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Structures and mechanisms of glycosyltransferases
Abstract
Glycosyltransferases (GTs) catalyze the transfer of a sugar moiety from an activated donor sugar onto saccharide and nonsaccharide acceptors. A sequence-based classification spreads GTs in many families thus reflecting the variety of molecules that can be used as acceptors. In contrast, this enzyme family is characterized by a more conserved three-dimensional architecture. Until recently, only two different folds (GT-A and GT-B) have been identified for solved crystal structures. The recent report of a structure for a bacterial sialyltransferase allows the definition of a new fold family. Progress in the elucidation of the structures and mechanisms of GTs are discussed in this review. To accommodate the growing number of crystal structures, we created the 3D-Glycosyltransferase database to gather structural information concerning this class of enzymes.
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NAD-binding domains of dehydrogenases
Lesk, A. M. (1995) · Current Opinion in Structural Biology · doi:10.1016/0959-440x(95)80010-7 · Cited by 239
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Advances in the Biology and Chemistry of Sialic Acids
Chen, X., & Varki, A. (2010) · ACS Chemical Biology · doi:10.1021/cb900266r · Cited by 543
Castelle, C. J., Wrighton, K. C., Thomas, B. C., Hug, L. A., Brown, C. T., Wilkins, M. J., Frischkorn, K. R., Tringe, S. G., Singh, A., Markillie, L. M., et al. (2015) · Current Biology · doi:10.1016/j.cub.2015.01.014 · Cited by 536
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Iyanagi, T. (2007) · International Review of Cytology · doi:10.1016/s0074-7696(06)60002-8 · Cited by 290
Enzymes in the Synthesis of Glycoconjugates
Schmaltz, R. M., Hanson, S. R., & Wong, C.-H. (2011) · Chemical Reviews · doi:10.1021/cr200113w · Cited by 283
Metadata
- Authors
- Breton, C., Šnajdrová, L., Jeanneau, C., Koča, J., & Imberty, A.
- Venue
- Glycobiology
- Publisher
- Oxford University Press (OUP)
- Published
- 2005-07-21
- Volume
- 16
- Issue
- 2
- Pages
- 29R-37R
- ISSN
- 0959-6658 (ISSN-L)
- 1460-2423
- OpenAlex
- W2018454041
- Cited by
- 711
- References
- 3
- FWCI
- 10.37
- Type
- journal article
- Language
- en
- Open access
- closed
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