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Volumn 30, Issue 5, 2013, Pages 536-544

Engineering transglycosidase activity into a GH51 α-l-arabinofuranosidase

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMICAL ANALYSIS; DIRECTED EVOLUTION; DNA SEQUENCE ANALYSIS; HYDROLYTIC ACTIVITIES; MOLECULAR MECHANISM; TRANS GLYCOSYLATION ACTIVITY; TRANSFER ACTIVITIES; TRANSGLYCOSYLATION;

EID: 84880176704     PISSN: 18716784     EISSN: 18764347     Source Type: Journal    
DOI: 10.1016/j.nbt.2013.04.002     Document Type: Article
Times cited : (29)

References (64)
  • 1
    • 67650620451 scopus 로고    scopus 로고
    • Recent developments in glycoside synthesis with glycosynthases and thioglycoligases
    • Rakić B., Withers S.G. Recent developments in glycoside synthesis with glycosynthases and thioglycoligases. Aust. J. Chem. 2009, 62(6):510-520.
    • (2009) Aust. J. Chem. , vol.62 , Issue.6 , pp. 510-520
    • Rakić, B.1    Withers, S.G.2
  • 2
    • 77955764751 scopus 로고    scopus 로고
    • New approaches to enzymatic glycoside synthesis through directed evolution
    • Kittl R., Withers S.G. New approaches to enzymatic glycoside synthesis through directed evolution. Carbohydr. Res. 2010, 345(10):1272-1279.
    • (2010) Carbohydr. Res. , vol.345 , Issue.10 , pp. 1272-1279
    • Kittl, R.1    Withers, S.G.2
  • 3
    • 79960588054 scopus 로고    scopus 로고
    • Precision polysaccharide synthesis catalyzed by enzymes
    • Kadokawa J. Precision polysaccharide synthesis catalyzed by enzymes. Chem. Rev. 2011, 111(7):4308-4345.
    • (2011) Chem. Rev. , vol.111 , Issue.7 , pp. 4308-4345
    • Kadokawa, J.1
  • 4
    • 79960566715 scopus 로고    scopus 로고
    • Enzymes in the synthesis of glycoconjugates
    • Schmaltz R.M., Hanson S.R., Wong C.-H. Enzymes in the synthesis of glycoconjugates. Chem. Rev. 2011, 111(7):4259-4307.
    • (2011) Chem. Rev. , vol.111 , Issue.7 , pp. 4259-4307
    • Schmaltz, R.M.1    Hanson, S.R.2    Wong, C.-H.3
  • 5
    • 33745728300 scopus 로고    scopus 로고
    • Synthesis of a library of xylogluco-oligosaccharides for active-site mapping of xyloglucan endo-transglycosylase
    • Fauré R., Saura-Valls M., Brumer H., Planas A., Cottaz S., Driguez H. Synthesis of a library of xylogluco-oligosaccharides for active-site mapping of xyloglucan endo-transglycosylase. Journal of Organic Chemistry 2006, 71(14):5151-5161.
    • (2006) Journal of Organic Chemistry , vol.71 , Issue.14 , pp. 5151-5161
    • Fauré, R.1    Saura-Valls, M.2    Brumer, H.3    Planas, A.4    Cottaz, S.5    Driguez, H.6
  • 7
    • 84856012271 scopus 로고    scopus 로고
    • Chemo-enzymatic synthesis of xylogluco-oligosaccharides and their interactions with cellulose
    • Lopez M., Fort S., Bizot H., Buléon A., Driguez H. Chemo-enzymatic synthesis of xylogluco-oligosaccharides and their interactions with cellulose. Carbohydrate Polymers 2012, 88(1):185-193.
    • (2012) Carbohydrate Polymers , vol.88 , Issue.1 , pp. 185-193
    • Lopez, M.1    Fort, S.2    Bizot, H.3    Buléon, A.4    Driguez, H.5
  • 8
    • 23044520072 scopus 로고    scopus 로고
    • Xylan and xylan derivatives - biopolymers with valuable properties. Naturally occurring xylans structures, isolation procedures and properties
    • Ebringerova A., Heinze T. Xylan and xylan derivatives - biopolymers with valuable properties. Naturally occurring xylans structures, isolation procedures and properties. Macromolecular Rapid Communications 2000, 21(9):542-556.
    • (2000) Macromolecular Rapid Communications , vol.21 , Issue.9 , pp. 542-556
    • Ebringerova, A.1    Heinze, T.2
  • 9
    • 79960227636 scopus 로고    scopus 로고
    • Adsorption of arabinoxylan on cellulosic surfaces: influence of degree of substitution and substitution pattern on adsorption characteristics
    • Köhnke T., Ostlund A., Brelid H. Adsorption of arabinoxylan on cellulosic surfaces: influence of degree of substitution and substitution pattern on adsorption characteristics. Biomacromolecules 2011, 12(7):2633-2641.
    • (2011) Biomacromolecules , vol.12 , Issue.7 , pp. 2633-2641
    • Köhnke, T.1    Ostlund, A.2    Brelid, H.3
  • 10
    • 79958248593 scopus 로고    scopus 로고
    • Prebiotic effects of wheat arabinoxylan related to the increase in Bifidobacteria, Roseburia and Bacteroides/Prevotella in diet-induced obese mice
    • Neyrinck A.M., Possemiers S., Druart C., Van de Wiele T., De Backer F., Cani P.D., et al. Prebiotic effects of wheat arabinoxylan related to the increase in Bifidobacteria, Roseburia and Bacteroides/Prevotella in diet-induced obese mice. PLoS ONE 2011, 6(6):e20944.
    • (2011) PLoS ONE , vol.6 , Issue.6
    • Neyrinck, A.M.1    Possemiers, S.2    Druart, C.3    Van de Wiele, T.4    De Backer, F.5    Cani, P.D.6
  • 11
    • 79960557953 scopus 로고    scopus 로고
    • Wheat bran arabinoxylans: chemical structure and film properties of three isolated fractions
    • Zhang Y., Pitkänen L., Douglade J., Tenkanen M., Remond C., Joly C. Wheat bran arabinoxylans: chemical structure and film properties of three isolated fractions. Carbohydrate Polymers 2011, 86(2):852-859.
    • (2011) Carbohydrate Polymers , vol.86 , Issue.2 , pp. 852-859
    • Zhang, Y.1    Pitkänen, L.2    Douglade, J.3    Tenkanen, M.4    Remond, C.5    Joly, C.6
  • 12
    • 53149116252 scopus 로고    scopus 로고
    • Biopolymer interactions affect the functional properties of edible films based on agar, cassava starch and arabinoxylan blends
    • Phan The D., Debeaufort F., Voilley A., Luu D. Biopolymer interactions affect the functional properties of edible films based on agar, cassava starch and arabinoxylan blends. Journal of Food Engineering 2009, 90(4):548-558.
    • (2009) Journal of Food Engineering , vol.90 , Issue.4 , pp. 548-558
    • Phan The, D.1    Debeaufort, F.2    Voilley, A.3    Luu, D.4
  • 13
    • 70349176149 scopus 로고    scopus 로고
    • In vitro model assemblies to study the impact of lignin-carbohydrate interactions on the enzymatic conversion of xylan
    • Boukari I., Putaux J.-L., Cathala B., Barakat A., Saake B., Rémond C., et al. In vitro model assemblies to study the impact of lignin-carbohydrate interactions on the enzymatic conversion of xylan. Biomacromolecules 2009, 10(9):2489-2498.
    • (2009) Biomacromolecules , vol.10 , Issue.9 , pp. 2489-2498
    • Boukari, I.1    Putaux, J.-L.2    Cathala, B.3    Barakat, A.4    Saake, B.5    Rémond, C.6
  • 14
    • 77955621864 scopus 로고    scopus 로고
    • Variability in fine structures of noncellulosic cell wall polysaccharides from cereal grains: potential importance in human health and nutrition
    • Collins H.M., Burton R.A., Topping D.L., Liao M., Bacic A., Fincher G.B. Variability in fine structures of noncellulosic cell wall polysaccharides from cereal grains: potential importance in human health and nutrition. Cereal Chemistry 2010, 87(4):272-282.
    • (2010) Cereal Chemistry , vol.87 , Issue.4 , pp. 272-282
    • Collins, H.M.1    Burton, R.A.2    Topping, D.L.3    Liao, M.4    Bacic, A.5    Fincher, G.B.6
  • 15
    • 78049237726 scopus 로고    scopus 로고
    • Direct conversion of xylan into alkyl pentosides
    • Bouxin F., Marinkovic S., Le Bras J., Estrine B. Direct conversion of xylan into alkyl pentosides. Carbohydr. Res. 2010, 345(17):2469-2473.
    • (2010) Carbohydr. Res. , vol.345 , Issue.17 , pp. 2469-2473
    • Bouxin, F.1    Marinkovic, S.2    Le Bras, J.3    Estrine, B.4
  • 17
    • 35449007226 scopus 로고    scopus 로고
    • Synthesis of a library of allyl α-l-arabinofuranosyl-α- or β-d-xylopyranosides; route to higher oligomers
    • Utille J.-P., Jeacomine I. Synthesis of a library of allyl α-l-arabinofuranosyl-α- or β-d-xylopyranosides; route to higher oligomers. Carbohydr. Res. 2007, 342:2649-2656.
    • (2007) Carbohydr. Res. , vol.342 , pp. 2649-2656
    • Utille, J.-P.1    Jeacomine, I.2
  • 18
    • 33751500312 scopus 로고
    • Regioselective protection strategies for d-xylopyranosides
    • Helm R.F., Ralphlb J., Anderson L. Regioselective protection strategies for d-xylopyranosides. Journal of Organic Chemistry 1991, 56(25):7015-7021.
    • (1991) Journal of Organic Chemistry , vol.56 , Issue.25 , pp. 7015-7021
    • Helm, R.F.1    Ralphlb, J.2    Anderson, L.3
  • 19
    • 0009713648 scopus 로고
    • Pentoside synthesis by dehydrative glycosylation. Synthesis of O-α-l-arabinofuranosyl-(1→3)-O-β-d-xylopyranosyl-(1→4)-d-xylopyranose
    • Koto S., Morishima N., Takenaka K., Uchida C., Zen S. Pentoside synthesis by dehydrative glycosylation. Synthesis of O-α-l-arabinofuranosyl-(1→3)-O-β-d-xylopyranosyl-(1→4)-d-xylopyranose. Bulletin of the Chemical Society of Japan 1985, 58(5):1464-1468.
    • (1985) Bulletin of the Chemical Society of Japan , vol.58 , Issue.5 , pp. 1464-1468
    • Koto, S.1    Morishima, N.2    Takenaka, K.3    Uchida, C.4    Zen, S.5
  • 20
    • 0000350844 scopus 로고
    • 13C-N.M.R. spectra of two isomeric methyl β-glycosides of trisaccharides related to arabinoxylan
    • 13C-N.M.R. spectra of two isomeric methyl β-glycosides of trisaccharides related to arabinoxylan. Carbohydr. Res. 1984, 131:219-226.
    • (1984) Carbohydr. Res. , vol.131 , pp. 219-226
    • Hirsch, J.1    Petrakova, E.2    Schraml, J.3
  • 22
    • 84856235183 scopus 로고    scopus 로고
    • Progress and future prospects for pentose-specific biocatalysts in biorefining
    • Dumon C., Song L., Bozonnet S., Fauré R., O'Donohue M.J. Progress and future prospects for pentose-specific biocatalysts in biorefining. Process Biochemistry 2012, 47(3):346-357.
    • (2012) Process Biochemistry , vol.47 , Issue.3 , pp. 346-357
    • Dumon, C.1    Song, L.2    Bozonnet, S.3    Fauré, R.4    O'Donohue, M.J.5
  • 24
    • 3142724725 scopus 로고    scopus 로고
    • Synthesis of pentose-containing disaccharides using a thermostable α-l-arabinofuranosidase
    • Rémond C., Plantier-Royon R., Aubry N., Maes E., Bliard C., O'Donohue M.J. Synthesis of pentose-containing disaccharides using a thermostable α-l-arabinofuranosidase. Carbohydr. Res. 2004, 339(11):2019-2025.
    • (2004) Carbohydr. Res. , vol.339 , Issue.11 , pp. 2019-2025
    • Rémond, C.1    Plantier-Royon, R.2    Aubry, N.3    Maes, E.4    Bliard, C.5    O'Donohue, M.J.6
  • 25
    • 13844308667 scopus 로고    scopus 로고
    • An original chemoenzymatic route for the synthesis of β-d-galactofuranosides using an α-l-arabinofuranosidase
    • Rémond C., Plantier-Royon R., Aubry N., O'Donohue M.J. An original chemoenzymatic route for the synthesis of β-d-galactofuranosides using an α-l-arabinofuranosidase. Carbohydr. Res. 2005, 340(4):637-644.
    • (2005) Carbohydr. Res. , vol.340 , Issue.4 , pp. 637-644
    • Rémond, C.1    Plantier-Royon, R.2    Aubry, N.3    O'Donohue, M.J.4
  • 26
    • 77951123284 scopus 로고    scopus 로고
    • Enzymatic synthesis of oligo-d-galactofuranosides and l-arabinofuranosides: from molecular dynamics to immunological assays
    • Chlubnová I., Filipp D., Spiwok V., Dvoráková H., Daniellou R., Nugier-Chauvin C., et al. Enzymatic synthesis of oligo-d-galactofuranosides and l-arabinofuranosides: from molecular dynamics to immunological assays. Organic & Biomolecular Chemistry 2010, 8(9):2092-2102.
    • (2010) Organic & Biomolecular Chemistry , vol.8 , Issue.9 , pp. 2092-2102
    • Chlubnová, I.1    Filipp, D.2    Spiwok, V.3    Dvoráková, H.4    Daniellou, R.5    Nugier-Chauvin, C.6
  • 27
    • 4444304036 scopus 로고    scopus 로고
    • Transglycosylation catalyzed by a Penicillium chrysogenum exo-1,5-α-l-arabinanase
    • Sakamoto T., Fujita T., Kawasaki H. Transglycosylation catalyzed by a Penicillium chrysogenum exo-1,5-α-l-arabinanase. Biochim. Biophys. Acta 2004, 1674:85-90.
    • (2004) Biochim. Biophys. Acta , vol.1674 , pp. 85-90
    • Sakamoto, T.1    Fujita, T.2    Kawasaki, H.3
  • 28
    • 33846532317 scopus 로고    scopus 로고
    • Mutagenesis and mechanistic study of a glycoside hydrolase family 54 α-l-arabinofuranosidase from Trichoderma koningii
    • Wan C.-F., Chen W.-H., Chen C.-T., Chang M.D.-T., Lo L.-C., Li Y.-K. Mutagenesis and mechanistic study of a glycoside hydrolase family 54 α-l-arabinofuranosidase from Trichoderma koningii. Biochemical Journal 2007, 401(2):551-558.
    • (2007) Biochemical Journal , vol.401 , Issue.2 , pp. 551-558
    • Wan, C.-F.1    Chen, W.-H.2    Chen, C.-T.3    Chang, M.D.-T.4    Lo, L.-C.5    Li, Y.-K.6
  • 30
    • 85045502002 scopus 로고
    • Randomization of genes by PCR mutagenesis
    • Cadwell R.C., Joyce G.F. Randomization of genes by PCR mutagenesis. Genome Res. 1992, 2:28-33.
    • (1992) Genome Res. , vol.2 , pp. 28-33
    • Cadwell, R.C.1    Joyce, G.F.2
  • 32
    • 33846591870 scopus 로고    scopus 로고
    • Directed evolution of the α-l-fucosidase from Thermotoga maritima into an α-l-transfucosidase
    • Osanjo G., Dion M., Drone J., Solleux C., Tran V., Rabiller C., et al. Directed evolution of the α-l-fucosidase from Thermotoga maritima into an α-l-transfucosidase. Biochemistry 2007, 46:1022-1033.
    • (2007) Biochemistry , vol.46 , pp. 1022-1033
    • Osanjo, G.1    Dion, M.2    Drone, J.3    Solleux, C.4    Tran, V.5    Rabiller, C.6
  • 34
    • 84866349606 scopus 로고    scopus 로고
    • Functional roles of H98 and W99 and β2α2 loop dynamics in the α-l-arabinofuranosidase from Thermobacillus xylanilyticus
    • Arab-Jaziri F., Bissaro B., Barbe S., Saurel O., Débat H., Dumon C., et al. Functional roles of H98 and W99 and β2α2 loop dynamics in the α-l-arabinofuranosidase from Thermobacillus xylanilyticus. FEBS Journal 2012, 279(19):3598-3611.
    • (2012) FEBS Journal , vol.279 , Issue.19 , pp. 3598-3611
    • Arab-Jaziri, F.1    Bissaro, B.2    Barbe, S.3    Saurel, O.4    Débat, H.5    Dumon, C.6
  • 35
    • 0034110774 scopus 로고    scopus 로고
    • Genetic and biochemical characterization of a highly thermostable α-l-arabinofuranosidase from Thermobacillus xylanilyticus
    • Debeche T., Cummings N., Connerton I., Debeire P., O'Donohue M.J. Genetic and biochemical characterization of a highly thermostable α-l-arabinofuranosidase from Thermobacillus xylanilyticus. Applied and Environment Microbiology 2000, 66(4):1734-1736.
    • (2000) Applied and Environment Microbiology , vol.66 , Issue.4 , pp. 1734-1736
    • Debeche, T.1    Cummings, N.2    Connerton, I.3    Debeire, P.4    O'Donohue, M.J.5
  • 36
    • 84889582115 scopus 로고    scopus 로고
    • NMR chemical shifts of common laboratory solvents as trace impurities
    • Gottlieb H.E., Kotlyar V., Nudelman A. NMR chemical shifts of common laboratory solvents as trace impurities. Journal of Organic Chemistry 1997, 62(21):7512-7515.
    • (1997) Journal of Organic Chemistry , vol.62 , Issue.21 , pp. 7512-7515
    • Gottlieb, H.E.1    Kotlyar, V.2    Nudelman, A.3
  • 37
    • 0034823890 scopus 로고    scopus 로고
    • Group epitope mapping by saturation transfer difference NMR to identify segments of a ligand in direct contact with a protein receptor
    • Mayer M., Meyer B. Group epitope mapping by saturation transfer difference NMR to identify segments of a ligand in direct contact with a protein receptor. J. Am. Chem. Soc. 2001, 123(25):6108-6117.
    • (2001) J. Am. Chem. Soc. , vol.123 , Issue.25 , pp. 6108-6117
    • Mayer, M.1    Meyer, B.2
  • 38
    • 0026951903 scopus 로고
    • Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions
    • Piotto M., Saudek V., Sklenár V. Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions. J. Biomol. NMR 1992, 2(6):661-665.
    • (1992) J. Biomol. NMR , vol.2 , Issue.6 , pp. 661-665
    • Piotto, M.1    Saudek, V.2    Sklenár, V.3
  • 39
    • 11944256494 scopus 로고
    • Catalytic mechanisms of enzymic glycosyl transfer
    • Sinnott M.L. Catalytic mechanisms of enzymic glycosyl transfer. Chem. Rev. 1990, 90:1171-1202.
    • (1990) Chem. Rev. , vol.90 , pp. 1171-1202
    • Sinnott, M.L.1
  • 41
    • 0033553844 scopus 로고    scopus 로고
    • Characterization of ligand binding by saturation transfer difference NMR spectroscopy
    • Mayer M., Meyer B. Characterization of ligand binding by saturation transfer difference NMR spectroscopy. Angewandte Chemie International Edition 1999, 38(12):1784-1788.
    • (1999) Angewandte Chemie International Edition , vol.38 , Issue.12 , pp. 1784-1788
    • Mayer, M.1    Meyer, B.2
  • 42
    • 0037463033 scopus 로고    scopus 로고
    • NMR spectroscopy techniques for screening and identifying ligand binding to protein receptors
    • Meyer B., Peters T. NMR spectroscopy techniques for screening and identifying ligand binding to protein receptors. Angewandte Chemie International Edition 2003, 42(8):864-890.
    • (2003) Angewandte Chemie International Edition , vol.42 , Issue.8 , pp. 864-890
    • Meyer, B.1    Peters, T.2
  • 43
    • 47249161669 scopus 로고    scopus 로고
    • The structure of the complex between a branched pentasaccharide and Thermobacillus xylanilyticus GH-51 arabinofuranosidase reveals xylan-binding determinants and induced fit
    • Paës G., Skov L.K., O'Donohue M.J., Rémond C., Kastrup J.S., Gajhede M., et al. The structure of the complex between a branched pentasaccharide and Thermobacillus xylanilyticus GH-51 arabinofuranosidase reveals xylan-binding determinants and induced fit. Biochemistry 2008, 47:7441-7451.
    • (2008) Biochemistry , vol.47 , pp. 7441-7451
    • Paës, G.1    Skov, L.K.2    O'Donohue, M.J.3    Rémond, C.4    Kastrup, J.S.5    Gajhede, M.6
  • 44
    • 0036190316 scopus 로고    scopus 로고
    • Probing the catalytically essential residues of the α-l-arabinofuranosidase from Thermobacillus xylanilyticus
    • Debeche T., Bliard C., Debeire P., O'Donohue M.J. Probing the catalytically essential residues of the α-l-arabinofuranosidase from Thermobacillus xylanilyticus. Protein Eng. 2002, 15(1):21-28.
    • (2002) Protein Eng. , vol.15 , Issue.1 , pp. 21-28
    • Debeche, T.1    Bliard, C.2    Debeire, P.3    O'Donohue, M.J.4
  • 45
    • 0028848613 scopus 로고
    • Identification of the acid/base catalyst in Agrobacterium faecalis β-glucosidase by kinetic analysis of mutants
    • Wang Q., Trimbur D., Graham R., Warren R.A.J., Withers S.G. Identification of the acid/base catalyst in Agrobacterium faecalis β-glucosidase by kinetic analysis of mutants. Biochemistry 1995, 34(44):14554-14562.
    • (1995) Biochemistry , vol.34 , Issue.44 , pp. 14554-14562
    • Wang, Q.1    Trimbur, D.2    Graham, R.3    Warren, R.A.J.4    Withers, S.G.5
  • 46
    • 0038035884 scopus 로고    scopus 로고
    • Identification of the catalytic residues in family 52 glycoside hydrolase, a β-xylosidase from Geobacillus stearothermophilus T-6
    • Bravman T., Belakhov V., Solomon D., Shoham G., Henrissat B., Baasov T., et al. Identification of the catalytic residues in family 52 glycoside hydrolase, a β-xylosidase from Geobacillus stearothermophilus T-6. Journal of Biological Chemistry 2003, 278(29):26742-26749.
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.29 , pp. 26742-26749
    • Bravman, T.1    Belakhov, V.2    Solomon, D.3    Shoham, G.4    Henrissat, B.5    Baasov, T.6
  • 47
    • 0028951034 scopus 로고
    • Enzymatic synthesis of oligosaccharides
    • Monsan P., Paul F. Enzymatic synthesis of oligosaccharides. FEMS Microbiology Review 1995, 16(2-3):187-192.
    • (1995) FEMS Microbiology Review , vol.16 , Issue.2-3 , pp. 187-192
    • Monsan, P.1    Paul, F.2
  • 48
    • 31444442746 scopus 로고    scopus 로고
    • Mutation of a conserved tryptophan in the chitin-binding cleft of Serratia marcescens chitinase A enhances transglycosylation
    • Aronson N.N., Halloran B.A., Alexeyev M.F., Zhou X.E., Wang Y., Meehan E.J., et al. Mutation of a conserved tryptophan in the chitin-binding cleft of Serratia marcescens chitinase A enhances transglycosylation. Bioscience Biotechnology and Biochemistry 2006, 70(1):243-251.
    • (2006) Bioscience Biotechnology and Biochemistry , vol.70 , Issue.1 , pp. 243-251
    • Aronson, N.N.1    Halloran, B.A.2    Alexeyev, M.F.3    Zhou, X.E.4    Wang, Y.5    Meehan, E.J.6
  • 49
    • 0036439021 scopus 로고    scopus 로고
    • 8-barrel and is critical for activity and substrate specificity
    • 8-barrel and is critical for activity and substrate specificity. Eur. J. Biochem. 2002, 269(22):5377-5390.
    • (2002) Eur. J. Biochem. , vol.269 , Issue.22 , pp. 5377-5390
    • Mori, H.1    Bak-Jensen, K.S.2    Svensson, B.3
  • 50
    • 1842813472 scopus 로고    scopus 로고
    • Crystal structures of a poplar xyloglucan endotransglycosylase reveal details of transglycosylation acceptor binding
    • Johansson P., Brumer H., Baumann M.J., Kallas A.M., Henriksson H., Denman S.E., et al. Crystal structures of a poplar xyloglucan endotransglycosylase reveal details of transglycosylation acceptor binding. Plant Cell 2004, 16(4):874-886.
    • (2004) Plant Cell , vol.16 , Issue.4 , pp. 874-886
    • Johansson, P.1    Brumer, H.2    Baumann, M.J.3    Kallas, A.M.4    Henriksson, H.5    Denman, S.E.6
  • 51
    • 0028115935 scopus 로고
    • Alteration of the cleavage mode and of the transglycosylation reactions of the xylanase A of Streptomyces lividans 1326 by site-directed mutagenesis of the Asn173 residue
    • Moreau A., Shareck F., Kluepfel D., Morosoli R. Alteration of the cleavage mode and of the transglycosylation reactions of the xylanase A of Streptomyces lividans 1326 by site-directed mutagenesis of the Asn173 residue. Eur. J. Biochem. 1994, 219(1-2):261-266.
    • (1994) Eur. J. Biochem. , vol.219 , Issue.1-2 , pp. 261-266
    • Moreau, A.1    Shareck, F.2    Kluepfel, D.3    Morosoli, R.4
  • 52
    • 0035954371 scopus 로고    scopus 로고
    • Influence of the aglycone region of the substrate binding cleft of Pseudomonas xylanase 10A on catalysis
    • Armand S., Andrews S.R., Charnock S.J., Gilbert H.J. Influence of the aglycone region of the substrate binding cleft of Pseudomonas xylanase 10A on catalysis. Biochemistry 2001, 40(25):7404-7409.
    • (2001) Biochemistry , vol.40 , Issue.25 , pp. 7404-7409
    • Armand, S.1    Andrews, S.R.2    Charnock, S.J.3    Gilbert, H.J.4
  • 53
    • 76849112035 scopus 로고    scopus 로고
    • Transglycosylation reaction catalyzed by a class V chitinase from cycad, Cycas revoluta: a study involving site-directed mutagenesis, HPLC, and real-time ESI-MS
    • Taira T., Fujiwara M., Dennhart N., Hayashi H., Onaga S., Ohnuma T., et al. Transglycosylation reaction catalyzed by a class V chitinase from cycad, Cycas revoluta: a study involving site-directed mutagenesis, HPLC, and real-time ESI-MS. Biochim. Biophys. Acta 2010, 1804(4):668-675.
    • (2010) Biochim. Biophys. Acta , vol.1804 , Issue.4 , pp. 668-675
    • Taira, T.1    Fujiwara, M.2    Dennhart, N.3    Hayashi, H.4    Onaga, S.5    Ohnuma, T.6
  • 54
    • 68949127197 scopus 로고    scopus 로고
    • Mutation of Trp137 to glutamate completely removes transglycosyl activity associated with the Aspergillus fumigatus AfChiB1
    • Lü Y., Yang H., Hu H., Wang Y., Rao Z., Jin C. Mutation of Trp137 to glutamate completely removes transglycosyl activity associated with the Aspergillus fumigatus AfChiB1. Glycoconj. J. 2009, 26(5):525-534.
    • (2009) Glycoconj. J. , vol.26 , Issue.5 , pp. 525-534
    • Lü, Y.1    Yang, H.2    Hu, H.3    Wang, Y.4    Rao, Z.5    Jin, C.6
  • 55
    • 41949130819 scopus 로고    scopus 로고
    • Mutants of Mucor hiemalis endo-β-N-acetylglucosaminidase show enhanced transglycosylation and glycosynthase-like activities
    • Umekawa M., Huang W., Li B., Fujita K., Ashida H., Wang L.-X., et al. Mutants of Mucor hiemalis endo-β-N-acetylglucosaminidase show enhanced transglycosylation and glycosynthase-like activities. Journal of Biological Chemistry 2008, 283(8):4469-4479.
    • (2008) Journal of Biological Chemistry , vol.283 , Issue.8 , pp. 4469-4479
    • Umekawa, M.1    Huang, W.2    Li, B.3    Fujita, K.4    Ashida, H.5    Wang, L.-X.6
  • 56
    • 84859486843 scopus 로고    scopus 로고
    • Remarkable transglycosylation activity of glycosynthase mutants of endo-d, an endo-β-N-acetylglucosaminidase from Streptococcus pneumoniae
    • Fan S.-Q., Huang W., Wang L.-X. Remarkable transglycosylation activity of glycosynthase mutants of endo-d, an endo-β-N-acetylglucosaminidase from Streptococcus pneumoniae. Journal of Biological Chemistry 2012, 287(14):11272-11281.
    • (2012) Journal of Biological Chemistry , vol.287 , Issue.14 , pp. 11272-11281
    • Fan, S.-Q.1    Huang, W.2    Wang, L.-X.3
  • 57
    • 67650603638 scopus 로고    scopus 로고
    • Design of α-transglucosidases of controlled specificity for programmed chemoenzymatic synthesis of antigenic oligosaccharides
    • Champion E., André I., Moulis C., Boutet J., Descroix K., Morel S., et al. Design of α-transglucosidases of controlled specificity for programmed chemoenzymatic synthesis of antigenic oligosaccharides. J. Am. Chem. Soc. 2009, 131:7379-7389.
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 7379-7389
    • Champion, E.1    André, I.2    Moulis, C.3    Boutet, J.4    Descroix, K.5    Morel, S.6
  • 58
    • 0033529853 scopus 로고    scopus 로고
    • Structural basis of the conversion of T4 lysozyme into a transglycosidase by reengineering the active site
    • Kuroki R., Weaver L.H., Matthews B.W. Structural basis of the conversion of T4 lysozyme into a transglycosidase by reengineering the active site. Proc. Natl. Acad. Sci. U.S.A. 1999, 96(16):8949-8954.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , Issue.16 , pp. 8949-8954
    • Kuroki, R.1    Weaver, L.H.2    Matthews, B.W.3
  • 59
    • 41549098189 scopus 로고    scopus 로고
    • Alternative strategy for converting an inverting glycoside hydrolase into a glycosynthase
    • Honda Y., Fushinobu S., Hidaka M., Wakagi T., Shoun H., Taniguchi H., et al. Alternative strategy for converting an inverting glycoside hydrolase into a glycosynthase. Glycobiology 2008, 18(4):325-330.
    • (2008) Glycobiology , vol.18 , Issue.4 , pp. 325-330
    • Honda, Y.1    Fushinobu, S.2    Hidaka, M.3    Wakagi, T.4    Shoun, H.5    Taniguchi, H.6
  • 61
    • 0030016344 scopus 로고    scopus 로고
    • Controlling substrate preference and transglycosylation activity of neopullulanase by manipulating steric constraint and hydrophobicity in active center
    • Kuriki T., Kaneko H., Yanase M., Takata H., Shimada J., Handa S., et al. Controlling substrate preference and transglycosylation activity of neopullulanase by manipulating steric constraint and hydrophobicity in active center. Journal of Biological Chemistry 1996, 271(29):17321-17329.
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.29 , pp. 17321-17329
    • Kuriki, T.1    Kaneko, H.2    Yanase, M.3    Takata, H.4    Shimada, J.5    Handa, S.6
  • 62
    • 66149174788 scopus 로고    scopus 로고
    • Analysis of nasturtium TmNXG1 complexes by crystallography and molecular dynamics provides detailed insight into substrate recognition by family GH16 xyloglucan endo-transglycosylases and endo-hydrolases
    • Mark P., Baumann M.J., Eklöf J.M., Gullfot F., Michel G., Kallas A.M., et al. Analysis of nasturtium TmNXG1 complexes by crystallography and molecular dynamics provides detailed insight into substrate recognition by family GH16 xyloglucan endo-transglycosylases and endo-hydrolases. Proteins: Structure, Function, and Bioinformatics 2009, 75(4):820-836.
    • (2009) Proteins: Structure, Function, and Bioinformatics , vol.75 , Issue.4 , pp. 820-836
    • Mark, P.1    Baumann, M.J.2    Eklöf, J.M.3    Gullfot, F.4    Michel, G.5    Kallas, A.M.6
  • 63
    • 34547657101 scopus 로고    scopus 로고
    • Structural evidence for the evolution of xyloglucanase activity from xyloglucan endo-transglycosylases: biological implications for cell wall metabolism
    • Baumann M.J., Eklöf J.M., Michel G., Kallas A.M., Teeri T.T., Czjzek M., et al. Structural evidence for the evolution of xyloglucanase activity from xyloglucan endo-transglycosylases: biological implications for cell wall metabolism. Plant Cell 2007, 19(6):1947-1963.
    • (2007) Plant Cell , vol.19 , Issue.6 , pp. 1947-1963
    • Baumann, M.J.1    Eklöf, J.M.2    Michel, G.3    Kallas, A.M.4    Teeri, T.T.5    Czjzek, M.6
  • 64
    • 48249092786 scopus 로고    scopus 로고
    • Elimination of competing hydrolysis and coupling side reactions of a cyclodextrin glucanotransferase by directed evolution
    • Kelly R.M., Leemhuis H., Rozeboom H.J., van Oosterwijk N., Dijkstra B.W., Dijkhuizen L. Elimination of competing hydrolysis and coupling side reactions of a cyclodextrin glucanotransferase by directed evolution. Biochemical Journal 2008, 413(3):517-525.
    • (2008) Biochemical Journal , vol.413 , Issue.3 , pp. 517-525
    • Kelly, R.M.1    Leemhuis, H.2    Rozeboom, H.J.3    van Oosterwijk, N.4    Dijkstra, B.W.5    Dijkhuizen, L.6


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