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ST3 Beta-Galactoside Alpha-2,3-Sialyltransferase 2 (ST3GAL2)

  • Shuichi Tsuji
  • Shou Takashima
Reference work entry

Abstract

ST3Gal-II is a β-galactoside α2,3-sialyltransferase, which transfers sialic acid from CMP-sialic acid (CMP-Sia) to the terminal Gal residues found in glycoconjugates through an α2,3-linkage. Six different cDNAs encoding ST3Gal enzyme have been identified in various higher vertebrates, which correspond to six ST3Gal gene subfamilies (Harduin-Lepers et al. 2005; Takashima 2008; Hashimoto et al. 2009). From amino acid sequence similarities, substrate specificities, and gene structures, these members can be classified into two subfamilies. One subfamily consists of two members, ST3Gal-I (E.C.2.4.99.4) and ST3Gal-II (E.C.2.4.99.4). The recombinant enzymes in this subfamily use exclusively the type III oligosaccharide structure Galβl-3GalNAc-R as an acceptor substrate. The other subfamily consists of ST3Gal-III, ST3Gal-IV, ST3Gal-V, and ST3Gal-VI. The members use the oligosaccharide isomers Galβ1-3/4Glc(NAc)-R as acceptor substrates.

Keywords

Sialic Acid Acceptor Substrate Renal Cell Carcinoma Cell Line ACHN Cell Renal Cell Carcinoma Tissue 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer Japan 2014

Authors and Affiliations

  1. 1.Institute of GlycoscienceTokai UniversityHiratsukaJapan
  2. 2.Laboratory of GlycobiologyThe Noguchi InstituteItabashiJapan

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