Aldolase-catalyzed synthesis of beta-D-galp-(1-->9)-D-KDN: a novel acceptor for sialyltransferases

Org Lett. 2006 May 25;8(11):2393-6. doi: 10.1021/ol060736m.

Abstract

[reaction: see text] beta-D-Galp-(1-->9)-D-KDN, a disaccharide component of the cell wall of Streptomyces sp. MB-8, was synthesized from beta-D-Galp-(1-->6)-D-Manp and pyruvate using a sialic acid aldolase. The obtained KDN-containing compound was a novel acceptor for bacterial sialyltransferases. Unusual alpha2,3- and alpha2,6-linked sialyltrisaccharides and a tetrasaccharide were synthesized using a one-pot two-enzyme system containing a Neisseria meningitidis CMP-sialic acid synthetase and a Pasteurella multocida sialyltransferase or a Photobacterium damsela alpha2,6-sialyltransferase.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Catalysis
  • Cell Wall / chemistry
  • Disaccharides / chemical synthesis*
  • Escherichia coli / genetics
  • Escherichia coli / metabolism
  • Molecular Structure
  • Neuraminic Acids / chemical synthesis*
  • Oxo-Acid-Lyases / metabolism*
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / metabolism
  • Sialyltransferases / chemistry
  • Sialyltransferases / metabolism*
  • Streptomyces / chemistry

Substances

  • Disaccharides
  • Neuraminic Acids
  • Recombinant Proteins
  • beta-D-galp-(1-9)-D-KDN
  • Sialyltransferases
  • Oxo-Acid-Lyases
  • N-acetylneuraminate lyase