PMID: 7696852Oct 1, 1994

Identification, characterization, and developmental expression of a novel alpha 2-->8-KDN-transferase which terminates elongation of alpha 2-->8-linked oligo-polysialic acid chain synthesis in trout egg polysialoglycoproteins

Glycoconjugate Journal
T AngataY Inoue


A novel glycosyltransferase which catalyses transfer of deaminated neuraminic acid, KDN (2-keto-3-deoxy-D-glycero-D-galacto-nononic acid) from CMP-KDN to the non-reducing termini of oligo-polysialyl chains of polysialoglycoprotein (PSGP), was discovered in the ovary of rainbow trout (Oncorhynchus mykiss). The KDN-transferase activity was optimal at neutral pH, and stimulated 2 to 2.5-fold by 2-5 mM Mg2+ or Mn2+. Expression of KDN-transferase was developmentally regulated in parallel with expression of the alpha 2-->8-polysialyltransferase, which catalyses synthesis of the oligo-polysialyl chains in PSGP. Incorporation of the KDN residues into the oligo-polysialyl chains prevented their further elongation, resulting in 'capping' of the oligo-polysialyl chains. This is the first example of a glycosyltransferase that catalyses termination of alpha 2-->8-polysialylation in glycoproteins.


Feb 1, 1992·Glycobiology·F A Troy
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Apr 25, 2012·Applied Microbiology and Biotechnology·Yanhong Li, Xi Chen
Apr 17, 2007·Biochemical and Biophysical Research Communications·Shinji GoK Kitajima
Sep 2, 2019·Carbohydrate Polymers·Xiaoxiao GuoRobert A Falconer

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Polysialic acid
Carbohydrate Sequence
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