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Transglycosylases are a class of GH enzymes that can catalyze the transformation of one glycoside to another. That is, these enzymes catalyze the intra- or intermolecular substitution of the anomeric position of a glycoside. Mechanistically, transglycosylases utilize the same mechanism as various retaining glycoside hydrolases [1, 2]. Thus, reaction of the nucleophile of a retaining glycoside hydrolase with a substrate gives a glycosyl-enzyme intermediate that can be intercepted either by water to give the hydrolysis product, or by another acceptor (often another carbohydrate alcohol), to give a new glycoside or oligosaccharide [3]. Alternatively, transglycosylation can occur by neighboring group participation, wherein a neighboring 2-acetamido group participates in the reaction to generate an oxazolinium ion intermediate, which again can react with another acceptor other than water. Some transglycosidases possess substantial glycoside hydrolase activity, and some glycoside hydrolases possess transglycosylase activity [4]. Indeed, in many cases it is unclear what the major role of an enzyme that possesses both activities may be. Transglycosylases are classified as glycoside hydrolases into various GH families on the basis of sequence similarity.

Figure. Generalized mechanism of a transglycosylase. Enzymatic cleavage of a substrate through a classical Koshland retaining mechanism results in formation of a glycosyl enzyme intermediate. This can partition to react with either water to cause hydrolysis (glycoside hydrolase activity) or to an alternative acceptor, often a sugar, to cause transglycosylation (transglycosylase activity).


GH families with notable transglycosylase activity include:

  • GH2, for example LacZ β-galactosidase converts lactose to allolactose [5].
  • GH13, for example cyclodextran glucanotransferases that convert linear amylose to cyclodextrins [6]; glycogen debranching enzyme, which transfers three glucose residues from the four-residue glycogen branch to a nearby branch [7]; and trehalose synthase, which catalyzes the interconversion of maltose and trehalose [8].
  • GH16, for example xyloglucan endotransglycosylases, which cuts and rejoins xyloglucan chains in the plant cell wall [9].
  • GH31, for example α-transglucosidases, which catalyze the transfer of individual glucosyl residues between α-(1→4)-glucans [10].
  • GH70, for example glucansucrases, which catalyse the synthesis of high molecular weight glucans, from sucrose [11].
  • GH77, for examples amylomaltase, which catalyzes the synthesis of maltodextrins from maltose [12].
  • GH23, GH102, GH103, and GH104 lytic transglycosylases, which convert peptidoglycan to 1,6-anhydrosugars [13].


  1. Sinnott, M.L. (1990) Catalytic mechanisms of enzymic glycosyl transfer. Chem. Rev. 90, 1171-1202. DOI: 10.1021/cr00105a006
  2. Bissaro B, Monsan P, Fauré R, and O'Donohue MJ. (2015) Glycosynthesis in a waterworld: new insight into the molecular basis of transglycosylation in retaining glycoside hydrolases. Biochem J. 467, 17-35. DOI:10.1042/BJ20141412 | PubMed ID:25793417 | HubMed [Bissaro2015]
  3. Crout DH and Vic G. (1998) Glycosidases and glycosyl transferases in glycoside and oligosaccharide synthesis. Curr Opin Chem Biol. 2, 98-111. DOI:10.1016/s1367-5931(98)80041-0 | PubMed ID:9667913 | HubMed [Crout1998]
  4. Vocadlo, D. J. and Withers, S. G. (2008) Glycosidase-Catalysed Oligosaccharide Synthesis, Chapter 29 in Carbohydrates in Chemistry and Biology, Ernst, B., Hart, G. W. and Sinaý, P., eds., Wiley-VCH Verlag GmbH, Weinheim, Germany. DOI:10.1002/9783527618255.ch29
  5. Juers DH, Matthews BW, and Huber RE. (2012) LacZ β-galactosidase: structure and function of an enzyme of historical and molecular biological importance. Protein Sci. 21, 1792-807. DOI:10.1002/pro.2165 | PubMed ID:23011886 | HubMed [Juers2012]
  6. Uitdehaag JC, Mosi R, Kalk KH, van der Veen BA, Dijkhuizen L, Withers SG, and Dijkstra BW. (1999) X-ray structures along the reaction pathway of cyclodextrin glycosyltransferase elucidate catalysis in the alpha-amylase family. Nat Struct Biol. 6, 432-6. DOI:10.1038/8235 | PubMed ID:10331869 | HubMed [Uitdehaag1999]
  7. Braun C, Lindhorst T, Madsen NB, and Withers SG. (1996) Identification of Asp 549 as the catalytic nucleophile of glycogen-debranching enzyme via trapping of the glycosyl-enzyme intermediate. Biochemistry. 35, 5458-63. DOI:10.1021/bi9526488 | PubMed ID:8611536 | HubMed [Braun1996]
  8. Zhang R, Pan YT, He S, Lam M, Brayer GD, Elbein AD, and Withers SG. (2011) Mechanistic analysis of trehalose synthase from Mycobacterium smegmatis. J Biol Chem. 286, 35601-35609. DOI:10.1074/jbc.M111.280362 | PubMed ID:21840994 | HubMed [Zhang2011]
  9. Eklöf JM and Brumer H. (2010) The XTH gene family: an update on enzyme structure, function, and phylogeny in xyloglucan remodeling. Plant Physiol. 153, 456-66. DOI:10.1104/pp.110.156844 | PubMed ID:20421457 | HubMed [Eklof2010]
  10. Larsbrink J, Izumi A, Hemsworth GR, Davies GJ, and Brumer H. (2012) Structural enzymology of Cellvibrio japonicus Agd31B protein reveals α-transglucosylase activity in glycoside hydrolase family 31. J Biol Chem. 287, 43288-99. DOI:10.1074/jbc.M112.416511 | PubMed ID:23132856 | HubMed [Larsbrink2012]
  11. van Hijum SA, Kralj S, Ozimek LK, Dijkhuizen L, and van Geel-Schutten IG. (2006) Structure-function relationships of glucansucrase and fructansucrase enzymes from lactic acid bacteria. Microbiol Mol Biol Rev. 70, 157-76. DOI:10.1128/MMBR.70.1.157-176.2006 | PubMed ID:16524921 | HubMed [Hijum2006]
  12. van der Maarel MJ and Leemhuis H. (2013) Starch modification with microbial alpha-glucanotransferase enzymes. Carbohydr Polym. 93, 116-21. DOI:10.1016/j.carbpol.2012.01.065 | PubMed ID:23465909 | HubMed [Maarel2013]
  13. Scheurwater E, Reid CW, and Clarke AJ. (2008) Lytic transglycosylases: bacterial space-making autolysins. Int J Biochem Cell Biol. 40, 586-91. DOI:10.1016/j.biocel.2007.03.018 | PubMed ID:17468031 | HubMed [Schuerwater2008]
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