/0378-1119(89)90339-9
    • Henrissat, B., Claeyssens, M., Tomme, P., Lemesle, L., and Mornon, J. P. (1989) Cellulase families revealed by hydrophobic cluster analysis. Gene 81, 83-95 (Pubitemid 19227537)
    • (1989) Gene , vol.81 , Issue.1 , pp. 83-95
    • Henrissat, B.1    Claeyssens, M.2    Tomme, P.3    Lemesle, L.4    Mornon, J.-P.5
  • 4
    • 79952551796 scopus 로고    scopus 로고
    • Elucidation of exo-β-D-glucosaminidase activity of a family 9 glycoside hydrolase (PBPRA0520) from Photobacterium profundum SS9
    • Honda, Y., Shimaya, N., Ishisaki, K., Ebihara, M., and Taniguchi, H. (2011) Elucidation of exo-β-D-glucosaminidase activity of a family 9 glycoside hydrolase (PBPRA0520) from Photobacterium profundum SS9. Glycobiology 21, 503-511
    • (2011) Glycobiology , vol.21 , pp. 503-511
    • Honda, Y.1    Shimaya, N.2    Ishisaki, K.3    Ebihara, M.4    Taniguchi, H.5
  • 5
    • 0037226350 scopus 로고    scopus 로고
    • Characterization of a cellulase containing a family 30 carbohydrate-binding module (CBM) derived from Clostridium thermocellum CelJ: Importance of the CBM to cellulose hydrolysis
    • DOI 10.1128/JB.185.2.504-512.2003
    • Arai, T., Araki, R., Tanaka, A., Karita, S., Kimura, T., Sakka, K., and Ohmiya, K. (2003) Characterization of a cellulase containing a family 30 carbohydrate-binding module (CBM) derived from Clostridium thermocellum CelJ: importance of the CBM to cellulose hydrolysis. J. Bacteriol. 185, 504-512 (Pubitemid 36070477)
    • (2003) Journal of Bacteriology , vol.185 , Issue.2 , pp. 504-512
    • Arai, T.1    Araki, R.2    Tanaka, A.3    Karita, S.4    Kimura, T.5    Sakka, K.6    Ohmiya, K.7
  • 6
    • 0037213678 scopus 로고    scopus 로고
    • Gene cloning, sequencing, and characterization of a family 9 endoglucanase (CelA) with an unusual pattern of activity from the thermoacidophile Alicyclobacillus acidocaldarius ATCC27009
    • DOI 10.1007/s00253-002-1131-4
    • Eckert, K., Zielinski, F., Lo Leggio, L., and Schneider, E. (2002) Gene cloning, sequencing, and characterization of a family 9 endoglucanase (CelA) with an unusual pattern of activity from the thermoacidophile Alicyclobacillus acidocaldarius ATCC27009. Appl. Microbiol. Biotechnol. 60, 428-436 (Pubitemid 35435812)
    • (2003) Applied Microbiology and Biotechnology , vol.60 , Issue.4 , pp. 428-436
    • Eckert, K.1    Zielinski, F.2    Lo, L.L.3    Schneider, E.4
  • 7
    • 84879186446 scopus 로고    scopus 로고
    • Cell-free protein synthesis and substrate specificity of full-length endoglucanase CelJ (Cel9D-Cel44A), the largest multi-enzyme subunit of the Clostridium thermocellum cellulosome
    • Hirano, N., Hasegawa, H., Nihei, S., and Haruki, M. (2013) Cell-free protein synthesis and substrate specificity of full-length endoglucanase CelJ (Cel9D-Cel44A), the largest multi-enzyme subunit of the Clostridium thermocellum cellulosome. FEMS Microbiol. Lett. 344, 25-30
    • (2013) FEMS Microbiol. Lett. , vol.344 , pp. 25-30
    • Hirano, N.1    Hasegawa, H.2    Nihei, S.3    Haruki, M.4
  • 8
    • 0030700658 scopus 로고    scopus 로고
    • CelG from Clostridium cellulolyticum: A multidomain endoglucanase acting efficiently on crystalline cellulose
    • Gal, L., Gaudin, C., Belaich, A., Pages, S., Tardif, C., and Belaich, J. P. (1997) CelG from Clostridium cellulolyticum: a multidomain endoglucanase acting efficiently on crystalline cellulose. J. Bacteriol. 179, 6595-6601 (Pubitemid 27465290)
    • (1997) Journal of Bacteriology , vol.179 , Issue.21 , pp. 6595-6601
    • Gal, L.1    Gaudin, C.2    Belaich, A.3    Pages, S.4    Tardif, C.5    Belaich, J.-P.6
  • 9
    • 0034064297 scopus 로고    scopus 로고
    • CelE, a multidomain cellulase from Clostridium cellulolyticum: A key enzyme in the cellulosome?
    • DOI 10.1128/JB.182.7.1910-1915.2000
    • Gaudin, C., Belaich, A., Champ, S., and Belaich, J. P. (2000) CelE, a multidomain cellulase from Clostridium cellulolyticum: a key enzyme in the cellulosome? J. Bacteriol. 182, 1910-1915 (Pubitemid 30165378)
    • (2000) Journal of Bacteriology , vol.182 , Issue.7 , pp. 1910-1915
    • Gaudin, C.1    Belaich, A.2    Champ, S.3    Belaich, J.-P.4
  • 11
    • 14644397981 scopus 로고    scopus 로고
    • Interactions between immunoglobulin-like and catalytic modules in Clostridium thermocellum cellulosomal cellobiohydrolase CbhA
    • DOI 10.1093/protein/gzh094
    • Kataeva, I. A., Uversky, V. N., Brewer, J. M., Schubot, F., Rose, J. P., Wang, B. C., and Ljungdahl, L. G. (2004) Interactions between immunoglobulin-like and catalytic modules in Clostridium thermocellum cellulosomal cellobiohydrolase CbhA. Protein Eng. Des. Sel. 17, 759-769 (Pubitemid 40313669)
    • (2004) Protein Engineering, Design and Selection , vol.17 , Issue.11 , pp. 759-769
    • Kataeva, I.A.1    Uversky, V.N.2    Brewer, J.M.3    Schubot, F.4    Rose, J.P.5    Wang, B.-C.6    Ljungdahl, L.G.7
  • 12
    • 77950340654 scopus 로고    scopus 로고
    • Glycoside hydrolase family 9 processive endoglucanase from Clostridium phytofermentans: Heterologous expression, characterization, and synergy with family-48 cellobiohydrolase
    • Zhang, X. Z., Sathitsuksanoh, N., and Zhang, Y. H. (2010) Glycoside hydrolase family 9 processive endoglucanase from Clostridium phytofermentans: heterologous expression, characterization, and synergy with family-48 cellobiohydrolase. Bioresource Technol. 101, 5534-5538
    • (2010) Bioresource Technol. , vol.101 , pp. 5534-5538
    • Zhang, X.Z.1    Sathitsuksanoh, N.2    Zhang, Y.H.3
  • 13
    • 77953631886 scopus 로고    scopus 로고
    • Cellulosomes: Highly efficient nanomachines designed to deconstruct plant cell wall complex carbohydrates
    • Fontes, C. M., and Gilbert, H. J. (2010) Cellulosomes: highly efficient nanomachines designed to deconstruct plant cell wall complex carbohydrates. Annu. Rev. Biochem. 79, 655-681
    • (2010) Annu. Rev. Biochem. , vol.79 , pp. 655-681
    • Fontes, C.M.1    Gilbert, H.J.2
  • 15
    • 79951904581 scopus 로고    scopus 로고
    • Comparison of the mesophilic cellulosome-producing Clostridium cellulovorans genome with other cellulosome-related clostridial genomes
    • Tamaru, Y., Miyake, H., Kuroda, K., Nakanishi, A., Matsushima, C., Doi, R. H., and Ueda, M. (2011) Comparison of the mesophilic cellulosome-producing Clostridium cellulovorans genome with other cellulosome-related clostridial genomes, Microb. Biotechnol. 4, 64-73
    • (2011) Microb. Biotechnol. , vol.4 , pp. 64-73
    • Tamaru, Y.1    Miyake, H.2    Kuroda, K.3    Nakanishi, A.4    Matsushima, C.5    Doi, R.H.6    Ueda, M.7
  • 16
    • 76649097005 scopus 로고    scopus 로고
    • Modulation of cellulosome composition in Clostridium cellulolyticum: Adaptation to the polysaccharide environment revealed by proteomic and carbohydrate-active enzyme analyses
    • Blouzard, J. C., Coutinho, P. M., Fierobe, H. P., Henrissat, B., Lignon, S., Tardif, C., Pagès, S., and de Philip, P. (2010) Modulation of cellulosome composition in Clostridium cellulolyticum: adaptation to the polysaccharide environment revealed by proteomic and carbohydrate-active enzyme analyses. Proteomics 10, 541-554
    • (2010) Proteomics , vol.10 , pp. 541-554
    • Blouzard, J.C.1    Coutinho, P.M.2    Fierobe, H.P.3    Henrissat, B.4    Lignon, S.5    Tardif, C.6    Pagès, S.7    De Philip, P.8
  • 17
    • 84873937796 scopus 로고    scopus 로고
    • A two-component system (XydS/R) controls the expression of genes encoding CBM6-containing proteins in response to straw in Clostridium cellulolyticum
    • Celik, H., Blouzard, J. C., Voigt, B., Becher, D., Trotter, V., Fierobe, H. P., Tardif, C., Pagès, S., and de Philip, P. (2013) A two-component system (XydS/R) controls the expression of genes encoding CBM6-containing proteins in response to straw in Clostridium cellulolyticum. PLoS One 8, e56063
    • (2013) PLoS One , vol.8
    • Celik, H.1    Blouzard, J.C.2    Voigt, B.3    Becher, D.4    Trotter, V.5    Fierobe, H.P.6    Tardif, C.7    Pagès, S.8    De Philip, P.9
  • 18
    • 0036175820 scopus 로고    scopus 로고
    • Cel9M, a new family 9 cellulase of the Clostridium cellulolyticum cellulosome
    • Belaich, A., Parsiegla, G., Gal, L., Villard, C., Haser, R., and Belaich, J. P. (2002) Cel9M, a new family 9 cellulase of the Clostridium cellulolyticum cellulosome. J. Bacteriol. 184, 1378-1384 (Pubitemid 34157560)
    • (2002) Journal of Bacteriology , vol.184 , Issue.5 , pp. 1378-1384
    • Belaich, A.1    Parsiegla, G.2    Gal, L.3    Villard, C.4    Haser, R.5    Belaich, J.-P.6
  • 20
    • 0035877619 scopus 로고    scopus 로고
    • Design and production of active cellulosome chimeras. Selective incorporation of dockerin-containing enzymes into defined functional complexes
    • Fierobe, H. P., Mechaly, A., Tardif, C., Belaich, A., Lamed, R., Shoham, Y., Belaich, J. P., and Bayer, E. A. (2001) Design and production of active cellulosome chimeras. Selective incorporation of dockerin-containing enzymes into defined functional complexes. J. Biol. Chem. 276, 21257-21261
    • (2001) J. Biol. Chem. , vol.276 , pp. 21257-21261
    • Fierobe, H.P.1    Mechaly, A.2    Tardif, C.3    Belaich, A.4    Lamed, R.5    Shoham, Y.6    Belaich, J.P.7    Bayer, E.A.8
  • 21
    • 20944438012 scopus 로고    scopus 로고
    • Action of designer cellulosomes on homogeneous Versus complex substrates: Controlled incorporation of three distinct enzymes into a defined trifunctional scaffoldin
    • DOI 10.1074/jbc.M414449200
    • Fierobe, H. P., Mingardon, F., Mechaly, A., Bélaïch, A., Rincon, M. T., Pagès, S., Lamed, R., Tardif, C., Bélaïch, J. P., and Bayer, E. A. (2005) Action of designer cellulosomes on homogeneous versus complex substrates: controlled incorporation of three distinct enzymes into a defined trifunctional scaffoldin. J. Biol. Chem. 280, 16325-16334 (Pubitemid 40616761)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.16 , pp. 16325-16334
    • Fierobe, H.-P.1    Mingardon, F.2    Mechaly, A.3    Belaich, A.4    Rincon, M.T.5    Pages, S.6    Lamed, R.7    Tardif, C.8    Belaich, J.-P.9    Bayer, E.A.10
  • 22
    • 0031019865 scopus 로고    scopus 로고
    • The processive endocellulase CelF, a major component of the Clostridium cellulolyticum cellulosome: Purification and characterization of the recombinant form
    • Reverbel-Leroy, C., Pages, S., Belaich, A., Belaich, J. P., and Tardif, C. (1997) The processive endocellulase CelF, a major component of the Clostridium cellulolyticum cellulosome: purification and characterization of the recombinant form. J. Bacteriol. 179, 46-52 (Pubitemid 26428464)
    • (1997) Journal of Bacteriology , vol.179 , Issue.1 , pp. 46-52
    • Reverbel-Leroy, C.1    Pages, S.2    Belaich, A.3    Belaich, J.-P.4    Tardif, C.5
  • 23
    • 76549203762 scopus 로고
    • A submicrodetermination of glucose
    • Park, J. T., and Johnson, M. J. (1949) A submicrodetermination of glucose. J. Biol. Chem. 181, 149-151
    • (1949) J. Biol. Chem. , vol.181 , pp. 149-151
    • Park, J.T.1    Johnson, M.J.2
  • 24
    • 77957061124 scopus 로고
    • Preparation of crystalline, amorphous and dyed cellulase substrates
    • Wood, T. M. (1988) Preparation of crystalline, amorphous and dyed cellulase substrates. Methods Enzymol. 160, 19-25
    • (1988) Methods Enzymol. , vol.160 , pp. 19-25
    • Wood, T.M.1
  • 25
    • 84886591052 scopus 로고    scopus 로고
    • Unraveling enzyme discrimination during cellulosome assembly independent of cohesin-dockerin affinity
    • Borne, R., Bayer, E. A., Pagès, S., Perret, S., and Fierobe, H. P. (2013) Unraveling enzyme discrimination during cellulosome assembly independent of cohesin-dockerin affinity. FEBS J. 280, 5764-5779
    • (2013) FEBS J. , vol.280 , pp. 5764-5779
    • Borne, R.1    Bayer, E.A.2    Pagès, S.3    Perret, S.4    Fierobe, H.P.5
  • 26
    • 0027651651 scopus 로고
    • Activity studies of eight purified cellulases: Specificity, synergism, and binding domain effects
    • Irwin, D. C., Spezio, M., Walker, L. P., and Wilson, D. B. (1993) Activity studies of eight purified cellulases: Specificity, synergism, and binding domain effects. Biotechnol. Bioeng. 42, 1002-1013 (Pubitemid 23288706)
    • (1993) Biotechnology and Bioengineering , vol.42 , Issue.8 , pp. 1002-1013
    • Irwin, D.C.1    Spezio, M.2    Walker, L.P.3    Wilson, D.B.4
  • 27
    • 84861123861 scopus 로고    scopus 로고
    • Distinguishing xyloglucanase activity in endo-beta(1→4)glucanases
    • Eklöf, J. M., Ruda, M. C., and Brumer, H. (2012) Distinguishing xyloglucanase activity in endo-beta(1→4)glucanases. Methods Enzymol. 510, 97-120
    • (2012) Methods Enzymol. , vol.510 , pp. 97-120
    • Eklöf, J.M.1    Ruda, M.C.2    Brumer, H.3
  • 28
    • 84864851731 scopus 로고    scopus 로고
    • A simple method for determining specificity of carbohydrate-binding modules for purified and crude insoluble polysaccharide substrates
    • Yaniv, O., Jindou, S., Frolow, F., Lamed, R., and Bayer, E. A. (2012) A simple method for determining specificity of carbohydrate-binding modules for purified and crude insoluble polysaccharide substrates. Methods Mol. Biol. 908, 101-107
    • (2012) Methods Mol. Biol. , vol.908 , pp. 101-107
    • Yaniv, O.1    Jindou, S.2    Frolow, F.3    Lamed, R.4    Bayer, E.A.5
  • 29
    • 33644860814 scopus 로고    scopus 로고
    • Novel architecture of family-9 glycoside hydrolases identified in cellulosomal enzymes of Acetivibrio cellulolyticus and Clostridium thermocellum
    • Jindou, S., Xu, Q., Kenig, R., Shulman, M., Shoham, Y., Bayer, E. A., and Lamed, R. (2006) Novel architecture of family-9 glycoside hydrolases identified in cellulosomal enzymes of Acetivibrio cellulolyticus and Clostridium thermocellum. FEMS Microbiol. Lett. 254, 308-316
    • (2006) FEMS Microbiol. Lett. , vol.254 , pp. 308-316
    • Jindou, S.1    Xu, Q.2    Kenig, R.3    Shulman, M.4    Shoham, Y.5    Bayer, E.A.6    Lamed, R.7
  • 30
    • 0027493384 scopus 로고
    • Purification and characterization of endoglucanase C from Clostridium cellulolyticum. Catalytic comparison with endoglucanase A
    • DOI 10.1111/j.1432-1033.1993.tb18277.x
    • Fierobe, H. P., Bagnara-Tardif, C., Gaudin, C., Guerlesquin, F., Sauve, P., Belaich, A., and Belaich, J. P. (1993) Purification and characterization of endoglucanase C from Clostridium cellulolyticum. Catalytic comparison with endoglucanase A. Eur. J. Biochem. 217, 557-565 (Pubitemid 23311965)
    • (1993) European Journal of Biochemistry , vol.217 , Issue.2 , pp. 557-565
    • Fierobe, H.-P.1    Bagnara-Tardif, C.2    Gaudin, C.3    Guerlesquin, F.4    Sauve, P.5    Belaich, A.6    Belaich, J.-P.7
  • 32
    • 78149414478 scopus 로고    scopus 로고
    • Kinetic characterization of a glycoside hydrolase family-44 xyloglucanase/endoglucanase from Ruminococcus flavefaciens FD-1
    • Warner, C. D., Go, R. M., García-Salinas, C., Ford, C., and Reilly, P. J. (2011) Kinetic characterization of a glycoside hydrolase family-44 xyloglucanase/endoglucanase from Ruminococcus flavefaciens FD-1. Enzyme Microb. Technol. 48, 27-32
    • (2011) Enzyme Microb. Technol. , vol.48 , pp. 27-32
    • Warner, C.D.1    Go, R.M.2    García-Salinas, C.3    Ford, C.4    Reilly, P.J.5
  • 33
    • 27144522294 scopus 로고    scopus 로고
    • Two new major subunits in the cellusome of Clostridium thermocellum: Xyloglucanase Xgh74A and endoxylanase Xyn10D
    • DOI 10.1099/mic.0.28206-0
    • Zverlov, V. V., Schantz, N., Schmitt-Kopplin, P., and Schwarz, W. H. (2005) Two new major subunits in the cellulosome of Clostridium thermocellum: xyloglucanase Xgh74A and endoxylanase Xyn10D. Microbiology 151, 3395-3401 (Pubitemid 41488921)
    • (2005) Microbiology , vol.151 , Issue.10 , pp. 3395-3401
    • Zverlov, V.V.1    Schantz, N.2    Schmitt-Kopplin, P.3    Schwarz, W.H.4
  • 34
    • 70350236753 scopus 로고    scopus 로고
    • Unusual binding properties of the dockerin module of Clostridium thermocellum endoglucanase CelJ (Cel9D-Cel44A)
    • Sakka, K., Kishino, Y., Sugihara, Y., Jindou, S., Sakka, M., Inagaki, M., and Kimura, T. (2009) Unusual binding properties of the dockerin module of Clostridium thermocellum endoglucanase CelJ (Cel9D-Cel44A). FEMS Microbiol. Lett. 300, 249-255
    • (2009) FEMS Microbiol. Lett. , vol.300 , pp. 249-255
    • Sakka, K.1    Kishino, Y.2    Sugihara, Y.3    Jindou, S.4    Sakka, M.5    Inagaki, M.6    Kimura, T.7
  • 36
    • 0842327141 scopus 로고    scopus 로고
    • Structural Basis for the Exocellulase Activity of the Cellobiohydrolase CbhA from Clostridium thermocellum
    • DOI 10.1021/bi030202i
    • Schubot, F. D., Kataeva, I. A., Chang, J., Shah, A. K., Ljungdahl, L. G., Rose, J. P., and Wang, B. C. (2004) Structural basis for the exocellulase activity of the cellobiohydrolase CbhA from Clostridium thermocellum. Biochemistry 43, 1163-1170 (Pubitemid 38176514)
    • (2004) Biochemistry , vol.43 , Issue.5 , pp. 1163-1170
    • Schubot, F.D.1    Kataeva, I.A.2    Chang, J.3    Shah, A.K.4    Ljungdahl, L.G.5    Rose, J.P.6    Wang, B.-C.7
  • 37
    • 39749140337 scopus 로고    scopus 로고
    • Transcriptional regulation of the Clostridium cellulolyticum cip-cel operon: A complex mechanism involving a catabolite-responsive element
    • DOI 10.1128/JB.01160-07
    • Abdou, L., Boileau, C., de Philip, P., Pagès, S., Fiérobe, H. P., and Tardif, C. (2008) Transcriptional regulation of the Clostridium cellulolyticum cip-cel operon: a complex mechanism involving a catabolite-responsive element. J. Bacteriol. 190, 1499-1506 (Pubitemid 351304003)
    • (2008) Journal of Bacteriology , vol.190 , Issue.5 , pp. 1499-1506
    • Abdou, L.1    Boileau, C.2    De Philip, P.3    Pages, S.4    Fierobe, H.-P.5    Tardif, C.6
  • 38
    • 65549102556 scopus 로고    scopus 로고
    • The cellulosomes from Clostridium cellulolyticum: Identification of new components and synergies between complexes
    • Fendri, I., Tardif, C., Fierobe, H. P., Lignon, S., Valette, O., Pagès, S., and Perret, S. (2009) The cellulosomes from Clostridium cellulolyticum: identification of new components and synergies between complexes. FEBS J. 276, 3076-3086
    • (2009) FEBS J. , vol.276 , pp. 3076-3086
    • Fendri, I.1    Tardif, C.2    Fierobe, H.P.3    Lignon, S.4    Valette, O.5    Pagès, S.6    Perret, S.7
  • 39
    • 33947152858 scopus 로고    scopus 로고
    • Enzyme diversity of the cellulolytic system produced by Clostridium cellulolyticum explored by two-dimensional analysis: Identification of seven genes encoding new dockerin-containing proteins
    • DOI 10.1128/JB.00917-06
    • Blouzard, J. C., Bourgeois, C., de Philip, P., Valette, O., Bélaïch, A., Tardif, C., Bélaïch, J. P., and Pagès, S. (2007) Enzyme diversity of the cellulolytic system produced by Clostridium cellulolyticum explored by two-dimensional analysis: identification of seven genes encoding new dockerin-containing proteins. J. Bacteriol. 189, 2300-2309 (Pubitemid 46411344)
    • (2007) Journal of Bacteriology , vol.189 , Issue.6 , pp. 2300-2309
    • Blouzard, J.-C.1    Bourgeois, C.2    De Philip, P.3    Valette, O.4    Belaich, A.5    Tardif, C.6    Belaich, J.-P.7    Pages, S.8
  • 41
    • 70350156419 scopus 로고    scopus 로고
    • Crystal structures of A. acidocaldarius endoglucanase Cel9A in complex with cello-oligosaccharides: Strong-1 and -2 subsites mimic cellobiohydrolase activity
    • Eckert, K., Vigouroux, A., Lo Leggio, L., and Moréra, S. (2009) Crystal structures of A. acidocaldarius endoglucanase Cel9A in complex with cello-oligosaccharides: strong-1 and -2 subsites mimic cellobiohydrolase activity. J. Mol. Biol. 394, 61-70
    • (2009) J. Mol. Biol. , vol.394 , pp. 61-70
    • Eckert, K.1    Vigouroux, A.2    Lo Leggio, L.3    Moréra, S.4
  • 42
    • 0037478772 scopus 로고    scopus 로고
    • X-ray crystal structure of the multidomain endoglucanase Cel9G from Clostridium cellulolyticum complexed with natural and synthetic cello-oligosaccharides
    • DOI 10.1128/JB.185.14.4127-4135.2003
    • Mandelman, D., Belaich, A., Belaich, J. P., Aghajari, N., Driguez, H., and Haser, R. (2003) X-Ray crystal structure of the multidomain endoglucanase Cel9G from Clostridium cellulolyticum complexed with natural and synthetic cello-oligosaccharides. J. Bacteriol. 185, 4127-4135 (Pubitemid 36835252)
    • (2003) Journal of Bacteriology , vol.185 , Issue.14 , pp. 4127-4135
    • Mandelman, D.1    Belaich, A.2    Belaich, J.P.3    Aghajari, N.4    Driguez, H.5    Haser, R.6
  • 43
    • 0030759920 scopus 로고    scopus 로고
    • Structure and mechanism of endo/exocellulase E4 from Thermomonospora fusca
    • DOI 10.1038/nsb1097-810
    • 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. 4, 810-818 (Pubitemid 27435346)
    • (1997) Nature Structural Biology , vol.4 , Issue.10 , pp. 810-818
    • Sakon, J.1    Irwin, D.2    Wilson, D.B.3    Andrew, K.P.4
  • 44
    • 60749121994 scopus 로고    scopus 로고
    • Physical association of the catalytic and helper modules of a family-9 glycoside hydrolase is essential for activity
    • Burstein, T., Shulman, M., Jindou, S., Petkun, S., Frolow, F., Shoham, Y., Bayer, E. A., and Lamed, R. (2009) Physical association of the catalytic and helper modules of a family-9 glycoside hydrolase is essential for activity. FEBS Lett. 583, 879-884
    • (2009) FEBS Lett. , vol.583 , pp. 879-884
    • Burstein, T.1    Shulman, M.2    Jindou, S.3    Petkun, S.4    Frolow, F.5    Shoham, Y.6    Bayer, E.A.7    Lamed, R.8


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