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  • Glycosyltransferases catalyze the transfer of a sugar moiety from an activated donor sugar onto saccharide and non-saccharide acceptors. A sequence-based classification spreads glycosyltransferases in a large number of families thus reflecting the variety of molecules that can be used as acceptors. In contrast, this enzyme family is characterized by a more conserved 3D 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 defination of a new fold family. Progress in the elucidation of the structures and mechanisms of glycosyltransferases are discussed in this review. To accomodate the growing number of crystal structures, the 3D-glycosyltransferase database has been created to gather structural information concerning this class of enzymes.
  • Glycosyltransferases catalyze the transfer of a sugar moiety from an activated donor sugar onto saccharide and non-saccharide acceptors. A sequence-based classification spreads glycosyltransferases in a large number of families thus reflecting the variety of molecules that can be used as acceptors. In contrast, this enzyme family is characterized by a more conserved 3D 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 defination of a new fold family. Progress in the elucidation of the structures and mechanisms of glycosyltransferases are discussed in this review. To accomodate the growing number of crystal structures, the 3D-glycosyltransferase database has been created to gather structural information concerning this class of enzymes. (en)
Title
  • Structures and mechanisms of glycosyltransferases
  • Structures and mechanisms of glycosyltransferases (en)
skos:prefLabel
  • Structures and mechanisms of glycosyltransferases
  • Structures and mechanisms of glycosyltransferases (en)
skos:notation
  • RIV/00216224:14310/06:00015567!RIV10-MSM-14310___
http://linked.open...avai/riv/aktivita
http://linked.open...avai/riv/aktivity
  • P(GD204/03/H016), Z(MSM0021622413)
http://linked.open...iv/cisloPeriodika
  • 2
http://linked.open...vai/riv/dodaniDat
http://linked.open...aciTvurceVysledku
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http://linked.open...iv/duvernostUdaju
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http://linked.open...dnocenehoVysledku
  • 502018
http://linked.open...ai/riv/idVysledku
  • RIV/00216224:14310/06:00015567
http://linked.open...riv/jazykVysledku
http://linked.open.../riv/klicovaSlova
  • glycosyltransferases; mechanism of reaction; structural characteristics; on-line database (en)
http://linked.open.../riv/klicoveSlovo
http://linked.open...odStatuVydavatele
  • GB - Spojené království Velké Británie a Severního Irska
http://linked.open...ontrolniKodProRIV
  • [2ACFE4842EDA]
http://linked.open...i/riv/nazevZdroje
  • Glycobiology
http://linked.open...in/vavai/riv/obor
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http://linked.open...vavai/riv/projekt
http://linked.open...UplatneniVysledku
http://linked.open...v/svazekPeriodika
  • 16
http://linked.open...iv/tvurceVysledku
  • Imberty, Anne
  • Koča, Jaroslav
  • Šnajdrová, Lenka
  • Breton, Christelle
  • Jeanneau, Charlotte
http://linked.open...n/vavai/riv/zamer
issn
  • 0959-6658
number of pages
http://localhost/t...ganizacniJednotka
  • 14310
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