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Volumn 85, Issue 5, 2010, Pages 1241-1249

Carbohydrate-binding domains: Multiplicity of biological roles

Author keywords

Carbohydrate targeting; Carbohydrate active proteins; Carbohydrate binding domains; Expansins; Glucoside hydrolases; Lectins

Indexed keywords

ACTIVE PROTEINS; BINDING DOMAIN; BIOLOGICAL FUNCTIONS; CARBOHYDRATE-BINDING MODULES; CATALYTIC MODULES; EXPANSINS; GLUCANS; HYDROLASES; HYDROLYTIC ENZYME; LIGAND BINDING; NON-CATALYTIC; PLANT DEVELOPMENT; PULLULANS; SUBSTRATE SPECIFICITY;

EID: 76649087970     PISSN: 01757598     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00253-009-2331-y     Document Type: Short Survey
Times cited : (333)

References (69)
  • 1
    • 33847696168 scopus 로고    scopus 로고
    • Identification and Characterization of a Novel Periplasmic Polygalacturonic Acid Binding Protein from Yersinia enterolitica
    • DOI 10.1016/j.jmb.2007.01.030, PII S0022283607000599
    • DW Abbott S Hrynuik AB Boraston 2007 Identification and characterization of a novel periplasmic polygalacturonic acid binding protein from Yersinia enterolitica J Mol Biol 367 1023 1033 10.1016/j.jmb.2007.01.030 1:CAS:528:DC%2BD2sXjtFKisbs%3D (Pubitemid 46386069)
    • (2007) Journal of Molecular Biology , vol.367 , Issue.4 , pp. 1023-1033
    • Abbott, D.W.1    Hrynuik, S.2    Boraston, A.B.3
  • 2
    • 1542495429 scopus 로고    scopus 로고
    • Complex structures of Thermoactinomyces vulgaris R-47 α-amylase 1 with malto-oligosaccharides demonstrate the role of domain N acting as a starch-binding domain
    • DOI 10.1016/j.jmb.2003.10.078, PII S0022283603013834
    • A Abe T Tonozuka Y Sakano S Kamitori 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 10.1016/j.jmb.2003.10.078 1:CAS:528:DC%2BD3sXpvVWltL0%3D (Pubitemid 38352822)
    • (2004) Journal of Molecular Biology , vol.335 , Issue.3 , pp. 811-822
    • Abe, A.1    Tonozuka, T.2    Sakano, Y.3    Kamitori, S.4
  • 3
    • 14844304675 scopus 로고    scopus 로고
    • A clostridial endo-β-galactosidase that cleaves both blood group A and B glycotopes: The first member of a new glycoside hydrolase family, GH98
    • DOI 10.1074/jbc.M414099200
    • KM Anderson H Ashida K Maskos A Dell S-C Li Y-T Li 2005 A clostridial endo-beta-galactosidase that cleaves both blood group A and B glycotopes: the first member of a new glycoside hydrolase family, GH98 J Biol Chem 280 7720 7728 10.1074/jbc.M414099200 1:CAS:528:DC%2BD2MXhs1yisb0%3D (Pubitemid 40349665)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.9 , pp. 7720-7728
    • Anderson, K.M.1    Ashida, H.2    Maskos, K.3    Dell, A.4    Li, S.-C.5    Li, Y.-T.6
  • 4
    • 23944484954 scopus 로고    scopus 로고
    • An olive pollen protein with allergenic activity, Ole e 10, defines a novel family of carbohydrate-binding modules and is potentially implicated in pollen germination
    • DOI 10.1042/BJ20050456
    • P Barral C Suárez E Batanero C Alfonso JD Alché MI Rodríguez-García M Villalba G Rivas R Rodríguez 2005 An olive pollen protein with allergenic activity, Ole e 10, defines a novel family of carbohydrate-binding modules and is potentially implicated in pollen germination Biochem J 390 77 84 10.1042/BJ20050456 1:CAS:528: DC%2BD2MXntFGmsr8%3D (Pubitemid 41192233)
    • (2005) Biochemical Journal , vol.390 , Issue.1 , pp. 77-84
    • Barral, P.1    Suarez, C.2    Batanero, E.3    Alfonso, C.4    Alche, J.D.D.5    Rodriguez-Garcia, M.I.6    Villalba, M.7    Rivas, G.8    Rodriguez, R.9
  • 5
    • 33749394275 scopus 로고    scopus 로고
    • Understanding the biological rationale for the diversity of cellulose-directed carbohydrate-binding modules in prokaryotic enzymes
    • DOI 10.1074/jbc.M605903200
    • AW Blake L McCartney JE Flint DN Bolam AB Boraston HJ Gilbert JP Knox 2006 Understanding the biological rationale for the diversity of cellulose-directed carbohydrate-binding modules in prokaryotic enzymes J Biol Chem 281 29321 29329 10.1074/jbc.M605903200 1:CAS:528:DC%2BD28XpvFamsbw%3D (Pubitemid 44507075)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.39 , pp. 29321-29329
    • Blake, A.W.1    McCartney, L.2    Flint, J.E.3    Bolam, D.N.4    Boraston, A.B.5    Gilbert, H.J.6    Knox, J.P.7
  • 7
    • 0036300988 scopus 로고    scopus 로고
    • Differential oligosaccharide recognition by evolutionarily-related β-1,4 and β-1,3 glucan-binding modules
    • DOI 10.1016/S0022-2836(02)00374-1
    • AB Boraston D Nurizzo V Notenboom V Ducros DR Rose DG Kilburn GJ Davies 2002 Differential oligosaccharide recognition by evolutionarily-related beta-1, 4 and beta-1, 3 glucan-binding modules J Mol Biol 319 1143 1156 10.1016/S0022-2836(02)00374-1 1:CAS:528:DC%2BD38Xkslantbs%3D (Pubitemid 34729424)
    • (2002) Journal of Molecular Biology , vol.319 , Issue.5 , pp. 1143-1156
    • Boraston, A.B.1    Nurizzo, D.2    Notenboom, V.3    Ducros, V.4    Rose, D.R.5    Kilburn, D.G.6    Davies, G.J.7
  • 9
    • 4744368323 scopus 로고    scopus 로고
    • Carbohydrate-binding modules: Fine-tuning polysaccharide recognition
    • DOI 10.1042/BJ20040892
    • AB Boraston DN Bolam HJ Gilbert GJ Davies 2004 Carbohydrate-binding modules: fine-tuning polysaccharide recognition Biochem J 382 769 781 10.1042/BJ20040892 1:CAS:528:DC%2BD2cXntlOrsL8%3D (Pubitemid 39312891)
    • (2004) Biochemical Journal , vol.382 , Issue.3 , pp. 769-781
    • Boraston, A.B.1    Bolam, D.N.2    Gilbert, H.J.3    Davies, G.J.4
  • 10
    • 33845935523 scopus 로고    scopus 로고
    • Blood group antigen recognition by a Streptococcus pneumoniae virulence factor
    • DOI 10.1074/jbc.M607620200
    • AB Boraston D Wang RD Burke 2006 Blood group antigen recognition by a Streptococcus pneumoniae virulence factor J Biol Chem 281 35263 35271 10.1074/jbc.M607620200 1:CAS:528:DC%2BD28XhtF2gur7I (Pubitemid 46036564)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.46 , pp. 35263-35271
    • Boraston, A.B.1    Wang, D.2    Burke, R.D.3
  • 11
    • 35048903505 scopus 로고    scopus 로고
    • Carbohydrate recognition by a large sialidase toxin from Clostridium perfringens
    • DOI 10.1021/bi701317g
    • AB Boraston E Ficko-Blean M Healey 2007 Carbohydrate recognition by a large sialidase toxin from Clostridium perfringens Biochemistry 46 11352 11360 10.1021/bi701317g 1:CAS:528:DC%2BD2sXhtVansbbL (Pubitemid 47556762)
    • (2007) Biochemistry , vol.46 , Issue.40 , pp. 11352-11360
    • Boraston, A.B.1    Ficko-Blean, E.2    Healey, M.3
  • 12
    • 48549100257 scopus 로고    scopus 로고
    • Role of swollenin, an expansin-like protein from Trichoderma, in plant root colonization
    • DOI 10.1104/pp.108.116293
    • Y Brotman E Briff A Viterbo I Chet 2008 Role of swollenin, an expansin-like protein from Trichoderma, in plant root colonization Plant Physiol 147 779 789 10.1104/pp.108.116293 1:CAS:528:DC%2BD1cXnsVyht7k%3D (Pubitemid 352844324)
    • (2008) Plant Physiology , vol.147 , Issue.2 , pp. 779-789
    • Brotman, Y.1    Briff, E.2    Viterbo, A.3    Chet, I.4
  • 14
    • 63149190203 scopus 로고    scopus 로고
    • A CBM20 low-affinity starch-binding domain from glucan, water dikinase
    • 10.1016/j.febslet.2009.02.045 1:CAS:528:DC%2BD1MXjslOqtL8%3D
    • C Christiansen MA Hachem MA Glaring A Viksø-Nielsen BW Sigurskjold B Svensson A Blennow 2009 A CBM20 low-affinity starch-binding domain from glucan, water dikinase FEBS Lett 583 1159 1163 10.1016/j.febslet.2009.02.045 1:CAS:528:DC%2BD1MXjslOqtL8%3D
    • (2009) FEBS Lett , vol.583 , pp. 1159-1163
    • Christiansen, C.1    Hachem, M.A.2    Glaring, M.A.3    Viksø-Nielsen, A.4    Sigurskjold, B.W.5    Svensson, B.6    Blennow, A.7
  • 15
    • 27644525170 scopus 로고    scopus 로고
    • Growth of the plant cell wall
    • DOI 10.1038/nrm1746, PII N1746
    • DJ Cosgrove 2005 Growth of the plant cell wall Nat Rev Mol Cell Biol 6 850 861 10.1038/nrm1746 1:CAS:528:DC%2BD2MXhtFKlsL3M (Pubitemid 41568734)
    • (2005) Nature Reviews Molecular Cell Biology , vol.6 , Issue.11 , pp. 850-861
    • Cosgrove, D.J.1
  • 16
    • 0026349480 scopus 로고
    • Non-hydrolytic disruption of cellulose fibres by the binding domain of a bacterial cellulase
    • 10.1038/nbt1191-1096 1:CAS:528:DyaK38Xhslansrg%3D
    • N Din NR Gilkes B Tekant Jr WRAJ RCM DG Kilburn 1991 Non-hydrolytic disruption of cellulose fibres by the binding domain of a bacterial cellulase Bio/Technol 9 1096 1099 10.1038/nbt1191-1096 1:CAS:528:DyaK38Xhslansrg%3D
    • (1991) Bio/Technol , vol.9 , pp. 1096-1099
    • Din, N.1    Gilkes, N.R.2    Tekant Jr, B.3    Wraj, R.4    Kilburn, D.G.5
  • 17
    • 41649095873 scopus 로고    scopus 로고
    • Cellulose-binding domains: Cellulose associated-defensive sensing partners?
    • 10.1016/j.tplants.2008.02.004 1:CAS:528:DC%2BD1cXksleisro%3D
    • B Dumas A Bottin E Gaulin M-T Esquerré-Tugayé 2008 Cellulose-binding domains: cellulose associated-defensive sensing partners? Trends Plant Sci 13 160 164 10.1016/j.tplants.2008.02.004 1:CAS:528: DC%2BD1cXksleisro%3D
    • (2008) Trends Plant Sci , vol.13 , pp. 160-164
    • Dumas, B.1    Bottin, A.2    Gaulin, E.3    Esquerré-Tugayé, M.-T.4
  • 18
    • 57349113816 scopus 로고    scopus 로고
    • Cell surface enzyme attachment is mediated by family 37 carbohydrate-binding modules, unique to Ruminococcus albus
    • 10.1128/JB.00609-08 1:CAS:528:DC%2BD1cXhsV2lsLnL
    • A Ezer E Matalon S Jindou I Borovok N Atamna Z Yu M Morrison EA Bayer R Lamed 2008 Cell surface enzyme attachment is mediated by family 37 carbohydrate-binding modules, unique to Ruminococcus albus J Bacteriol 190 8220 8222 10.1128/JB.00609-08 1:CAS:528:DC%2BD1cXhsV2lsLnL
    • (2008) J Bacteriol , vol.190 , pp. 8220-8222
    • Ezer, A.1    Matalon, E.2    Jindou, S.3    Borovok, I.4    Atamna, N.5    Yu, Z.6    Morrison, M.7    Bayer, E.A.8    Lamed, R.9
  • 19
    • 48649104231 scopus 로고    scopus 로고
    • Regulation and characterization of Thermobifida fusca carbohydrate-binding module proteins E7 and E8
    • 10.1002/bit.21856
    • M Felix I Diana C Shaolin BW David 2008 Regulation and characterization of Thermobifida fusca carbohydrate-binding module proteins E7 and E8 Biotechnol Bioeng 100 1066 1077 10.1002/bit.21856
    • (2008) Biotechnol Bioeng , vol.100 , pp. 1066-1077
    • Felix, M.1    Diana, I.2    Shaolin, C.3    David, B.W.4
  • 20
    • 33845968854 scopus 로고    scopus 로고
    • The interaction of a carbohydrate-binding module from a Clostridium perfringens N-acetyl-β-hexosaminidase with its carbohydrate receptor
    • DOI 10.1074/jbc.M606126200
    • E Ficko-Blean AB Boraston 2006 The interaction of a carbohydrate-binding module from a Clostridium perfringens N-acetyl-beta-hexosaminidase with its carbohydrate receptor J Biol Chem 281 37748 37757 10.1074/jbc.M606126200 1:CAS:528:DC%2BD28Xht1KitrfL (Pubitemid 46042078)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.49 , pp. 37748-37757
    • Ficko-Blean, E.1    Boraston, A.B.2
  • 21
    • 67349191450 scopus 로고    scopus 로고
    • N-acetylglucosamine recognition by a family 32 carbohydrate-binding module from Clostridium perfringens NagH
    • 10.1016/j.jmb.2009.04.066 1:CAS:528:DC%2BD1MXnt1Kisb0%3D
    • E Ficko-Blean AB Boraston 2009 N-acetylglucosamine recognition by a family 32 carbohydrate-binding module from Clostridium perfringens NagH J Mol Biol 390 208 220 10.1016/j.jmb.2009.04.066 1:CAS:528:DC%2BD1MXnt1Kisb0%3D
    • (2009) J Mol Biol , vol.390 , pp. 208-220
    • Ficko-Blean, E.1    Boraston, A.B.2
  • 23
    • 0042099120 scopus 로고    scopus 로고
    • Non-hydrolytic disruption of crystalline structure of cellulose by cellulose binding domain and linker sequence of cellobiohydrolase i from Penicillium janthinellum
    • 1:CAS:528:DC%2BD3MXhvFWjsrg%3D
    • P-J Gao G-J Chen T-H Wang Y-S Zhang J Liu 2001 Non-hydrolytic disruption of crystalline structure of cellulose by cellulose binding domain and linker sequence of cellobiohydrolase I from Penicillium janthinellum Acta Biochim Biophys Sin 33 13 18 1:CAS:528:DC%2BD3MXhvFWjsrg%3D
    • (2001) Acta Biochim Biophys Sin , vol.33 , pp. 13-18
    • Gao, P.-J.1    Chen, G.-J.2    Wang, T.-H.3    Zhang, Y.-S.4    Liu, J.5
  • 25
    • 0035834494 scopus 로고    scopus 로고
    • Both binding sites of the starch-binding domain of Aspergillus niger glucoamylase are essential for inducing a conformational change in amylose
    • DOI 10.1006/jmbi.2001.5097
    • T Giardina AP Gunning N Juge CB Faulds CSM Furniss B Svensson VJ Morris G Williamson 2001 Both binding sites of the starch-binding domain of Aspergillus niger glucoamylase are essential for inducing a conformational change in amylose J Mol Biol 313 1149 10.1006/jmbi.2001.5097 1:CAS:528:DC%2BD3MXotFWgtbw%3D (Pubitemid 33081908)
    • (2001) Journal of Molecular Biology , vol.313 , Issue.5 , pp. 1149-1159
    • Giardina, T.1    Gunning, A.P.2    Juge, N.3    Faulds, C.B.4    Furniss, C.S.M.5    Svensson, B.6    Morris, V.J.7    Williamson, G.8
  • 26
    • 0030724903 scopus 로고    scopus 로고
    • Molecular characterization of the α-amylase genes of Lactobacillus plantarum A6 and Lactobacillus amylovorus reveals an unusual 3' end structure with direct tandem repeats and suggests a common evolutionary origin
    • DOI 10.1016/S0378-1119(97)00309-0, PII S0378111997003090
    • E Giraud G Cuny 1997 Molecular characterization of the alpha-amylase genes of Lactobacillus plantarum A6 and Lactobacillus amylovorus reveals an unusual 3′ end structure with direct tandem repeats and suggests a common evolutionary origin Gene 198 149 157 10.1016/S0378-1119(97)00309-0 1:CAS:528:DyaK2sXlslSksbg%3D (Pubitemid 27453737)
    • (1997) Gene , vol.198 , Issue.1-2 , pp. 149-157
    • Giraud, E.1    Cuny, G.2
  • 27
    • 0028139203 scopus 로고
    • Analysis of the raw starch-binding domain by mutation of a glucoamylase from Aspergillus awamori var. kawachi expressed in Saccharomyces cerevisiae
    • 1:CAS:528:DyaK2cXmvFGqt7c%3D
    • M Goto T Semimaru K Furukawa S Hayashida 1994 Analysis of the raw starch-binding domain by mutation of a glucoamylase from Aspergillus awamori var. kawachi expressed in Saccharomyces cerevisiae Appl Environ Microbiol 60 3926 3930 1:CAS:528:DyaK2cXmvFGqt7c%3D
    • (1994) Appl Environ Microbiol , vol.60 , pp. 3926-3930
    • Goto, M.1    Semimaru, T.2    Furukawa, K.3    Hayashida, S.4
  • 28
    • 45549100630 scopus 로고    scopus 로고
    • Divergent modes of glycan recognition by a new family of carbohydrate-binding modules
    • 10.1074/jbc.M709865200 1:CAS:528:DC%2BD1cXltVyqt70%3D
    • KJ Gregg R Finn DW Abbott AB Boraston 2008 Divergent modes of glycan recognition by a new family of carbohydrate-binding modules J Biol Chem 283 12604 12613 10.1074/jbc.M709865200 1:CAS:528:DC%2BD1cXltVyqt70%3D
    • (2008) J Biol Chem , vol.283 , pp. 12604-12613
    • Gregg, K.J.1    Finn, R.2    Abbott, D.W.3    Boraston, A.B.4
  • 29
    • 53049107996 scopus 로고    scopus 로고
    • Structural and functional studies of Streptococcus pneumoniae neuraminidase B: An intramolecular trans-sialidase
    • 10.1016/j.febslet.2008.08.026 1:CAS:528:DC%2BD1cXht1SnurrM
    • H Gut SJ King MA Walsh 2008 Structural and functional studies of Streptococcus pneumoniae neuraminidase B: an intramolecular trans-sialidase FEBS Lett 582 3348 3352 10.1016/j.febslet.2008.08.026 1:CAS:528:DC%2BD1cXht1SnurrM
    • (2008) FEBS Lett , vol.582 , pp. 3348-3352
    • Gut, H.1    King, S.J.2    Walsh, M.A.3
  • 30
    • 33846113064 scopus 로고    scopus 로고
    • Recent structural studies of carbohydrate-binding modules
    • DOI 10.1007/s00018-006-6195-3
    • H Hashimoto 2006 Recent structural studies of carbohydrate-binding modules Cell Mol Life Sc 63 2954 2967 10.1007/s00018-006-6195-3 1:CAS:528:DC%2BD2sXht1egtbg%3D (Pubitemid 46072301)
    • (2006) Cellular and Molecular Life Sciences , vol.63 , Issue.24 , pp. 2954-2967
    • Hashimoto, H.1
  • 31
    • 2142745877 scopus 로고    scopus 로고
    • Cloning, Expression, and Cell Surface Localization of Paenibacillus sp. Strain W-61 Xylanase 5, a Multidomain Xylanase
    • DOI 10.1128/AEM.69.12.6969-6978.2003
    • Y Ito T Tomita N Roy A Nakano N Sugawara-Tomita S Watanabe N Okai N Abe Y Kamio 2003 Cloning, expression, and cell surface localization of Paenibacillus sp. strain W-61 xylanase 5, a multidomain xylanase Appl Environ Microbiol 69 6969 6978 10.1128/AEM.69.12.6969-6978.2003 1:CAS:528:DC%2BD3sXpvFCmtbc%3D (Pubitemid 38585341)
    • (2003) Applied and Environmental Microbiology , vol.69 , Issue.12 , pp. 6969-6978
    • Ito, Y.1    Tomita, T.2    Roy, N.3    Nakano, A.4    Sugawara-Tomita, N.5    Watanabe, S.6    Okai, N.7    Abe, N.8    Kamio, Y.9
  • 32
    • 33749827454 scopus 로고    scopus 로고
    • Importance of Trp59 and Trp60 in chitin-binding, hydrolytic, and antifungal activities of Streptomyces griseus chitinase C
    • DOI 10.1007/s00253-006-0405-7
    • Y Itoh J Watanabe H Fukada R Mizuno Y Kezuka T Nonaka T Watanabe 2006 Importance of Trp59 and Trp60 in chitin-binding, hydrolytic, and antifungal activities of Streptomyces griseus chitinase C Appl Microbiol Biotechnol 72 1176 1184 10.1007/s00253-006-0405-7 1:CAS:528:DC%2BD28XhtVKrtLjM (Pubitemid 44564452)
    • (2006) Applied Microbiology and Biotechnology , vol.72 , Issue.6 , pp. 1176-1184
    • Itoh, Y.1    Watanabe, J.2    Fukada, H.3    Mizuno, R.4    Kezuka, Y.5    Nonaka, T.6    Watanabe, T.7
  • 33
    • 0030825785 scopus 로고    scopus 로고
    • Surface diffusion of cellulases and their isolated binding domains on cellulose
    • DOI 10.1074/jbc.272.38.24016
    • EJ Jervis CA Haynes DG Kilburn 1997 Surface diffusion of cellulases and their isolated binding domains on cellulose J Biol Chem 272 24016 24023 10.1074/jbc.272.38.24016 1:CAS:528:DyaK2sXmtlOmurs%3D (Pubitemid 27410986)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.38 , pp. 24016-24023
    • Jervis, E.J.1    Haynes, C.A.2    Kilburn, D.G.3
  • 34
    • 33749854901 scopus 로고    scopus 로고
    • Comparative characterization of deletion derivatives of the modular xylanase XynA of Thermotoga maritima
    • DOI 10.1007/s00792-006-0509-0
    • K Jörg L Wolfgang 2006 Comparative characterization of deletion derivatives of the modular xylanase XynA of Thermotoga maritima Extremophiles 10 373 381 10.1007/s00792-006-0509-0 (Pubitemid 44564001)
    • (2006) Extremophiles , vol.10 , Issue.5 , pp. 373-381
    • Kleine, J.1    Liebl, W.2
  • 35
    • 0012275278 scopus 로고    scopus 로고
    • The starch binding domain of glucoamylase from Aspergillus niger: Overview of its structure, function, and role in raw-starch hydrolysis
    • 1:CAS:528:DC%2BD3sXhtVCksbw%3D
    • N Juge ML Gal-Coeffet C Furniss A Gunning B Kramhoft VJ Morris G Williamson B Svensson 2002 The starch binding domain of glucoamylase from Aspergillus niger: overview of its structure, function, and role in raw-starch hydrolysis Biologia Bratisl 57 239 245 1:CAS:528:DC%2BD3sXhtVCksbw%3D
    • (2002) Biologia Bratisl , vol.57 , pp. 239-245
    • Juge, N.1    Gal-Coeffet, M.L.2    Furniss, C.3    Gunning, A.4    Kramhoft, B.5    Morris, V.J.6    Williamson, G.7    Svensson, B.8
  • 36
    • 0023234645 scopus 로고
    • Cloning and nucleotide sequence of the gene coding for enzymatically active fragments of the Bacillus polymyxa beta-amylase
    • 1:CAS:528:DyaL2sXhvV2qu7g%3D
    • T Kawazu Y Nakanishi N Uozumi T Sasaki H Yamagata N Tsukagoshi S Udaka 1987 Cloning and nucleotide sequence of the gene coding for enzymatically active fragments of the Bacillus polymyxa beta-amylase J Bacteriol 169 1564 1570 1:CAS:528:DyaL2sXhvV2qu7g%3D
    • (1987) J Bacteriol , vol.169 , pp. 1564-1570
    • Kawazu, T.1    Nakanishi, Y.2    Uozumi, N.3    Sasaki, T.4    Yamagata, H.5    Tsukagoshi, N.6    Udaka, S.7
  • 38
    • 0024962351 scopus 로고
    • Determination of the three-dimensional solution structure of the C-terminal domain of cellobiohydrolase i from Trichoderma reesei. A study using nuclear magnetic resonance and hybrid distance geometry-dynamical simulated annealing
    • 10.1021/bi00444a016
    • J Kraulis G Clore MJ Nilges PG TA J Knowles A Gronenborn 1987 Determination of the three-dimensional solution structure of the C-terminal domain of cellobiohydrolase I from Trichoderma reesei. A study using nuclear magnetic resonance and hybrid distance geometry-dynamical simulated annealing Biochemistry 28 7241 7257 10.1021/bi00444a016
    • (1987) Biochemistry , vol.28 , pp. 7241-7257
    • Kraulis, J.1    Clore, G.2    Nilges, M.J.3    Ta, P.G.4    Knowles, J.5    Gronenborn, A.6
  • 39
    • 68149178810 scopus 로고    scopus 로고
    • Does the cellulose-binding module move on the cellulose surface?
    • 10.1007/s10570-009-9306-0
    • Y-S Liu Y Zeng Y Luo Q Xu ME Himmel SJ Smith S-Y Ding 2009 Does the cellulose-binding module move on the cellulose surface? Cellulose 16 587 597 10.1007/s10570-009-9306-0
    • (2009) Cellulose , vol.16 , pp. 587-597
    • Liu, Y.-S.1    Zeng, Y.2    Luo, Y.3    Xu, Q.4    Himmel, M.E.5    Smith, S.J.6    Ding, S.-Y.7
  • 40
    • 33645229120 scopus 로고    scopus 로고
    • Differential recognition of plant cell walls by microbial xylan-specific carbohydrate-binding modules
    • 10.1073/pnas.0508887103 1:CAS:528:DC%2BD28Xjtl2luro%3D
    • L McCartney AW Blake J Flint DN Bolam AB Boraston HJ Gilbert JP Knox 2006 Differential recognition of plant cell walls by microbial xylan-specific carbohydrate-binding modules Proc Natl Acad Sci U S A 103 4765 4770 10.1073/pnas.0508887103 1:CAS:528:DC%2BD28Xjtl2luro%3D
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 4765-4770
    • McCartney, L.1    Blake, A.W.2    Flint, J.3    Bolam, D.N.4    Boraston, A.B.5    Gilbert, H.J.6    Knox, J.P.7
  • 42
    • 65849277994 scopus 로고    scopus 로고
    • The family 6 carbohydrate-binding modules have coevolved with their appended catalytic modules toward similar substrate specificity
    • 10.1093/glycob/cwp028 1:CAS:528:DC%2BD1MXmtFSgtb4%3D
    • G Michel T Barbeyron B Kloareg M Czjzek 2009 The family 6 carbohydrate-binding modules have coevolved with their appended catalytic modules toward similar substrate specificity Glycobiology 19 615 623 10.1093/glycob/cwp028 1:CAS:528:DC%2BD1MXmtFSgtb4%3D
    • (2009) Glycobiology , vol.19 , pp. 615-623
    • Michel, G.1    Barbeyron, T.2    Kloareg, B.3    Czjzek, M.4
  • 43
    • 33645670615 scopus 로고    scopus 로고
    • A novel type carbohydrate-binding module identified in α-glucan, water dikinases is specific for regulated plastidial starch metabolism
    • 10.1021/bi051712a 1:CAS:528:DC%2BD28XisFymsL8%3D
    • R Mikkelsen K Suszkiewicz A Blennow 2006 A novel type carbohydrate-binding module identified in α-glucan, water dikinases is specific for regulated plastidial starch metabolism Biochemistry 45 4674 4682 10.1021/bi051712a 1:CAS:528:DC%2BD28XisFymsL8%3D
    • (2006) Biochemistry , vol.45 , pp. 4674-4682
    • Mikkelsen, R.1    Suszkiewicz, K.2    Blennow, A.3
  • 44
    • 33750575137 scopus 로고    scopus 로고
    • The family 42 carbohydrate-binding module of family 54 α-L- arabinofuranosidase specifically binds the arabinofuranose side chain of hemicellulose
    • DOI 10.1042/BJ20060567
    • A Miyanaga T Koseki Y Miwa Y Mese S Nakamura A Kuno J Hirabayashi H Matsuzawa T Wakagi H Shoun S Fushinobu 2006 The family 42 carbohydrate-binding module of family 54 a-l-arabinofuranosidase specifically binds the arabinofuranose side chain of hemicellulose Biochem J 399 503 511 10.1042/BJ20060567 1:CAS:528:DC%2BD28XhtVOis7rL (Pubitemid 44672641)
    • (2006) Biochemical Journal , vol.399 , Issue.3 , pp. 503-511
    • Miyanaga, A.1    Koseki, T.2    Miwa, Y.3    Mese, Y.4    Nakamura, S.5    Kuno, A.6    Hirabayashi, J.7    Matsuzawa, H.8    Wakagi, T.9    Shoun, H.10    Fushinobu, S.11
  • 46
    • 0034809160 scopus 로고    scopus 로고
    • Characterization of the Lactobacillus manihotivorans α-amylase gene
    • 10.3109/10425170109042048 1:CAS:528:DC%2BD38Xks1yku7w%3D
    • J Morlon-Guyot F Mucciolo-Roux R Rodríguez Sanoja JP Guyot 2001 Characterization of the Lactobacillus manihotivorans α-amylase gene DNA Seq 12 27 37 10.3109/10425170109042048 1:CAS:528:DC%2BD38Xks1yku7w%3D
    • (2001) DNA Seq , vol.12 , pp. 27-37
    • Morlon-Guyot, J.1    Mucciolo-Roux, F.2    Rodríguez Sanoja, R.3    Guyot, J.P.4
  • 49
    • 33644645394 scopus 로고    scopus 로고
    • Galactose recognition by the carbohydrate-binding module of a bacterial sialidase
    • SL Newstead JN Watson AJ Bennet G Taylor 2005 Galactose recognition by the carbohydrate-binding module of a bacterial sialidase Acta Cryst 61 1483 1491
    • (2005) Acta Cryst , vol.61 , pp. 1483-1491
    • Newstead, S.L.1    Watson, J.N.2    Bennet, A.J.3    Taylor, G.4
  • 50
    • 0035967536 scopus 로고    scopus 로고
    • Crystal structures of the family 9 carbohydrate-binding module from Thermotoga maritima xylanase 10a in native and ligand-bound forms
    • DOI 10.1021/bi0101704
    • V Notenboom AB Boraston DG Kilburn DR Rose 2001 Crystal structures of the family 9 carbohydrate-binding module from Thermotoga maritima xylanase 10A in native and ligand-bound forms Biochemistry 40 6248 6256 10.1021/bi0101704 1:CAS:528:DC%2BD3MXjt1WnsLY%3D (Pubitemid 32472713)
    • (2001) Biochemistry , vol.40 , Issue.21 , pp. 6248-6256
    • Notenboom, V.1    Boraston, A.B.2    Kilburn, D.G.3    Rose, D.R.4
  • 51
    • 34548425030 scopus 로고    scopus 로고
    • Promiscuous, non-catalytic, tandem carbohydrate-binding modules modulate the cell-wall structure and development of transgenic tobacco (Nicotiana tabacum) plants
    • DOI 10.1007/s10265-007-0099-7
    • O Obembe E Jacobsen J Timmers H Gilbert A Blake J Knox R Visser J-P Vincken 2007 Promiscuous, non-catalytic, tandem carbohydrate-binding modules modulate the cell-wall structure and development of transgenic tobacco (Nicotiana tabacum) plants J Plant Res 120 605 617 10.1007/s10265-007-0099-7 1:CAS:528:DC%2BD2sXhtVSjsrnN (Pubitemid 47367693)
    • (2007) Journal of Plant Research , vol.120 , Issue.5 , pp. 605-617
    • Obembe, O.O.1    Jacobsen, E.2    Timmers, J.3    Gilbert, H.4    Blake, A.W.5    Knox, J.P.6    Visser, R.G.F.7    Vincken, J.-P.8
  • 52
    • 40549092336 scopus 로고    scopus 로고
    • The effects of the surface-exposed residues on the binding and hydrolytic activities of Vibrio carchariae chitinase A
    • DOI 10.1186/1471-2091-9-2
    • S Pantoom C Songsiriritthigul W Suginta 2008 The effects of the surface-exposed residues on the binding and hydrolytic activities of Vibrio carchariae chitinase A BMC Biochem 9 2 10.1186/1471-2091-9-2 (Pubitemid 351361841)
    • (2008) BMC Biochemistry , vol.9 , Issue.1 , pp. 2
    • Pantoom, S.1    Songsiriritthigul, C.2    Suginta, W.3
  • 54
    • 53149142512 scopus 로고    scopus 로고
    • The catalytic and lectin domains of UDP-GalNAc:Polypeptide alpha-N-acetylgalactosaminyltransferase function in concert to direct glycosylation site selection
    • 10.1074/jbc.M803387200 1:CAS:528:DC%2BD1cXpvFGgsr4%3D
    • J Raman TA Fritz TA Gerken O Jamison D Live M Liu LA Tabak 2008 The catalytic and lectin domains of UDP-GalNAc:Polypeptide alpha-N- acetylgalactosaminyltransferase function in concert to direct glycosylation site selection J Biol Chem 283 22942 22951 10.1074/jbc.M803387200 1:CAS:528:DC%2BD1cXpvFGgsr4%3D
    • (2008) J Biol Chem , vol.283 , pp. 22942-22951
    • Raman, J.1    Fritz, T.A.2    Gerken, T.A.3    Jamison, O.4    Live, D.5    Liu, M.6    Tabak, L.A.7
  • 55
    • 61349124174 scopus 로고    scopus 로고
    • A single residue mutation abolishes attachment of the CBM26 starch-binding domain from Lactobacillus amylovorus α-amylase
    • 10.1007/s10295-008-0502-y
    • R Rodríguez-Sanoja N Oviedo L Escalante B Ruiz S Sanchez 2009 A single residue mutation abolishes attachment of the CBM26 starch-binding domain from Lactobacillus amylovorus α-amylase J Ind Microbiol Biotechnol 36 341 346 10.1007/s10295-008-0502-y
    • (2009) J Ind Microbiol Biotechnol , vol.36 , pp. 341-346
    • Rodríguez-Sanoja, R.1    Oviedo, N.2    Escalante, L.3    Ruiz, B.4    Sanchez, S.5
  • 56
    • 33745161547 scopus 로고    scopus 로고
    • Carbohydrate binding modules: Biochemical properties and novel applications
    • DOI 10.1128/MMBR.00028-05
    • O Shoseyov Z Shani I Levy 2006 Carbohydrate binding modules: biochemical properties and novel applications Microbiol Mol Biol Rev 70 283 295 10.1128/MMBR.00028-05 1:CAS:528:DC%2BD28XmvFGrtLk%3D (Pubitemid 43895029)
    • (2006) Microbiology and Molecular Biology Reviews , vol.70 , Issue.2 , pp. 283-295
    • Shoseyov, O.1    Shani, Z.2    Levy, I.3
  • 57
    • 0034731387 scopus 로고    scopus 로고
    • The structural basis for the ligand specificity of family 2 carbohydrate-binding modules
    • DOI 10.1074/jbc.M006948200
    • PJ Simpson H Xie DN Bolam HJ Gilbert MP Williamson 2000 The structural basis for the ligand specificity of family 2 carbohydrate-binding modules J Biol Chem 275 41137 41142 10.1074/jbc.M006948200 1:CAS:528:DC%2BD3MXjsVGqtg%3D%3D (Pubitemid 32054944)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.52 , pp. 41137-41142
    • Simpson, P.J.1    Xie, H.2    Bolam, D.N.3    Gilbert, H.J.4    Williamson, M.P.5
  • 58
    • 0031570348 scopus 로고    scopus 로고
    • Solution structure of the granular starch binding domain of Aspergillus niger glucoamylase bound to β-cyclodextrin
    • K Sorimachi M-FL Gal-Coëffet G Williamson DB Archer MP Williamson 1997 Solution structure of the granular starch binding domain of Aspergillus niger glucoamylase bound to β-cyclodextrin Structure 5 647 661 10.1016/S0969-2126(97)00220-7 1:CAS:528:DyaK2sXjvFamt7Y%3D (Pubitemid 27236264)
    • (1997) Structure , vol.5 , Issue.5 , pp. 647-661
    • Sorimachi, K.1    Le Gal-Coeffet, M.-F.2    Williamson, G.3    Archer, D.B.4    Williamson, M.P.5
  • 59
    • 0033013902 scopus 로고    scopus 로고
    • The starch-binding domain from glucoamylase disrupts the structure of starch
    • DOI 10.1016/S0014-5793(99)00263-X, PII S001457939900263X
    • SM Southall PJ Simpson HJ Gilbert G Williamson MP Williamson 1999 The starch-binding domain from glucoamylase disrupts the structure of starch FEBS Lett 447 58 60 10.1016/S0014-5793(99)00263-X 1:CAS:528:DyaK1MXhvVClsr0%3D (Pubitemid 29134948)
    • (1999) FEBS Letters , vol.447 , Issue.1 , pp. 58-60
    • Southall, S.M.1    Simpson, P.J.2    Gilbert, H.J.3    Williamson, G.4    Williamson, M.P.5
  • 61
    • 23344446196 scopus 로고    scopus 로고
    • The non-catalytic chitin-binding protein CBP21 from Serratia marcescens is essential for chitin degradation
    • DOI 10.1074/jbc.M504468200
    • G Vaaje-Kolstad SJ Horn DMF van Aalten B Synstad VGH Eijsink 2005 The non-catalytic chitin-binding protein CBP21 from Serratia marcescens is essential for chitin degradation J Biol Chem 280 28492 28497 10.1074/jbc.M504468200 1:CAS:528:DC%2BD2MXmvFSnsL0%3D (Pubitemid 41105749)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.31 , pp. 28492-28497
    • Vaaje-Kolstad, G.1    Horn, S.J.2    Van Aalten, D.M.F.3    Synstad, B.4    Eijsink, V.G.H.5
  • 62
    • 15744367514 scopus 로고    scopus 로고
    • Crystal structure and binding properties of the Serratia marcescens chitin-binding protein CBP21
    • DOI 10.1074/jbc.M407175200
    • G Vaaje-Kolstad DR Houston AHK Riemen VGH Eijsink DMF van Aalten 2005 Crystal structure and binding properties of the Serratia marcescens chitin-binding protein CBP21 J Biol Chem 280 11313 11319 10.1074/jbc.M407175200 1:CAS:528:DC%2BD2MXisVyjs7k%3D (Pubitemid 40418438)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.12 , pp. 11313-11319
    • Vaaje-Kolstad, G.1    Houston, D.R.2    Riemen, A.H.K.3    Eijsink, V.G.H.4    Van Aalten, D.M.F.5
  • 63
    • 40149108056 scopus 로고    scopus 로고
    • Role of the N-terminal starch-binding domains in the kinetic properties of starch synthase III from Arabidopsis thaliana
    • DOI 10.1021/bi702418h
    • HA Valdez MV Busi NZ Wayllace G Parisi RA Ugalde DF Gomez-Casati 2008 Role of the N-terminal starch-binding domains in the kinetic properties of starch synthase III from Arabidopsis thaliana Biochemistry 47 3026 3032 10.1021/bi702418h 1:CAS:528:DC%2BD1cXhslChtb4%3D (Pubitemid 351328855)
    • (2008) Biochemistry , vol.47 , Issue.9 , pp. 3026-3032
    • Valdez, H.A.1    Busi, M.V.2    Wayllace, N.Z.3    Parisi, G.4    Ugalde, R.A.5    Gomez-Casati, D.F.6
  • 64
    • 33846096051 scopus 로고    scopus 로고
    • Identification and structural basis of binding to host lung glycogen by streptococcal virulence factors
    • DOI 10.1038/nsmb1187, PII NSMB1187
    • AL van Bueren M Higgins D Wang RD Burke AB Boraston 2007 Identification and structural basis of binding to host lung glycogen by streptococcal virulence factors Nat Struct Mol Biol 14 76 84 10.1038/nsmb1187 (Pubitemid 46067426)
    • (2007) Nature Structural and Molecular Biology , vol.14 , Issue.1 , pp. 76-84
    • Van Bueren, A.L.1    Higgins, M.2    Wang, D.3    Burke, R.D.4    Boraston, A.B.5
  • 66
    • 64549113059 scopus 로고    scopus 로고
    • Cloning, sequencing, and expression of the gene encoding a multidomain endo-beta-1, 4-xylanase from Paenibacillus curdlanolyticus B-6, and characterization of the recombinant enzyme
    • 1:CAS:528:DC%2BD1MXlt1GisL0%3D
    • R Waeonukul P Pason KL Kyu K Sakka A Kosugi Y Mori K Ratanakhanokchai 2009 Cloning, sequencing, and expression of the gene encoding a multidomain endo-beta-1, 4-xylanase from Paenibacillus curdlanolyticus B-6, and characterization of the recombinant enzyme J Microbiol Biotechnol 19 277 285 1:CAS:528:DC%2BD1MXlt1GisL0%3D
    • (2009) J Microbiol Biotechnol , vol.19 , pp. 277-285
    • Waeonukul, R.1    Pason, P.2    Kyu, K.L.3    Sakka, K.4    Kosugi, A.5    Mori, Y.6    Ratanakhanokchai, K.7
  • 67
    • 47349122440 scopus 로고    scopus 로고
    • A novel function for the cellulose binding module of cellobiohydrolase I
    • DOI 10.1007/s11427-008-0088-3
    • L Wang Y Zhang P Gao 2008 A novel function for the cellulose binding module of cellobiohydrolase I Sci China C Life Sci 51 620 629 10.1007/s11427-008-0088-3 1:CAS:528:DC%2BD1cXhtValtrrI (Pubitemid 351999750)
    • (2008) Science in China, Series C: Life Sciences , vol.51 , Issue.7 , pp. 620-629
    • Wang, L.1    Zhang, Y.2    Gao, P.3
  • 68
    • 84954358046 scopus 로고    scopus 로고
    • Crystal structure of the NanB sialidase from Streptococcus pneumoniae
    • 10.1016/j.jmb.2008.09.032 1:CAS:528:DC%2BD1cXhtlaqsrfI
    • G Xu JA Potter RJM Russell MR Oggioni PW Andrew GL Taylor 2008 Crystal structure of the NanB sialidase from Streptococcus pneumoniae J Mol Biol 384 436 449 10.1016/j.jmb.2008.09.032 1:CAS:528:DC%2BD1cXhtlaqsrfI
    • (2008) J Mol Biol , vol.384 , pp. 436-449
    • Xu, G.1    Potter, J.A.2    Russell, R.J.M.3    Oggioni, M.R.4    Andrew, P.W.5    Taylor, G.L.6
  • 69
    • 10844286172 scopus 로고    scopus 로고
    • Toward an aggregated understanding of enzymatic hydrolysis of cellulose: Noncomplexed cellulase systems
    • DOI 10.1002/bit.20282
    • Z Yi-Heng Percival RL Lee 2004 Toward an aggregated understanding of enzymatic hydrolysis of cellulose: noncomplexed cellulase systems Biotechnol Bioeng 88 797 824 10.1002/bit.20282 (Pubitemid 40003769)
    • (2004) Biotechnology and Bioengineering , vol.88 , Issue.7 , pp. 797-824
    • Zhang, Y.-H.P.1    Lynd, L.R.2


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