Glycoconjugate Journal

, Volume 13, Issue 6, pp 927–931

A1H NMR investigation of the hydrolysis of a synthetic substrate by KDN-sialidase fromCrassostrea virginica

  • Jennifer C. Wilson
  • David C. M. Kong
  • Yu-Teh Li
  • Mark Von Itzstein
Short Communication

DOI: 10.1007/BF01053187

Cite this article as:
Wilson, J.C., Kong, D.C.M., Li, YT. et al. Glycoconjugate J (1996) 13: 927. doi:10.1007/BF01053187

Abstract

The mechanism of hydrolysis of 4-methylumbelliferyl 3-deoxy-d-glycero-α-d-galacto-2-nonulopyranosidonic acid (KDNα2MeUmb,4) by KDN-sialidase isolated from the hepatopancreas of the oysterCrassostrea virginica has been monitored by1H NMR spectroscopy. The results of these experiments reveal that KDN-sialidase catalyses the hydrolysis of the synthetic substrate KDNα2MeUmb, with initial release of α-d-KDN. This is consistent with an overall mechanism for the hydrolysis which proceeds with retention of anomeric configuration. These results agree with earlier NMR studies of otherN-acetylneuraminic acid-recognising sialidases from both viral and bacterial sources.

Keywords

KDN-sialidaseNMR spectroscopysialidasesKDN

Copyright information

© Chapman & Hall 1996

Authors and Affiliations

  • Jennifer C. Wilson
    • 1
  • David C. M. Kong
    • 1
  • Yu-Teh Li
    • 2
  • Mark Von Itzstein
    • 1
  1. 1.Department of Medicinal Chemistry, Victorian College of PharmacyMonash UniversityParkvilleAustralia
  2. 2.Department of BiochemistryTulane University School of MedicineNew OrleansUSA