Glycosynthesis in a waterworld: New insight into the molecular basis of transglycosylation in retaining glycoside hydrolases

Biochemical Journal

Volumn 467, Issue 1, 2015, Pages 17-35

  Bissaro, Bastien ^a,b,c   Monsan, Pierre ^a,b,c,d   Fauré, Régis ^a,b,c   O'Donohue, Michael J ^a,b,c  

^a UNIVERSITÉ DE TOULOUSE   (France)

^b UMR792 INGÉNIERIE DES SYSTÈMES BIOLOGIQUES ET DES PROCÉDÉS   (France)

^c CNRS   (France)

^d INSA   (France)

Author keywords

Evolution; Glycoside hydrolase; Structure function; Transglycosylation; Transition state theory.

Indexed keywords

AMYLASE; CARBOHYDRATE; CYCLOMALTODEXTRIN GLUCANOTRANSFERASE; ENZYME; FRUCTANSUCRASE; GLUCANSUCRASE; GLYCOSIDASE; GLYCOSIDE; GLYCOSYLTRANSFERASE; SIALIDASE; SUCRASE; UNCLASSIFIED DRUG; WATER; XYLOGLUCAN ENDO TRANSGLYCOSYLASE; GLYCOPROTEIN; ISOENZYME; RECOMBINANT PROTEIN;

CARBOHYDRATE SYNTHESIS; CATALYSIS; CHEMICAL BOND; CHEMICAL REACTION; DEGLYCOSYLATION; ENZYME ENGINEERING; ENZYME SPECIFICITY; GLYCOSYLATION; GLYCOSYNTHESIS; HYDROLYSIS; NONHUMAN; PRIORITY JOURNAL; REVIEW; ANIMAL; BIOCATALYSIS; CARBOHYDRATE METABOLISM; CHEMICAL STRUCTURE; CHEMISTRY; COMPARATIVE STUDY; ENZYME ACTIVE SITE; GENETICS; HUMAN; METABOLISM; MOLECULAR EVOLUTION; PROTEIN CONFORMATION; PROTEIN ENGINEERING; THERMODYNAMICS; TRENDS;

ANIMALS; BIOCATALYSIS; CARBOHYDRATE METABOLISM; CATALYTIC DOMAIN; EVOLUTION, MOLECULAR; GLYCOPROTEINS; GLYCOSIDE HYDROLASES; GLYCOSYLATION; GLYCOSYLTRANSFERASES; HUMANS; HYDROLYSIS; ISOENZYMES; MODELS, MOLECULAR; PROTEIN CONFORMATION; PROTEIN ENGINEERING; RECOMBINANT PROTEINS; SUBSTRATE SPECIFICITY; THERMODYNAMICS;

EID: 84929941359     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20141412     Document Type: Review

References (198)

1. Varki, A., Cummings, R.D., Esko, J.D., Freeze, H.H., Stanley, P., Bertozzi, C.R., Hart, G.W. and Etzler, M.E. (2009) Essentials of Glycobiology, Cold Spring Harbor Laboratory Press, Cold Spring Harbor
2. Edelman, J. (1956) The formation of oligosaccharides by enzymic transglycosylation. Adv. Enzymol. Relat. Subj. Biochem 17, 189-232 PubMed
3. Breton, C., Fournel-Gigleux, S. and Palcic, M.M. (2012) Recent structures, evolution and mechanisms of glycosyltransferases. Curr. Opin. Struct. Biol. 22, 540-549 CrossRef PubMed
4. Lairson, L.L., Henrissat, B., Davies, G.J. and Withers, S.G. (2008) Glycosyltransferases: structures, functions, and mechanisms. Annu. Rev. Biochem. 77, 521-555 CrossRef PubMed
5. Field, R.A. (2011) Glycobiology: challenging reaction equilibria. Nat. Chem. Biol. 7, 658-659 CrossRef PubMed
6. Gantt, R.W., Peltier-Pain, P., Cournoyer, W.J. and Thorson, J.S. (2011) Using simple donors to drive the equilibria of glycosyltransferase-catalyzed reactions. Nat. Chem. Biol. 7, 685-691 CrossRef PubMed
7. Cote, G.L. and Tao, B.Y. (1990) Oligosaccharide synthesis by enzymatic transglycosylation. Glycoconj. J. 7, 145-162 CrossRef
8. Mackenzie, L.F., Wang, Q., Warren, R.A.J. and Withers, S.G. (1998) Glycosynthases: mutant glycosidases for oligosaccharide synthesis. J. Am. Chem. Soc. 120, 5583-5584 CrossRef
9. Malet, C. and Planas, A. (1998) From β-glucanase to β-glucansynthase: glycosyl transfer to α-glycosyl fluoridescatalyzed bya mutant endoglucanaselacking its catalytic nucleophile. FEBS Lett. 440, 208-212 CrossRef PubMed
10. Moracci, M., Trincone, A. and Rossi, M. (2001) Glycosynthases: new enzymes for oligosaccharide synthesis. J. Mol. Catal. B Enzym. 11, 155-163 CrossRef
11. Perugino, G., Trincone, A., Rossi, M. and Moracci, M. (2004) Oligosaccharide synthesis by glycosynthases. Trends Biotechnol. 22, 31-37 CrossRef PubMed
12. Faijes, M. and Planas, A. (2007) In vitro synthesis of artificial polysaccharides by glycosidases and glycosynthases. Carbohydr. Res. 342, 1581-1594 CrossRef PubMed
13. Rakić, B. and Withers, S.G. (2009) Recent developments in glycoside synthesis with glycosynthases and thioglycoligases. Aust. J. Chem. 62, 510-520 CrossRef
14. Cobucci-Ponzano, B. and Moracci, M. (2012) Glycosynthases as tools for the production of glycan analogs of natural products. Nat. Prod. Rep. 29, 697-709 CrossRef PubMed
15. Schmaltz, R.M., Hanson, S.R. and Wong, C.-H. (2011) Enzymes in the synthesis of glycoconjugates. Chem. Rev. 111, 4259-4307 CrossRef PubMed
16. Kobayashi, S. and Makino, A. (2009) Enzymatic polymer synthesis: an opportunity for green polymer chemistry. Chem. Rev. 109, 5288-5353 CrossRef PubMed
17. Kadokawa, J. (2011) Precision polysaccharide synthesis catalyzed by enzymes. Chem. Rev. 111, 4308-4345 CrossRef PubMed
18. Zechel, D.L. and Withers, S.G. (2000) Glycosidase mechanisms: anatomy of a finely tuned catalyst. Acc. Chem. Res. 33, 11-18 CrossRef PubMed
19. Vasella, A., Davies, G.J. and Böhm, M. (2002) Glycosidase mechanisms. Curr. Opin. Chem. Biol. 6, 619-629 CrossRef PubMed
20. Vuong, T.V. and Wilson, D.B. (2010) Glycoside hydrolases: catalytic base/nucleophile diversity. Biotechnol. Bioeng. 107, 195-205 CrossRef PubMed
21. Henrissat, B. (1991) A classification of glycosyl hydrolases based sequence similarities amino acid. Biochem. J. 280, 309-316 PubMed
22. Henrissat, B. and Davies, G. (1997) Structural and sequence-based classification of glycoside hydrolases. Curr. Opin. Struct. Biol. 7, 637-644 CrossRef PubMed
23. Lombard, V., Golaconda Ramulu, H., Drula, E., Coutinho, P.M. and Henrissat, B. (2014) The carbohydrate-active enzymes database (CAZy) in 2013. Nucleic Acids Res. 42, D490-D495 CrossRef PubMed
24. Street, I.P., Kempton, J.B. and Withers, S.G. (1992) Inactivation of a β-glucosidase through the accumulation of a stable 2-deoxy-2-fluoro-α-D-glucopyranosyl-enzyme intermediate: a detailed investigation. Biochemistry 31, 9970-9978 CrossRef PubMed
25. Ducros, M.-A., Tarling, C.A., Zechel, D.L., Brzozowski, A.M., Frandsen, T.P., von Ossowski, I., Withers, S.G. and Davies, G.J. (2003) Anatomy of glycosynthesis: structure and kinetics of the Humicola insolens Cel7B E197A and E197S glycosynthase mutants. Chem. Biol. 10, 619-628 CrossRef PubMed
26. Koshland, Jr, D.E. (1953) Stereochemistry and the mechanism of enzymatic reactions. Biol. Rev. 28, 416-436 CrossRef
27. Eisenthal, R., Danson, M.J. and Hough, D.W. (1997) Catalytic efficiency and kcat /Km :a useful comparator? Trends Biotechnol. 25, 247-249 CrossRef PubMed
28. Johnson, K.A. (2013) A century of enzyme kinetic analysis, 1913 to 2013. FEBS Lett. 587, 2753-2766 CrossRef PubMed
29. Fischer, E. (1894) Einfluss der configuration auf die wirkung der enzyme. Ber. Dtsch. Chem. Ges. 27, 2985-2993 CrossRef
30. Koshland, D.E. (1995) The key-lock theory and the induced fit theory. Angew. Chem. Int. Ed. 33, 2375-2378 CrossRef
31. Davies, G.J., Wilson, K.S. and Henrissat, B. (1997) Nomenclature for sugar-binding subsites in glycosyl hydrolases. Biochem. J. 321, 557-559 PubMed
32. Wolfenden, R. and Snider, M.J. (2001) The depth of chemical time and the power of enzymes as catalysts. Acc. Chem. Res. 34, 938-945 CrossRef PubMed
33. Pauling, L. (1946) Molecular architecture and biological reactions. Chem. Eng. News 24, 1375-1377 CrossRef
34. Wolfenden, R., Lu, X. and Young, G. (1998) Spontaneous hydrolysis of glycosides. J. Am. Chem. Soc. 120, 6814-6815 CrossRef
35. Eyring, H. (1935) The activated complex in chemical reactions. J. Chem. Phys. 3, 107-115 CrossRef
36. Warshel, A. (1981) Electrostatic basis of structure-function correlation in proteins. Acc. Chem. Res. 14, 284-290 CrossRef
37. Tokuriki, N. and Tawfik, D.S. (2009) Protein dynamism and evolvability. Science 324, 203-207 CrossRef PubMed
38. Chouard, T. (2011) Breaking the protein rules. Nature 471, 151-153 CrossRef PubMed
39. Glowacki, D.R., Harvey, J.N. and Mulholland, A.J. (2012) Taking Ockham's razor to enzyme dynamics and catalysis. Nat. Chem. 4, 169-176 CrossRef PubMed
40. Davies, G.J., Ducros, V. M.-A., Varrot, A. and Zechel, D.L. (2003) Mapping the conformational itinerary of β-glycosidases by X-ray crystallography. Biochem. Soc. Trans. 31, 523-527 CrossRef PubMed
41. Taha, H.A., Richards, M.R. and Lowary, T.L. (2013) Conformational analysis of furanoside-containing mono- and oligosaccharides. Chem. Rev. 113, 1851-1876 CrossRef PubMed
42. Houseknecht, J.B., Altona, C., Hadad, C.M. and Lowary, T.L. (2002) Conformational analysis of furanose rings with PSEUROT: parametrization for rings possessing the arabino, lyxo, ribo, and xylo stereochemistry and application to arabinofuranosides. J. Org. Chem. 67, 4647-4651 CrossRef PubMed
43. Sinnott, M.L. (1990) Catalytic mechanism of enzymic glycosyl transfer. Chem. Rev. 90, 1171-1202 CrossRef
44. Vocadlo, D.J. and Davies, G.J. (2008) Mechanistic insights into glycosidase chemistry. Curr. Opin. Chem. Biol. 12, 539-555 CrossRef PubMed
45. Hovel, K., Shallom, D., Niefind, K., Belakhov, V., Shoham, G., Baasov, T., Shoham, Y. and Schomburg, D. (2003) Crystal structure and snapshots along the reaction pathway of a family 51 α-L-arabinofuranosidase. EMBO J. 22, 4922-4932 CrossRef PubMed
46. Davies, G.J., Planas, A. and Rovira, C. (2012) Conformational analyses of the reaction coordinate of glycosidases. Acc. Chem. Res. 45, 308-316 CrossRef PubMed
47. Sulzenbacher, G., Driguez, H., Henrissat, B., Schülein, M. and Davies, G.J. (1996) Structure of the Fusarium oxysporum endoglucanase I with a nonhydrolyzable substrate analogue: substrate distortion gives rise to the preferred axial orientation for the leaving group. Biochemistry 35, 15280-15287 CrossRef PubMed
48. Davies, G.J., Mackenzie, L., Varrot, A., Dauter, M. and Brzozowski, A.M. (1998) Snapshots along an enzymatic reaction coordinate: analysis of a retaining β-glycosidase. Biochemistry 37, 11707-11713 CrossRef PubMed
49. Biarnés, X., Nieto, J., Planas, A. and Rovira, C. (2006) Substrate distortion in the Michaelis complex of Bacillus 1,3-1,4-β-glucanase. Insight from first principles molecular dynamics simulations. J. Biol. Chem. 281, 1432-1441 CrossRef PubMed
50. Biarnés, X., Ardèvol, A., Iglesias-Fernández, J., Planas, A. and Rovira, C. (2011) Catalytic itinerary in 1,3-1,4-β-glucanase unraveled by QM/MM metadynamics. Charge is not yet fully developed at the oxocarbenium ion-like transition state. J. Am. Chem. Soc. 133, 20301-20309 CrossRef PubMed
51. Zechel, D.L., Reid, S.P., Stoll, D., Nashiru, O., Warren, R.A.J. and Withers, S.G. (2003) Mechanism, mutagenesis, and chemical rescue of a β-mannosidase from Cellulomonas fimi. Biochemistry 42, 7195-7204 CrossRef PubMed
52. Namchuk, M.N. and Withers, S.G. (1995) Mechanism of Agrobacterium β-glucosidase: kinetic analysis of the role of noncovalent enzyme/substrate interactions. Biochemistry 34, 16194-16202 CrossRef PubMed
53. Notenboom, V., Birsan, C., Nitz, M., Rose, D.R., Warren, R. and Withers, S.G. (1998) Insights into transition state stabilization of the β-1,4-glycosidase Cex by covalent intermediate accumulation in active site mutants. Nat. Struct. Biol. 5, 812-818 CrossRef PubMed
54. Sierks, M.R. and Svensson, B. (1992) Kinetic identification of a hydrogen bonding pair in the glucoamylase-maltose transition state complex. Protein Eng. 5, 185-188 CrossRef PubMed
55. Kim, Y.-W., Zhang, R., Chen, H. and Withers, S.G. (2010) O-glycoligases, a new category of glycoside bond-forming mutant glycosidases, catalyse facile syntheses of isoprimeverosides. Chem. Commun. 46, 8725-8727 CrossRef PubMed
56. Heightman, T.D. and Vasella, A.T. (1999) Recent insights into inhibition, structure, and mechanism of configuration-retaining glycosidases. Angew. Chem. Int. Ed. 38, 750-770 CrossRef
57. Nerinckx, W., Desmet, T., Piens, K. and Claeyssens, M. (2005) An elaboration on the syn-anti proton donor concept of glycoside hydrolases: electrostatic stabilisation of the transition state as a general strategy. FEBS Lett. 579, 302-312 CrossRef PubMed
58. Nerinckx, W., Desmet, T. and Claeyssens, M. (2003) A hydrophobic platform as a mechanistically relevant transition state stabilising factor appears to be present in the active centre of all glycoside hydrolases. FEBS Lett. 538, 1-7CrossRef PubMed
59. Schramm, V.L. (2011) Enzymatic transition states, transition-state analogs, dynamics, thermodynamics, and lifetimes. Annu. Rev. Biochem. 80, 703-732 CrossRef PubMed
60. Bigeleisen, J. and Mayer, M.G. (1947) Calculation of equilibrium constants for isotopic exchange reactions. J. Chem. Phys. 15, 261-267 CrossRef
61. Cleland, W.W. (2003) The use of isotope effects to determine enzyme mechanisms. J. Biol. Chem. 278, 51975-51984 CrossRef PubMed
62. Kempton, J.B. and Withers, S.G. (1992) Mechanism of Agrobacterium β-glucosidase: kinetic studies. Biochemistry 31, 9961-9969 CrossRef PubMed
63. Wang, J., Hou, Q., Sheng, X., Gao, J., Liu, Y. and Liu, C. (2013) Theoretical study on the deglycosylation mechanism of rice BGlu1 β-glucosidase. Int. J. Quantum Chem. 113, 1071-1075 CrossRef
64. Wang, J., Hou, Q., Dong, L., Liu, Y. and Liu, C. (2011) QM/MM studies on the glycosylation mechanism of rice BGlu1 β-glucosidase. J. Mol. Graph. Model. 30, 148-152 CrossRef PubMed
65. Brás, N.F., Ramos, M.J. and Fernandes, P.A. (2010) DFT studies on the β-glycosidase catalytic mechanism: the deglycosylation step. J. Mol. Struct. THEOCHEM 946, 125-133 CrossRef
66. Badieyan, S., Bevan, D.R. and Zhang, C. (2012) Probing the active site chemistry of β-glucosidases along the hydrolysis reaction pathway. Biochemistry 51, 8907-8918 CrossRef PubMed
67. Demetrius, L. (1998) Role of enzyme-substrate flexibility in catalytic activity: an evolutionary perspective. J. Theor. Biol. 194, 175-194 CrossRef PubMed
68. del-Rio, G., Morett, E. and Soberon, X. (1997) Did cyclodextrin glycosyltransferases evolve from α-amylases? FEBS Lett. 416, 221-224 CrossRef PubMed
69. Ritsema, T., Hernández, L., Verhaar, A., Altenbach, D., Boller, T., Wiemken, A. and Smeekens, S. (2006) Developing fructan-synthesizing capability in a plant invertase via mutations in the sucrose-binding box. Plant J. 48, 228-237 CrossRef PubMed
70. Luang, S., Cho, J.-I., Mahong, B., Opassiri, R., Akiyama, T., Phasai, K., Komvongsa, J., Sasaki, N., Hua, Y., Matsuba, Y. et al. (2013) Rice Os9BGlu31 is a transglucosidase with the capacity to equilibrate phenylpropanoid, flavonoid, and phytohormone glycoconjugates. J. Biol. Chem. 288, 10111-10123 CrossRef PubMed
71. Schröder, R., Atkinson, R.G. and Redgwell, R.J. (2009) Re-interpreting the role of endo-β-mannanases as mannan endotransglycosylase/hydrolases in the plant cell wall. Ann. Bot. 104, 197-204 CrossRef PubMed
72. Johnston, S.L., Prakash, R., Chen, N.J., Kumagai, M.H., Turano, H.M., Cooney, J.M., Atkinson, R.G., Paull, R.E., Cheetamun, R., Bacic, A. et al. (2013) An enzyme activity capable of endotransglycosylation of heteroxylan polysaccharides is present in plant primary cell walls. Planta 237, 173-187 CrossRef PubMed
73. Franková, L. and Fry, S.C. (2011) Phylogenetic variation in glycosidases and glycanases acting on plant cell wall polysaccharides, and the detection of transglycosidase and trans-β-xylanase activities. Plant J. 67, 662-681 CrossRef PubMed
74. Franková, L. and Fry, S.C. (2012) Trans-α-xylosidase and trans-β-galactosidase activities, widespread in plants, modify and stabilize xyloglucan structures. Plant J. 71, 45-60 CrossRef PubMed
75. Fry, S.C. (2004) Primary cell wall metabolism: tracking the careers of wall polymers in living plant cells. New Phytol. 161, 641-675 CrossRef
76. van der Veen, B.A., Uitdehaag, J.C., Penninga, D., van Alebeek, G.J., Smith, L.M., Dijkstra, B.W. and Dijkhuizen, L. (2000) Rational design of cyclodextrin glycosyltransferase from Bacillus circulans strain 251 to increase α-cyclodextrin production. J. Mol. Biol. 296, 1027-1038 CrossRef PubMed
77. Mori, H., Bak-Jensen, K.S. and Svensson, B. (2002) Barley α-amylase Met53 situated at the high-affinity subsite - 2 belongs to a substratebinding motif in theβ→α loop 2 of the catalytic (β/α)8-barrel and is critical for activity and substrate specificity. Eur. J. Biochem. 269, 5377-5390 CrossRef PubMed
78. Potocki de Montalk, G., Remaud-Simeon, M., Willemot, R.M., Sarçabal, P., Planchot, V. and Monsan, P. (2000) Amylosucrase from Neisseria polysaccharea: novel catalytic properties. FEBS Lett. 471, 219-223 CrossRef PubMed
79. Kim, M.-I., Kim, H.-S., Jung, J. and Rhee, S. (2008) Crystal structures and mutagenesis of sucrose hydrolase from Xanthomonas axonopodis pv. glycines: insight into the exclusively hydrolytic amylosucrase fold. J. Mol. Biol. 380, 636-647 CrossRef PubMed
80. Baumann, M.J., Eklöf, J.M., Michel, G., Kallas, A.M., Teeri, T.T., Czjzek, M. and Brumer, H. (2007) Structural evidence for the evolution of xyloglucanase activity from xyloglucan endo-transglycosylases: biological implications for cell wall metabolism. Plant Cell 19, 1947-1963 CrossRef PubMed
81. Schroeven, L., Lammens, W., Van Laere, A. and Van den Ende, W. (2008) Transforming wheat vacuolar invertase into a high affinity sucrose: sucrose 1-fructosyltransferase. New Phytol. 180, 822-831 CrossRef PubMed
82. Ribeirâo, M., Pereira-Chioccola, V.L., Eichinger, D., Rodrigues, M.M. and Schenkman, S. (1997) Temperature differences for trans-glycosylation and hydrolysis reaction reveal an acceptor binding site in the catalytic mechanism of Trypanosoma cruzi trans-sialidase. Glycobiology 7, 1237-1246 CrossRef PubMed
83. Paris, G., Ratier, L., Amaya, M.F., Nguyen, T., Alzari, P.M. and Frasch, A.C.C. (2005) A sialidase mutant displaying trans-sialidase activity. J. Mol. Biol. 345, 923-934 CrossRef PubMed
84. Fry, S.C., York, W.S., Albersheim, P., Darvill, A., Hayashi, T., Joseleau, J.-P., Kato, Y., Lorences, E.P., Maclachlan, G.A., McNeil, M. et al. (1993) An unambigous nomenclature for xyloglucan-derived oligosaccharides. Physiol. Plant. 89, 1-3CrossRef
85. Gilbert, H.J., Stålbrand, H. and Brumer, H. (2008) How the walls come crumbling down: recent structural biochemistry of plant polysaccharide degradation. Curr. Opin. Plant Biol. 11, 338-348 CrossRef PubMed
86. Strohmeier, M., Hrmova, M., Fischer, M., Harvey, A.J., Fincher, G.B. and Pleiss, J. (2004) Molecular modeling of family GH16 glycoside hydrolases: potential roles for xyloglucan transglucosylases/hydrolases in cell wall modification in the poaceae. Protein Sci. 13, 3200-3213 CrossRef PubMed
87. Campbell, P. and Braam, J. (1999) Xyloglucan endotransglycosylases: diversity of genes, enzymes and potential wall-modifying functions. Trends Plant. Sci. 4, 361-366 CrossRef PubMed
88. Rose, J.K.C., Braam, J., Fry, S.C. and Nishitani, K. (2002) The XTH family of enzymes involved in xyloglucan endotransglucosylation and endohydrolysis: current perspectives and a new unifying nomenclature. Plant Cell Physiol. 43, 1421-1435 CrossRef PubMed
89. Eklöf, J.M. and Brumer, H. (2010) The XTH gene family: an update on enzyme structure, function, and phylogeny in xyloglucan remodeling. Plant Physiol. 153, 456-466 CrossRef PubMed
90. Saura-Valls, M., Fauré, R., Ragàs, S., Piens, K., Brumer, H., Teeri, T.T., Cottaz, S., Driguez, H. and Planas, A. (2006) Kinetic analysis using low-molecular mass xyloglucan oligosaccharides defines the catalytic mechanism of a Populus xyloglucan endotransglycosylase. Biochem. J. 395, 99-106 CrossRef PubMed
91. Saura-Valls, M., Fauré, R., Brumer, H., Teeri, T.T., Cottaz, S., Driguez, H. and Planas, A. (2008) Active-site mapping of a Populus xyloglucan endo-transglycosylase with a library of xylogluco-oligosaccharides. J. Biol. Chem. 283, 21853-21863 CrossRef PubMed
92. Piens, K., Fauré, R., Sundqvist, G., Baumann, M.J., Saura-Valls, M., Teeri, T.T., Cottaz, S., Planas, A., Driguez, H. and Brumer, H. (2008) Mechanism-based labeling defines the free energy change for formation of the covalent glycosyl-enzyme intermediate in a xyloglucan endo-transglycosylase. J. Biol. Chem. 283, 21864-21872 CrossRef PubMed
93. Steele, N.M. and Fry, S.C. (1999) Purification of xyloglucan endotransglycosylases (XETs): a generally applicable and simple method based on reversible formation of an enzyme-substrate complex. Biochem. J. 340, 207-211 CrossRef PubMed
94. Sulová, Z., Takáèová, M., Steele, N.M., Fry, S.C. and Farkaš, V. (1998) Xyloglucan endotransglycosylase: evidence for the existence of a relatively stable glycosyl-enzyme intermediate. Biochem. J. 330, 1475-1480 PubMed
95. Johansson, P., Brumer, H., Baumann, M.J., Kallas, A.M., Henriksson, H., Denman, S.E., Teeri, T.T. and Jones, T.A. (2004) Crystal structures of a poplar xyloglucan endotransglycosylase reveal details of transglycosylation acceptor binding. Plant Cell 16, 874-886 CrossRef PubMed
96. Fauré, R., Saura-Valls, M., Brumer, H., Planas, A., Cottaz, S. and Driguez, H. (2006) Synthesis of a library of xylogluco-oligosaccharides for active-site mapping of xyloglucan endo-transglycosylase. J. Org. Chem. 71, 5151-5161 CrossRef PubMed
97. Eklöf, J.M., Shojania, S., Okon, M., McIntosh, L.P. and Brumer, H. (2013) Structure-function analysis of a broad specificity Populus trichocarpa endo-β-glucanase reveals an evolutionary link between bacterial licheninases and plant XTH gene products. J. Biol. Chem. 288, 15786-15799 CrossRef PubMed
98. Mark, P., Baumann, M.J., Eklöf, J.M., Gullfot, F., Michel, G., Kallas, A.M., Teeri, T.T., Brumer, H. and Czjzek, M. (2009) 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 75, 820-836 CrossRef PubMed
99. Monsan, P., Remaud-Siméon, M. and André, I. (2010) Transglucosidases as efficient tools for oligosaccharide and glucoconjugate synthesis. Curr. Opin. Microbiol. 13, 293-300 CrossRef PubMed
100. van Hijum, S. A. F. T., Kralj, S., Ozimek, L.K., Dijkhuizen, L. and van Geel-Schutten, I.G.H. (2006) Structure-function relationships of glucansucrase and fructansucrase enzymes from lactic acid bacteria. Microbiol. Mol. Biol. Rev. 70, 157-176 CrossRef PubMed
101. Monchois, V., Willemot, R.M. and Monsan, P. (1999) Glucansucrases: mechanism of action and structure-function relationships. FEMS Microbiol. Rev. 23, 131-151 PubMed
102. Leemhuis, H., Pijning, T., Dobruchowska, J.M., van Leeuwen, S.S., Kralj, S., Dijkstra, B.W. and Dijkhuizen, L. (2013) Glucansucrases: three-dimensional structures, reactions, mechanism, α-glucan analysis and their implications in biotechnology and food applications. J. Biotechnol. 163, 250-272 CrossRef PubMed
103. Stam, M.R., Danchin, E.G.J., Rancurel, C., Coutinho, P.M. and Henrissat, B. (2006) Dividing the large glycoside hydrolase family 13 into subfamilies: towards improved functional annotations of α-amylase-related proteins. Protein Eng. Des. Sel. 19, 555-562 CrossRef PubMed
104. Vujicic-Zagar, A., Pijning, T., Kralj, S., López, C.A. and Eeuwema, W. (2010) Crystal structure of a 117 kDa glucansucrase fragment provides insight into evolution and product specificity of GH70 enzymes. Proc. Natl. Acad. Sci. U.S.A. 107, 21406-21411 CrossRef PubMed
105. Ito, K., Ito, S., Shimamura, T., Weyand, S., Kawarasaki, Y., Misaka, T., Abe, K., Kobayashi, T., Cameron, A.D. and Iwata, S. (2011) Crystal structure of glucansucrase from the dental caries pathogen Streptococcus mutans. J.Mol.Biol.408, 177-186 CrossRef PubMed
106. Brison, Y., Pijning, T., Malbert, Y., Fabre, É., Mourey, L., Morel, S., Potocki-Véronèse, G., Monsan, P., Tranier, S., Remaud-Siméon, M. and Dijkstra, B.W. (2012) Functional and structural characterization of α-(1→2) branching sucrase derived from DSR-E glucansucrase. J. Biol. Chem. 287, 7915-7924 CrossRef PubMed
107. Leemhuis, H., Pijning, T., Dobruchowska, J.M., Dijkstra, B.W. and Dijkhuizen, L. (2012) Glycosidic bond specificity of glucansucrases: on the role of acceptor substrate binding residues. Biocatal. Biotransform. 30, 366-376 CrossRef
108. Kralj, S., van Geel-Schutten, G.H., van der Maarel, M. J. E. C. and Dijkhuizen, L. (2004) Biochemical and molecular characterization of Lactobacillus reuteri 121 reuteransucrase. Microbiology 150, 2099-2112 CrossRef PubMed
109. Kralj, S., van Leeuwen, S.S., Valk, V., Eeuwema, W., Kamerling, J.P. and Dijkhuizen, L. (2008) Hybrid reuteransucrase enzymes reveal regions important for glucosidic linkage specificity and the transglucosylation/hydrolysis ratio. FEBS J. 275, 6002-6010 CrossRef PubMed
110. Goldberg, R.N., Tewaril, Y.B. and Ahluwaliaq, J.C. (1989) Thermodynamics of the hydrolysis of sucrose. J. Biol. Chem. 264, 9901-9904 PubMed
111. Kralj, S., Grijpstra, P., van Leeuwen, S.S., Leemhuis, H., Dobruchowska, J.M., van der Kaaij, R.M., Malik, A., Oetari, A., Kamerling, J.P. and Dijkhuizen, L. (2011) 4,6-α-Glucanotransferase, a novel enzyme that structurally and functionally provides an evolutionary link between glycoside hydrolase enzyme families 13 and 70. Appl. Environ. Microbiol. 77, 8154-8163 CrossRef PubMed
112. Skov, L.K., Mirza, O., Henriksen, A., De Montalk, G.P., Remaud-Siméon, M., Sarçabal, P., Willemot, R.M., Monsan, P. and Gajhede, M. (2001) Amylosucrase, a glucan-synthesizing enzyme from the α-amylase family. J. Biol. Chem. 276, 25273-25278 CrossRef PubMed
113. Guérin, F., Barbe, S., Pizzut-Serin, S., Potocki-Véronèse, G., Guieysse, D., Guillet, V., Monsan, P., Mourey, L., Remaud-Siméon, M., André, I. and Tranier, S. (2012) Structural investigation of the thermostability and product specificity of amylosucrase from the bacterium Deinococcus geothermalis. J. Biol. Chem. 287, 6642-6654 CrossRef PubMed
114. Albenne, C., Skov, L.K., Mirza, O., Gajhede, M., Feller, G., D'Amico, S., André, G., Potocki-Véronèse, G., van der Veen, B., Monsan, P. and Remaud-Simeon, M. (2004) Molecular basis of the amylose-like polymer formation catalyzed by Neisseria polysaccharea amylosucrase. J. Biol. Chem. 279, 726-734 CrossRef PubMed
115. Cambon, E., Barbe, S., Pizzut-Serin, S., Remaud-Simeon, M. and André, I. (2014) Essential role of amino acid position 226 in oligosaccharide elongation by amylosucrase from Neisseria polysaccharea. Biotechnol. Bioeng. 111, 1719-1728 CrossRef PubMed
116. Champion, E., Guérin, F., Moulis, C., Barbe, S., Tran, T.H., Morel, S., Descroix, K., Monsan, P., Mourey, L., Mulard, L. et al. (2012) Applying pairwise combinations of amino acid mutations for sorting out highly efficient glucosylation tools for chemo-enzymatic synthesis of bacterial oligosaccharides. J. Am. Chem. Soc. 134, 18677-18688 CrossRef PubMed
117. Daudé, D., Champion, E., Morel, S., Guieysse, D., Remaud-Siméon, M. and André, I. (2013) Probing substrate promiscuity of amylosucrase from Neisseria polysaccharea. ChemCatChem 5, 2288-2295 CrossRef
118. Kim, H., Park, H., Heu, S. and Jung, J. (2004) Molecular and functional characterization of a unique sucrose hydrolase from Xanthomonas axonopodis pv. glycines. J. Bacteriol. 186, 411-418 CrossRef PubMed
119. Skov, L.K., Pizzut-Serin, S., Remaud-Siméon, M., Ernst, H.A., Gajhede, M. and Mirza, O. (2013) The structure of amylosucrase from Deinococcus radiodurans has an unusual open active-site topology. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 69, 973-978 CrossRef PubMed
120. Pizzut-Serin, S., Potocki-Véronèse, G., van der Veen, B.A., Albenne, C., Monsan, P. and Remaud-Siméon, M. (2005) Characterisation of a novel amylosucrase from Deinococcus radiodurans. FEBS Lett. 579, 1405-1410 CrossRef PubMed
121. Olvera, C., Centeno-Leija, S., Ruiz-Leyva, P. and López-Munguía, A. (2012) Design of chimeric levansucrases with improved transglycosylation activity. Appl. Environ. Microbiol. 78, 1820-1825 CrossRef PubMed
122. Lammens, W., Le Roy, K., Schroeven, L., Van Laere, A., Rabijns, A. and Van den Ende, W. (2009) Structural insights into glycoside hydrolase family 32 and 68 enzymes: functional implications. J. Exp. Bot. 60, 727-740 CrossRef PubMed
123. Van den Ende, W., Lammens, W., Van Laere, A., Schroeven, L. and Le Roy, K. (2009) Donor and acceptor substrate selectivity among plant glycoside hydrolase family 32 enzymes. FEBS J. 276, 5788-5798 CrossRef PubMed
124. Sainz-Polo, M.A., Ramírez-Escudero, M., Lafraya, A., González, B., Marín-Navarro, J., Polaina, J. and Sanz-Aparicio, J. (2013) Three-dimensional structure of Saccharomyces invertase: role of a non-catalytic domain in oligomerization and substrate specificity. J. Biol. Chem. 288, 9755-9766 CrossRef PubMed
125. Lafraya, Á., Sanz-Aparicio, J., Polaina, J. and Marín-Navarro, J. (2011) Fructo-oligosaccharide synthesis by mutant versions of Saccharomyces cerevisiae invertase. Appl. Environ. Microbiol. 77, 6148-6157 CrossRef PubMed
126. Ritsema, T., Verhaar, A., Vijn, I. and Smeekens, S. (2005) Using natural variation to investigate the function of individual amino acids in the sucrose-binding box of fructan:fructan 6G-fructosyltransferase (6G-FFT) in product formation. Plant Mol. Biol. 58, 597-607 CrossRef PubMed
127. Altenbach, D., Rudiño-Pinera, E., Olvera, C., Boller, T., Wiemken, A. and Ritsema, T. (2009) An acceptor-substrate binding site determining glycosyl transfer emerges from mutant analysis of a plant vacuolar invertase and a fructosyltransferase. Plant Mol. Biol. 69, 47-56 CrossRef PubMed
128. Álvaro-Benito, M., Sainz-Polo, M.A., González-Pérez, D., González, B., Plou, F.J., Fernández-Lobato, M. and Sanz-Aparicio, J. (2012) Structural and kinetic insights reveal that the amino acid pair Gln228/Asn254 modulates the transfructosylating specificity of Schwanniomyces occidentalis β-fructofuranosidase, an enzyme that produces prebiotics. J. Biol. Chem. 287, 19674-19686 CrossRef PubMed
129. Uitdehaag, J.C.M. (1999) The cyclization mechanism of cyclodextrin glycosyltransferase (CGTase) as revealed by a γ-cyclodextrin-CGTase complex at 1.8-Å resolution. J. Biol. Chem. 274, 34868-34876 CrossRef PubMed
130. Leemhuis, H., Kelly, R.M. and Dijkhuizen, L. (2010) Engineering of cyclodextrin glucanotransferases and the impact for biotechnological applications. Appl. Microbiol. Biotechnol. 85, 823-835 CrossRef PubMed
131. Van der Veen, B.A., Leemhuis, H., Kralj, S., Uitdehaag, J.C., Dijkstra, B.W. and Dijkhuizen, L. (2001) Hydrophobic amino acid residues in the acceptor binding site are main determinants for reaction mechanism and specificity of cyclodextrin-glycosyltransferase. J. Biol. Chem. 276, 44557-44562 CrossRef PubMed
132. Kelly, R.M., Leemhuis, H. and Dijkhuizen, L. (2007) Conversion of a cyclodextrin glucanotransferase into an α-amylase: assessment of directed evolution strategies. Biochemistry 46, 11216-11222 CrossRef PubMed
133. Rivera, M.H., López-Munguía, A., Soberón, X. and Saab-Rincón, G. (2003) α-Amylase from Bacillus licheniformis mutants near to the catalytic site: effects on hydrolytic and transglycosylation activity. Protein Eng. 16, 505-514 CrossRef PubMed
134. Kim, T., Park, C., Cho, H., Cha, S., Kim, J., Lee, S., Moon, T., Kim, J., Oh, B. and Park, K. (2000) Role of the glutamate 332 residue in the transglycosylation activity of Thermus maltogenic amylase. Biochemistry 39, 6773-6780 CrossRef PubMed
135. Tran, P.L., Cha, H.-J., Lee, J.-S., Park, S.-H., Woo, E.-J. and Park, K.-H. (2014) Introducing transglycosylation activity in Bacillus licheniformis α-amylase by replacement of His235 with Glu. Biochem. Biophys. Res. Commun. 451, 541-547 CrossRef PubMed
136. Beier, L., Svendsen, A., Andersen, C., Frandsen, T.P., Borchert, T.V. and Cherry, J.R. (2000) Conversion of the maltogenic α-amylase Novamyl into a CGTase. Protein Eng. 13, 509-513 CrossRef PubMed
137. Jemli, S., Ben-Ali, M., Ben-Hlima, H., Khemakhem, B. and Bejar, S. (2012) Mutations affecting the activity of the cyclodextrin glucanotransferase of Paenibacillus pabuli US132: insights into the low hydrolytic activity of cyclodextrin glucanotransferases. Biologia 67, 636-643 CrossRef
138. Asensio, J.L., Ardá, A., Cañada, F.J. and Jiménez-Barbero, J. (2013) Carbohydrate-aromatic interactions. Acc. Chem. Res. 46, 946-954 CrossRef PubMed
139. Janeček, S. and Blesák, K. (2011) Sequence-structural features and evolutionary relationships of family GH57 α-amylases and their putative α-amylase-like homologues. Protein J. 30, 429-435 CrossRef PubMed
140. Janeček, S., Svensson, B. and MacGregor, E.A. (2003) Relation between domain evolution, specificity, and taxonomy of the α-amylase family members containing a C-terminal starch-binding domain. Eur. J. Biochem. 270, 635-645 CrossRef PubMed
141. Sun, T., Letsididi, R., Pan, B. and Jiang, B. (2013) Production of a novel cyclodextrin glycosyltransferase from Bacillus sp. SK13.002. Afr. J. Microbiol. Res. 7, 2311-2315
142. Bornscheuer, U.T. and Kazlauskas, R.J. (2004) Catalytic promiscuity in biocatalysis: using old enzymes to form new bonds and follow new pathways. Angew. Chem. Int. Ed. 43, 6032-6040 CrossRef PubMed
143. Watts, A.G., Damager, I., Amaya, M.L., Buschiazzo, A., Alzari, P., Frasch, A.C. and Withers, S.G. (2003) Trypanosoma cruzi trans-sialidase operates through a covalent sialyl-enzyme intermediate: tyrosine is the catalytic nucleophile. J. Am. Chem. Soc. 125, 7532-7533 CrossRef PubMed
144. Amaya, M.F., Watts, A.G., Damager, I., Wehenkel, A., Nguyen, T., Buschiazzo, A., Paris, G., Frasch, A.C., Withers, S.G. and Alzari, P.M. (2004) Structural insights into the catalytic mechanism of Trypanosoma cruzi trans-sialidase. Structure 12, 775-784 CrossRef PubMed
145. Damager, I., Buchini, S., Amaya, M.F., Buschiazzo, A., Alzari, P., Frasch, A.C., Watts, A. and Withers, S.G. (2008) Kinetic and mechanistic analysis of Trypanosoma cruzi trans-sialidase reveals a classical ping-pong mechanism with acid/base catalysis. Biochemistry 47, 3507-3512 CrossRef PubMed
146. Montagna, G., Cremona, M.L., Paris, G., Amaya, M.F., Buschiazzo, A., Alzari, P.M. and Frasch, A.C.C. (2002) The trans-sialidase from the african trypanosome Trypanosoma brucei. Eur. J. Biochem. 269, 2941-2950 CrossRef PubMed
147. Buschiazzo, A., Tavares, G.A., Campetella, O., Spinelli, S., Cremona, M.L., París, G., Amaya, M.F., Frasch, A.C. and Alzari, P.M. (2000) Structural basis of sialyltransferase activity in trypanosomal sialidases. EMBO J. 19, 16-24 CrossRef PubMed
148. Amaya, M.F., Buschiazzo, A., Nguyen, T. and Alzari, P.M. (2003) The high resolution structures of free and inhibitor-bound Trypanosoma rangeli sialidase and its comparison with T. cruzi trans-sialidase. J. Mol. Biol. 325, 773-784 CrossRef PubMed
149. Buschiazzo, A., Amaya, M.F., Cremona, M.L., Frasch, A.C. and Alzari, P.M. (2002) The crystal structure and mode of action of trans-sialidase, a key enzyme in Trypanosoma cruzi pathogenesis. Mol. Cell 10, 757-768 CrossRef PubMed
150. Stierand, K. and Rarey, M. (2011) Consistent two-dimensional visualization of protein-ligand complex series. J. Cheminform. 3, 21CrossRef PubMed
151. Demir, O. and Roitberg, A.E. (2009) Modulation of catalytic function by differential plasticity of the active site: case study of Trypanosoma cruzi trans-sialidase and Trypanosoma rangeli sialidase. Biochemistry 48, 3398-3406 CrossRef PubMed
152. Pierdominici-Sottile, G., Horenstein, N.A. and Roitberg, A.E. (2011) A free energy study of the catalytic mechanism of Trypanosoma cruzi trans-sialidase. From the Michaelis complex to the covalent intermediate. Biochemistry 50, 10150-10158 CrossRef PubMed
153. Pierdominici-Sottile, G., Palma, J. and Roitberg, A.E. (2013) Free energy computations identify the mutations required to confer trans-sialidase activity into Trypanosoma rangeli sialidase. Proteins 82, 424-435 CrossRef PubMed
154. Jers, C., Michalak, M., Larsen, D.M., Kepp, K.P., Li, H., Guo, Y., Kirpekar, F., Meyer, A.S. and Mikkelsen, J.D. (2014) Rational design of a new Trypanosoma rangeli trans-sialidase for efficient sialylation of glycans. PLoS ONE 9, e83902 CrossRef PubMed
155. Feng, H.-Y., Drone, J., Hoffmann, L., Tran, V., Tellier, C., Rabiller, C. and Dion, M. (2005) Converting a β-glycosidase into a β-transglycosidase by directed evolution. J. Biol. Chem. 280, 37088-37097 CrossRef PubMed
156. Teze, D., Hendrickx, J., Czjzek, M., Ropartz, D., Sanejouand, Y.-H., Tran, V., Tellier, C. and Dion, M. (2014) Semi-rational approach for converting a GH1 β-glycosidase into a β-transglycosidase. Protein Eng. Des. Sel. 27, 13-19 CrossRef PubMed
157. Teze, D., Daligault, F., Ferrières, V., Sanejouand, Y.-H. and Tellier, C. (2014) Semi-rational approach for converting a GH36 α-glycosidase into an α-transglycosidase. Glycobiology, doi:10.1093/glycob/cwu124 PubMed
158. Aronson, N.N., Halloran, B.A., Alexeyev, M.F., Zhou, X.E., Wang, Y., Meehan, E.J. and Chen, L. (2006) Mutation of a conserved tryptophan in the chitin-binding cleft of Serratia marcescens chitinase A enhances transglycosylation. Biosci. Biotechnol. Biochem. 70, 243-251 CrossRef PubMed
159. Madhuprakash, J., Tanneeru, K., Purushotham, P., Guruprasad, L. and Podile, A.R. (2012) Transglycosylation by chitinase D from Serratia proteamaculans improved through altered substrate interactions. J. Biol. Chem. 287, 44619-44627 CrossRef PubMed
160. Lü, Y., Yang, H., Hu, H., Wang, Y., Rao, Z. and Jin, C. (2009) Mutation of Trp137 to glutamate completely removes transglycosyl activity associated with the Aspergillus fumigatus AfChiB1. Glycoconj. J. 26, 525-534 CrossRef PubMed
161. Zakariassen, H., Hansen, M.C., Jøranli, M., Eijsink, V. G. H. and Sørlie, M. (2011) Mutational effects on transglycosylating activity of family 18 chitinases and construction of a hypertransglycosylating mutant. Biochemistry 50, 5693-5703 CrossRef PubMed
162. Merceron, R., Foucault, M., Haser, R., Mattes, R., Watzlawick, H. and Gouet, P. (2012) The molecular mechanism of thermostable α-galactosidases AgaA and AgaB explained by X-ray crystallography and mutational studies. J. Biol. Chem. 287, 39642-39652 CrossRef PubMed
163. Placier, G., Watzlawick, H., Rabiller, C. and Mattes, R. (2009) Evolved β-galactosidases from Geobacillus stearothermophilus with improved transgalactosylation yield for galacto-oligosaccharide production. Appl. Environ. Microbiol. 75, 6312-6321 CrossRef PubMed
164. Saburi, W., Kobayashi, M., Mori, H., Okuyama, M. and Kimura, A. (2013) Replacement of the catalytic nucleophile aspartyl residue of dextran glucosidase by cysteine sulfinate enhances transglycosylation activity. J. Biol. Chem. 288, 31670-31677 CrossRef PubMed
165. Lawson, S.L., Wakarchuk, W.W. and Withers, S.G. (1996) Effects of both shortening and lengthening the active site nucleophile of Bacillus circulans xylanase on catalytic activity. Biochemistry 35, 10110-10108 CrossRef PubMed
166. Andrés, E., Aragunde, H. and Planas, A. (2014) Screening glycosynthase libraries with a fluoride chemosensor assay independently of enzyme specificity: identification of a transitional hydrolase to synthase mutant. Biochem. J. 458, 355-363 CrossRef PubMed
167. Aragunde, H., Castilla, E., Biarnés, X., Faijes, M. and Planas, A. (2014) A transitional hydrolase to glycosynthase mutant by Glu to Asp substitution at the catalytic nucleophile in a retaining glycosidase. Carbohydr. Res. 389, 85-92 CrossRef PubMed
168. Rémond, C., Plantier-Royon, R., Aubry, N., Maes, E., Bliard, C. and O'Donohue, M.J. (2004) Synthesis of pentose-containing disaccharides using a thermostable α-L-arabinofuranosidase. Carbohydr. Res. 339, 2019-2025 CrossRef PubMed
169. Rémond, C., Plantier-Royon, R., Aubry, N. and O'Donohue, M.J. (2005) An original chemoenzymatic route for the synthesis of β-D-galactofuranosides using an α-L-arabinofuranosidase. Carbohydr. Res. 340, 637-644 CrossRef PubMed
170. Chlubnova, I., Filipp, D., Spiwok, V., Dvorakova, H., Daniellou, R., Nugier-Chauvin, C., Kralova, B. and Ferrières, V. (2010) Enzymatic synthesis of oligo-D-galactofuranosides and L-arabinofuranosides: from molecular dynamics to immunological assays. Org. Biomol. Chem. 8, 2092-2102 CrossRef PubMed
171. Hidaka, M., Fushinobu, S., Honda, Y., Wakagi, T., Shoun, H. and Kitaoka, M. (2010) Structural explanation for the acquisition of glycosynthase activity. J. Biochem. 147, 237-244 CrossRef PubMed
172. Pollock, J.J. and Sharon, N. (1970) Acceptor specificity of the lysozyme-catalyzed transglycosylation reaction. Biochemistry 9, 3913-3925 CrossRef PubMed
173. Toshima, G., Kawamura, S., Araki, T. and Torikata, T. (2003) Histidine-114 at subsites E and F can explain the characteristic enzymatic activity of guinea hen egg-white lysozyme. Biosci. Biotechnol. Biochem. 67, 540-546 CrossRef PubMed
174. Kawamura, S., Eto, M., Imoto, T., Ikemizu, S., Araki, T. and Torikata, T. (2004) Functional and structural effects of mutagenic replacement of Asn37 at subsite F on the lysozyme-catalyzed reaction. Biosci. Biotechnol. Biochem. 68, 593-601 CrossRef PubMed
175. Moreau, A., Shareck, F., Kluepfel, D. and Morosoli, R. (1994) 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. 219, 261-266 CrossRef PubMed
176. Armand, S., Andrews, S.R., Charnock, S.J. and Gilbert, H.J. (2001) Influence of the aglycone region of the substrate binding cleft of Pseudomonas xylanase 10A on catalysis. Biochemistry 40, 7404-7409 CrossRef PubMed
177. Rosengren, A., Hägglund, P., Anderson, L., Pavon-Orozco, P., Peterson-Wulff, R., Nerinckx, W. and Stålbrand, H. (2012) The role of subsite + 2oftheTrichoderma reesei β-mannanase TrMan5A in hydrolysis and transglycosylation. Biocatal. Biotransform. 30, 338-352 CrossRef
178. Dilokpimol, A., Nakai, H., Gotfredsen, C.H., Baumann, M.J., Nakai, N., Abou Hachem, M. and Svensson, B. (2011) Recombinant production and characterisation of two related GH5 endo-β-1,4-mannanases from Aspergillus nidulans FGSC A4 showing distinctly different transglycosylation capacity. Biochim. Biophys. Acta 1814, 1720-1729 CrossRef PubMed
179. Taira, T., Fujiwara, M., Dennhart, N., Hayashi, H., Onaga, S., Ohnuma, T., Letzel, T., Sakuda, S. and Fukamizo, T. (2010) 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 1804, 668-675 CrossRef PubMed
180. Umekawa, M., Huang, W., Li, B., Fujita, K., Ashida, H., Wang, L.-X. and Yamamoto, K. (2008) Mutants of Mucor hiemalis endo-β-N-acetylglucosaminidase show enhanced transglycosylation and glycosynthase-like activities. J. Biol. Chem. 283, 4469-4479 CrossRef PubMed
181. Yin, J., Li, L., Shaw, N., Li, Y., Song, J.K., Zhang, W., Xia, C., Zhang, R., Joachimiak, A., Zhang, H.-C. et al. (2009) Structural basis and catalytic mechanism for the dual functional endo-β-N-acetylglucosaminidase A. PLoS ONE 4, e4658 CrossRef PubMed
182. Bobrov, K.S., Borisova, A.S., Eneyskaya, E.V., Ivanen, D.R., Shabalin, K.A., Kulminskaya, A.A. and Rychkov, G.N. (2013) Improvement of the efficiency of transglycosylation catalyzed by α-galactosidase from Thermotoga maritima by protein engineering. Biochemistry (Mosc.) 78, 1112-1123 CrossRef PubMed
183. Ochs, M., Belloy, N., Dauchez, M., Muzard, M., Plantier-Royon, R. and Rémond, C. (2013) Role of hydrophobic residues in the aglycone binding subsite of a GH39 β-xylosidase in alkyl xylosides synthesis. J. Mol. Catal. B Enzym. 96, 21-26 CrossRef
184. Kuroki, R., Weaver, L.H. and Matthews, B.W. (1999) Structural basis of the conversion of T4 lysozyme into a transglycosidase by reengineering the active site. Proc. Natl. Acad. Sci. U.S.A. 96, 8949-8954 CrossRef PubMed
185. Matsui, I., Yoneda, S., Ishikawa, K., Miyairi, S., Fukui, S., Umeyama, H. and Honda, K. (1994) Roles of the aromatic residues conserved in the active center of Saccharomycopsis α-amylase for transglycosylation and hydrolysis activity. Biochemistry 33, 451-458 CrossRef PubMed
186. Mizuno, M., Tonozuka, T., Uechi, A., Ohtaki, A., Ichikawa, K., Kamitori, S., Nishikawa, A. and Sakano, Y. (2004) The crystal structure of Thermoactinomyces vulgaris R-47 α-amylase II (TVA II) complexed with transglycosylated product. Eur. J. Biochem. 271, 2530-2538 CrossRef PubMed
187. Collins, T., De Vos, D., Hoyoux, A., Savvides, S.N., Gerday, C., Van Beeumen, J. and Feller, G. (2005) Study of the active site residues of a glycoside hydrolase family 8 xylanase. J. Mol. Biol. 354, 425-435 CrossRef PubMed
188. Wakarchuk, W.W., Campbell, R.L., Sung, W.L., Davoodi, J. and Yaguchi, M. (1994) Mutational and crystallographic analyses of the active site residues of the Bacillus circulans xylanase. Protein Sci. 3, 467-475 CrossRef PubMed
189. Honda, Y., Fushinobu, S., Hidaka, M., Wakagi, T., Shoun, H., Taniguchi, H. and Kitaoka, M. (2008) Alternative strategy for converting an inverting glycoside hydrolase into a glycosynthase. Glycobiology 18, 325-330 CrossRef PubMed
190. Purkiss, A., Skoulakis, S. and Goodfellow, J.M. (2001) The protein-solvent interface: a big splash. Phil. Trans. R. Soc. Lond. A 359, 1515-1527 CrossRef
191. Aghajari, N., Roth, M. and Haser, R. (2002) Crystallographic evidence of a transglycosylation reaction: ternary complexes of a psychrophilic α-amylase. Biochemistry 41, 4273-4280 CrossRef PubMed
192. Kuriki, T., Kaneko, H., Yanase, M., Takata, H., Shimada, J., Handa, S., Takada, T., Umeyama, H. and Okada, S. (1996) Controlling substrate preference and transglycosylation activity of neopullulanase by manipulating steric constraint and hydrophobicity in active center. J. Biol. Chem. 271, 17321-17329 CrossRef PubMed
193. Ramasubbu, N., Ragunath, C., Sundar, K., Mishra, P.J. and Kandra, L. (2005) Structure-function relationships in human salivary α-amylase: role of aromatic residues. Biologia 60, 47-56
194. Frutuoso, M.A. and Marana, S.R. (2013) A single amino acid residue determines the ratio of hydrolysis to transglycosylation catalyzed by β-glucosidases. Protein Pept. Lett. 20, 102-106 CrossRef PubMed
195. Teze, D., Hendrickx, J., Dion, M., Tellier, C., Woods, V.L., Tran, V. and Sanejouand, Y.-H. (2013) Conserved water molecules in family 1 glycosidases: a DXMS and molecular dynamics study. Biochemistry 52, 5900-5910 CrossRef PubMed
196. Rebuffet, E., Groisillier, A., Thompson, A., Jeudy, A., Barbeyron, T., Czjzek, M. and Michel, G. (2011) Discovery and structural characterization of a novel glycosidase family of marine origin. Environ. Microbiol. 13, 1253-1270 CrossRef PubMed
197. Jensen, H.H. and Bols, M. (2006) Stereoelectronic substituent effects. Acc. Chem. Res. 39, 259-265 CrossRef PubMed
198. Mydock, L.K. and Demchenko, A.V. (2010) Mechanism of chemical O-glycosylation: from early studies to recent discoveries. Org. Biomol. Chem. 8, 497-510 CrossRef PubMed