메뉴 건너뛰기




Volumn 156, Issue 4, 2011, Pages 253-260

Engineering of cellobiose phosphorylase for glycoside synthesis

Author keywords

Cellobiose phosphorylase; Directed evolution; Enzyme engineering; Glycoside synthesis

Indexed keywords

CLONING; ENZYMES; PHOSPHORYLATION; SUBSTRATES; SUGARS;

EID: 82955187730     PISSN: 01681656     EISSN: 18734863     Source Type: Journal    
DOI: 10.1016/j.jbiotec.2011.07.006     Document Type: Review
Times cited : (16)

References (46)
  • 1
    • 0014409336 scopus 로고
    • Purification and specificity of cellobiose phosphorylase from Clostridium thermocellum
    • Alexander J.K. Purification and specificity of cellobiose phosphorylase from Clostridium thermocellum. J. Biol. Chem. 1968, 243:2899-2904.
    • (1968) J. Biol. Chem. , vol.243 , pp. 2899-2904
    • Alexander, J.K.1
  • 4
    • 82955230090 scopus 로고    scopus 로고
    • Engineering of cellobiose phosphorylase for glycoside synthesis. PhD thesis, Faculty of Bioscience Engineering, Ghent University, Ghent, Belgium.
    • De Groeve, M.R.M., 2009. Engineering of cellobiose phosphorylase for glycoside synthesis. PhD thesis, Faculty of Bioscience Engineering, Ghent University, Ghent, Belgium, p. 243.
    • (2009) , pp. 243
    • De Groeve, M.R.M.1
  • 6
    • 73949098109 scopus 로고    scopus 로고
    • Enzymatic production of alpha-d-galactose 1-phosphate by lactose phosphorolysis
    • De Groeve M.R.M., Depreitere V., Desmet T., Soetaert W. Enzymatic production of alpha-d-galactose 1-phosphate by lactose phosphorolysis. Biotechnol. Lett. 2009, 31:1873-1877.
    • (2009) Biotechnol. Lett. , vol.31 , pp. 1873-1877
    • De Groeve, M.R.M.1    Depreitere, V.2    Desmet, T.3    Soetaert, W.4
  • 7
    • 78650138613 scopus 로고    scopus 로고
    • Construction of cellobiose phosphorylase variants with broadened acceptor specificity towards anomerically substituted glucosides
    • De Groeve M.R.M., Remmery L., Van Hoorebeke A., Stout J., Desmet T., Savvides S.N., Soetaert W. Construction of cellobiose phosphorylase variants with broadened acceptor specificity towards anomerically substituted glucosides. Biotechnol. Bioeng. 2010, 107:413-420.
    • (2010) Biotechnol. Bioeng. , vol.107 , pp. 413-420
    • De Groeve, M.R.M.1    Remmery, L.2    Van Hoorebeke, A.3    Stout, J.4    Desmet, T.5    Savvides, S.N.6    Soetaert, W.7
  • 9
    • 79551509765 scopus 로고    scopus 로고
    • Enzymatic glycosyl transfer: mechanisms and applications
    • Desmet T., Soetaert W. Enzymatic glycosyl transfer: mechanisms and applications. Biocatal. Biotransform. 2011, 29:1-18.
    • (2011) Biocatal. Biotransform. , vol.29 , pp. 1-18
    • Desmet, T.1    Soetaert, W.2
  • 10
    • 60349127519 scopus 로고    scopus 로고
    • Catalytic effectiveness, a measure of enzyme proficiency for industrial applications
    • Fox R.J., Clay M.D. Catalytic effectiveness, a measure of enzyme proficiency for industrial applications. Trends Biotechnol. 2009, 27:137-140.
    • (2009) Trends Biotechnol. , vol.27 , pp. 137-140
    • Fox, R.J.1    Clay, M.D.2
  • 11
    • 33747265618 scopus 로고    scopus 로고
    • Enhancing the thermal stability of sucrose phosphorylase from Streptococcus mutans by random mutagenesis
    • Fujii K., Iboshi M., Yanase M., Takaha T., Kuriki T. Enhancing the thermal stability of sucrose phosphorylase from Streptococcus mutans by random mutagenesis. J. Appl. Glycosci. 2006, 53:91-97.
    • (2006) J. Appl. Glycosci. , vol.53 , pp. 91-97
    • Fujii, K.1    Iboshi, M.2    Yanase, M.3    Takaha, T.4    Kuriki, T.5
  • 12
    • 41149175076 scopus 로고    scopus 로고
    • Computational analyses of the conformational itinerary along the reaction pathway of GH94 cellobiose phosphorylase
    • Fushinobu S., Mertz B., Hill A.D., Hidaka M., Kitaoka M., Reilly P.J. Computational analyses of the conformational itinerary along the reaction pathway of GH94 cellobiose phosphorylase. Carbohydr. Res. 2008, 343:1023-1033.
    • (2008) Carbohydr. Res. , vol.343 , pp. 1023-1033
    • Fushinobu, S.1    Mertz, B.2    Hill, A.D.3    Hidaka, M.4    Kitaoka, M.5    Reilly, P.J.6
  • 13
    • 57749102704 scopus 로고    scopus 로고
    • A high-yielding biocatalytic process for the production of 2-O-(alpha-d-glucopyranosyl)-sn-glycerol, a natural osmolyte and useful moisturizing ingredient
    • Goedl C., Sawangwan T., Mueller M., Schwarz A., Nidetzky B. A high-yielding biocatalytic process for the production of 2-O-(alpha-d-glucopyranosyl)-sn-glycerol, a natural osmolyte and useful moisturizing ingredient. Angew. Chem. Int. Ed. Engl. 2008, 47:10086-10089.
    • (2008) Angew. Chem. Int. Ed. Engl. , vol.47 , pp. 10086-10089
    • Goedl, C.1    Sawangwan, T.2    Mueller, M.3    Schwarz, A.4    Nidetzky, B.5
  • 14
    • 0030733350 scopus 로고    scopus 로고
    • Structural and sequence-based classification of glycoside hydrolases
    • Henrissat B., Davies G. Structural and sequence-based classification of glycoside hydrolases. Curr. Opin. Struct. Biol. 1997, 7:637-644.
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 637-644
    • Henrissat, B.1    Davies, G.2
  • 15
  • 16
    • 0036685627 scopus 로고    scopus 로고
    • Kinetic studies of a recombinant cellobiose phosphorylase (CBP) of the Clostridium thermocellum YM4 strain expressed in Escherichia coli
    • Kim Y.K., Kitaoka M., Krishnareddy M., Mori Y., Hayashi K. Kinetic studies of a recombinant cellobiose phosphorylase (CBP) of the Clostridium thermocellum YM4 strain expressed in Escherichia coli. J. Biochem. 2002, 132:197-203.
    • (2002) J. Biochem. , vol.132 , pp. 197-203
    • Kim, Y.K.1    Kitaoka, M.2    Krishnareddy, M.3    Mori, Y.4    Hayashi, K.5
  • 19
    • 32044438652 scopus 로고    scopus 로고
    • Reaction on d-glucal by an inverting phosphorylase to synthesize derivatives of 2-deoxy-beta-d-arabino-hexopyranosyl-(1→4)-d-glucose (2II-deoxycellobiose)
    • Kitaoka M., Nomura S., Yoshida M., Hayashi K. Reaction on d-glucal by an inverting phosphorylase to synthesize derivatives of 2-deoxy-beta-d-arabino-hexopyranosyl-(1→4)-d-glucose (2II-deoxycellobiose). Carbohydr. Res. 2006, 341:545-549.
    • (2006) Carbohydr. Res. , vol.341 , pp. 545-549
    • Kitaoka, M.1    Nomura, S.2    Yoshida, M.3    Hayashi, K.4
  • 20
    • 0026637250 scopus 로고
    • Synthetic reaction of Cellvibrio gilvus cellobiose phosphorylase
    • Kitaoka M., Sasaki T., Taniguchi H. Synthetic reaction of Cellvibrio gilvus cellobiose phosphorylase. J. Biochem. 1992, 112:40-44.
    • (1992) J. Biochem. , vol.112 , pp. 40-44
    • Kitaoka, M.1    Sasaki, T.2    Taniguchi, H.3
  • 21
    • 0034872489 scopus 로고    scopus 로고
    • Glycosides in medicine: the role of glycosidic residue in biological activity
    • Kren V., Martinkova L. Glycosides in medicine: the role of glycosidic residue in biological activity. Curr. Med. Chem. 2001, 8:1303-1328.
    • (2001) Curr. Med. Chem. , vol.8 , pp. 1303-1328
    • Kren, V.1    Martinkova, L.2
  • 22
    • 0033539166 scopus 로고    scopus 로고
    • Design and synthesis of water-soluble glucuronide derivatives of camptothecin for cancer prodrug monotherapy and antibody-directed enzyme prodrug therapy (ADEPT)
    • Leu Y.L., Roffler S.R., Chern J.W. Design and synthesis of water-soluble glucuronide derivatives of camptothecin for cancer prodrug monotherapy and antibody-directed enzyme prodrug therapy (ADEPT). J. Med. Chem. 1999, 42:3623-3628.
    • (1999) J. Med. Chem. , vol.42 , pp. 3623-3628
    • Leu, Y.L.1    Roffler, S.R.2    Chern, J.W.3
  • 23
    • 78650090993 scopus 로고    scopus 로고
    • Carbohydrate synthesis by disaccharide phosphorylases: Reactions, catalytic mechanisms and application in the glycosciences
    • Luley-Goedl C., Nidetzky B. Carbohydrate synthesis by disaccharide phosphorylases: Reactions, catalytic mechanisms and application in the glycosciences. Biotechnol. J. 2010, 5:1324-1338.
    • (2010) Biotechnol. J. , vol.5 , pp. 1324-1338
    • Luley-Goedl, C.1    Nidetzky, B.2
  • 24
    • 78649861857 scopus 로고    scopus 로고
    • Efficient chemoenzymatic oligosaccharide synthesis by reverse phosphorolysis using cellobiose phosphorylase and cellodextrin phosphorylase from Clostridium thermocellum
    • Nakai H., Hachem M.A., Petersen B.O., Westphal Y., Mannerstedt K., Baumann M.J., Dilokpimol A., Schols H.A., Duus J.O., Svensson B. Efficient chemoenzymatic oligosaccharide synthesis by reverse phosphorolysis using cellobiose phosphorylase and cellodextrin phosphorylase from Clostridium thermocellum. Biochimie 2010, 92:1818-1826.
    • (2010) Biochimie , vol.92 , pp. 1818-1826
    • Nakai, H.1    Hachem, M.A.2    Petersen, B.O.3    Westphal, Y.4    Mannerstedt, K.5    Baumann, M.J.6    Dilokpimol, A.7    Schols, H.A.8    Duus, J.O.9    Svensson, B.10
  • 25
    • 77956570506 scopus 로고    scopus 로고
    • Rational engineering of Lactobacillus acidophilus NCFM maltose phosphorylase into either trehalose or kojibiose dual specificity phosphorylase
    • Nakai H., Petersen B.O., Westphal Y., Dilokpimol A., Abou Hachem M., Duus J.O., Schols H.A., Svensson B. Rational engineering of Lactobacillus acidophilus NCFM maltose phosphorylase into either trehalose or kojibiose dual specificity phosphorylase. Protein Eng. Des. Sel. 2010, 23:781-787.
    • (2010) Protein Eng. Des. Sel. , vol.23 , pp. 781-787
    • Nakai, H.1    Petersen, B.O.2    Westphal, Y.3    Dilokpimol, A.4    Abou Hachem, M.5    Duus, J.O.6    Schols, H.A.7    Svensson, B.8
  • 26
    • 67749097994 scopus 로고    scopus 로고
    • Characterization of three beta-galactoside phosphorylases from Clostridium phytofermentans: discovery of d-galactosyl-beta1→4-l-rhamnose phosphorylase
    • Nakajima M., Nishimoto M., Kitaoka M. Characterization of three beta-galactoside phosphorylases from Clostridium phytofermentans: discovery of d-galactosyl-beta1→4-l-rhamnose phosphorylase. J. Biol. Chem. 2009, 284:19220-19227.
    • (2009) J. Biol. Chem. , vol.284 , pp. 19220-19227
    • Nakajima, M.1    Nishimoto, M.2    Kitaoka, M.3
  • 27
    • 0022493894 scopus 로고
    • Synthesis of [14C] cellobiose with Clostridium thermocellum cellobiose phosphorylase
    • Ng T.K., Zeikus J.G. Synthesis of [14C] cellobiose with Clostridium thermocellum cellobiose phosphorylase. Appl. Environ. Microbiol. 1986, 52:902-904.
    • (1986) Appl. Environ. Microbiol. , vol.52 , pp. 902-904
    • Ng, T.K.1    Zeikus, J.G.2
  • 28
    • 0034329594 scopus 로고    scopus 로고
    • Role of non-covalent enzyme-substrate interactions in the reaction catalysed by cellobiose phosphorylase from Cellulomonas uda
    • Nidetzky B., Eis C., Albert M. Role of non-covalent enzyme-substrate interactions in the reaction catalysed by cellobiose phosphorylase from Cellulomonas uda. Biochem. J. 2000, 351:649-659.
    • (2000) Biochem. J. , vol.351 , pp. 649-659
    • Nidetzky, B.1    Eis, C.2    Albert, M.3
  • 29
    • 2442502648 scopus 로고    scopus 로고
    • Cellobiose phosphorylase from Cellulomonas uda: gene cloning and expression in Escherichia coli, and application of the recombinant enzyme in a 'glycosynthase-type' reaction
    • Nidetzky B., Griessler R., Schwarz A., Splechtna B. Cellobiose phosphorylase from Cellulomonas uda: gene cloning and expression in Escherichia coli, and application of the recombinant enzyme in a 'glycosynthase-type' reaction. J. Mol. Catal. B-Enzym. 2004, 29:241-248.
    • (2004) J. Mol. Catal. B-Enzym. , vol.29 , pp. 241-248
    • Nidetzky, B.1    Griessler, R.2    Schwarz, A.3    Splechtna, B.4
  • 30
    • 35548975958 scopus 로고    scopus 로고
    • Practical preparation of lacto-N-biose I, a candidate for the bifidus factor in human milk
    • Nishimoto M., Kitaoka M. Practical preparation of lacto-N-biose I, a candidate for the bifidus factor in human milk. Biosci. Biotechnol. Biochem. 2007, 71:2101-2104.
    • (2007) Biosci. Biotechnol. Biochem. , vol.71 , pp. 2101-2104
    • Nishimoto, M.1    Kitaoka, M.2
  • 32
    • 0032053291 scopus 로고    scopus 로고
    • Acceptor specificity of cellobiose phosphorylase from Cellvibrio gilvus: synthesis of three branched trisaccharides
    • Percy A., Ono H., Hayashi K. Acceptor specificity of cellobiose phosphorylase from Cellvibrio gilvus: synthesis of three branched trisaccharides. Carbohydr. Res. 1998, 308:423-429.
    • (1998) Carbohydr. Res. , vol.308 , pp. 423-429
    • Percy, A.1    Ono, H.2    Hayashi, K.3
  • 33
    • 0344972985 scopus 로고    scopus 로고
    • Synthesis of beta-d-glucopyranosyl-(1→4)-d-arabinose, beta-d-glucopyranosyl-(1→4)-l-fucose and beta-d-glucopyranosyl-(1→4)-d-altrose catalysed by cellobiose phosphorylase from Cellvibrio gilvus
    • Percy A., Ono H., Watt D., Hayashi K. Synthesis of beta-d-glucopyranosyl-(1→4)-d-arabinose, beta-d-glucopyranosyl-(1→4)-l-fucose and beta-d-glucopyranosyl-(1→4)-d-altrose catalysed by cellobiose phosphorylase from Cellvibrio gilvus. Carbohydr. Res. 1997, 305:543-548.
    • (1997) Carbohydr. Res. , vol.305 , pp. 543-548
    • Percy, A.1    Ono, H.2    Watt, D.3    Hayashi, K.4
  • 35
    • 0042201948 scopus 로고    scopus 로고
    • Characterization of a cellobiose phosphorylase from a hyperthermophilic eubacterium, Thermotoga maritima MSB8
    • Rajashekhara E., Kitaoka M., Kim Y.K., Hayashi K. Characterization of a cellobiose phosphorylase from a hyperthermophilic eubacterium, Thermotoga maritima MSB8. Biosci. Biotechnol. Biochem. 2002, 66:2578-2586.
    • (2002) Biosci. Biotechnol. Biochem. , vol.66 , pp. 2578-2586
    • Rajashekhara, E.1    Kitaoka, M.2    Kim, Y.K.3    Hayashi, K.4
  • 36
    • 78149432825 scopus 로고    scopus 로고
    • Laboratory evolution of stereoselective enzymes: a prolific source of catalysts for asymmetric reactions
    • Reetz M.T. Laboratory evolution of stereoselective enzymes: a prolific source of catalysts for asymmetric reactions. Angew. Chem. Int. Ed. Engl. 2010, 50:138-174.
    • (2010) Angew. Chem. Int. Ed. Engl. , vol.50 , pp. 138-174
    • Reetz, M.T.1
  • 37
    • 0030609809 scopus 로고    scopus 로고
    • Purification and properties of a cellobiose phosphorylase (CepA) and a cellodextrin phosphorylase (CepB) from the cellulolytic thermophile Clostridium stercorarium
    • Reichenbecher M., Lottspeich F., Bronnenmeier K. Purification and properties of a cellobiose phosphorylase (CepA) and a cellodextrin phosphorylase (CepB) from the cellulolytic thermophile Clostridium stercorarium. Eur. J. Biochem. 1997, 247:262-267.
    • (1997) Eur. J. Biochem. , vol.247 , pp. 262-267
    • Reichenbecher, M.1    Lottspeich, F.2    Bronnenmeier, K.3
  • 38
    • 0010381685 scopus 로고
    • A cellobiose phosphorylase in Clostridium thermocellum
    • Sih C.J., McBee R.H. A cellobiose phosphorylase in Clostridium thermocellum. Proc. Montana Acad. Sci. 1955, 15:21-22.
    • (1955) Proc. Montana Acad. Sci. , vol.15 , pp. 21-22
    • Sih, C.J.1    McBee, R.H.2
  • 39
    • 82955185587 scopus 로고
    • A phosphorylase active on cellobiose
    • Sih C.J., McBee R.H. A phosphorylase active on cellobiose. Bacteriol. Proc. 1955, 126.
    • (1955) Bacteriol. Proc. , pp. 126
    • Sih, C.J.1    McBee, R.H.2
  • 40
    • 65249177164 scopus 로고    scopus 로고
    • Directed enzyme evolution: climbing fitness peaks one amino acid at a time
    • Tracewell C.A., Arnold F.H. Directed enzyme evolution: climbing fitness peaks one amino acid at a time. Curr. Opin. Chem. Biol. 2009, 13:3-9.
    • (2009) Curr. Opin. Chem. Biol. , vol.13 , pp. 3-9
    • Tracewell, C.A.1    Arnold, F.H.2
  • 41
    • 33644948874 scopus 로고    scopus 로고
    • Increased amylosucrase activity and specificity, and identification of regions important for activity, specificity and stability through molecular evolution
    • van der Veen B.A., Skov L.K., Potocki-Veronese G., Gajhede M., Monsan P., Remaud-Simeon M. Increased amylosucrase activity and specificity, and identification of regions important for activity, specificity and stability through molecular evolution. FEBS J. 2006, 273:673-681.
    • (2006) FEBS J. , vol.273 , pp. 673-681
    • van der Veen, B.A.1    Skov, L.K.2    Potocki-Veronese, G.3    Gajhede, M.4    Monsan, P.5    Remaud-Simeon, M.6
  • 42
    • 58149215554 scopus 로고    scopus 로고
    • Prebiotics: present and future in food science and technology
    • Wang Y.B. Prebiotics: present and future in food science and technology. Food Res. Int. 2009, 42:8-12.
    • (2009) Food Res. Int. , vol.42 , pp. 8-12
    • Wang, Y.B.1
  • 44
    • 0034935071 scopus 로고    scopus 로고
    • Lipid, sugar and liposaccharide based delivery systems
    • Wong A., Toth I. Lipid, sugar and liposaccharide based delivery systems. Curr. Med. Chem. 2001, 8:1123-1136.
    • (2001) Curr. Med. Chem. , vol.8 , pp. 1123-1136
    • Wong, A.1    Toth, I.2
  • 45
    • 27644475316 scopus 로고    scopus 로고
    • Enhancement of thermostability of kojibiose phosphorylase from Thermoanaerobacter brockii ATCC35047 by random mutagenesis
    • Yamamoto T., Mukai K., Yamashita H., Kubota M., Fukuda S., Kurimoto M., Tsujisaka Y. Enhancement of thermostability of kojibiose phosphorylase from Thermoanaerobacter brockii ATCC35047 by random mutagenesis. J. Biosci. Bioeng. 2005, 100:212-215.
    • (2005) J. Biosci. Bioeng. , vol.100 , pp. 212-215
    • Yamamoto, T.1    Mukai, K.2    Yamashita, H.3    Kubota, M.4    Fukuda, S.5    Kurimoto, M.6    Tsujisaka, Y.7
  • 46
    • 33747750213 scopus 로고    scopus 로고
    • Construction and characterization of chimeric enzymes of kojibiose phosphorylase and trehalose phosphorylase Thermoanaerobacter brockii
    • Yamamoto T., Yamashita H., Mukai K., Watanabe H., Kubota M., Chaen H., Fukuda S. Construction and characterization of chimeric enzymes of kojibiose phosphorylase and trehalose phosphorylase Thermoanaerobacter brockii. Carbohydr. Res. 2006, 341:2350-2359.
    • (2006) Carbohydr. Res. , vol.341 , pp. 2350-2359
    • Yamamoto, T.1    Yamashita, H.2    Mukai, K.3    Watanabe, H.4    Kubota, M.5    Chaen, H.6    Fukuda, S.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.