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

Abstract

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.

References

Feb 1, 1992·Glycobiology·F A Troy
Aug 1, 1982·Journal of Virology·B KwiatkowskiS Stirm

Citations

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

Related Concepts

Polysialic acid
KDN-transferase
Metazoa
Carbohydrate Sequence
Ovum
Sialic Acids
Polysialoglycoproteins
Ectosialyltransferase
Substrate Specificity
Cabeza Acerada

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