Induction of KDNase Sm, a deaminoneuraminic acid (KDN) residue-specific sialidase from Sphingobacterium multivorum, using synthetic KDN-glycosides

Biochem Biophys Res Commun. 1998 Jul 30;248(3):505-10. doi: 10.1006/bbrc.1998.9002.


Various aryl and alkyl alpha-glycosides of KDN were synthesized and tested as substrates for their susceptibility to a deaminoneuraminic acid (KDN)-specific sialidase from Sphingobacterium multivorum, designated KDNase Sm. The synthetic KDN-glycosides were all hydrolyzed by the action of KDNase Sm. A hydroxyl group at C-5 position of KDN was required for the recognition by the enzyme, and was shown not to be replaced by an amino- or an acylamino group for the enzymatic recognition. These synthetic KDN-glycosides were also examined for their inducing activity of KDNase in S. multivorum and were shown to induce the KDNase activity effectively when the bacterium was cultured minimum salt medium containing both 0.1% glucose and 0.1% various KDN-glycosides. No KDNase activity was induced by the KDN-glycosides without 0.1% glucose. This is the first case of using synthetic KDN-glycosides as inducers of KDNase Sm.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Carbohydrate Conformation
  • Enzyme Induction
  • Glycoside Hydrolases / biosynthesis*
  • Glycoside Hydrolases / metabolism
  • Glycosides / chemical synthesis
  • Glycosides / chemistry
  • Glycosides / metabolism
  • Gram-Negative Bacteria / enzymology*
  • Models, Molecular
  • Substrate Specificity
  • Sugar Acids


  • Glycosides
  • Sugar Acids
  • 3-deoxyglycero-galacto-nonulosonic acid
  • Glycoside Hydrolases
  • deaminoneuraminate hydrolase