A chemoenzymatic route to synthesize unnatural sugar nucleotides using a novel N-acetylglucosamine-1-phosphate pyrophosphorylase from Camphylobacter jejuni NCTC 11168

Bioorg Med Chem Lett. 2013 Aug 1;23(15):4303-7. doi: 10.1016/j.bmcl.2013.06.003. Epub 2013 Jun 11.

Abstract

A novel N-acetylglucosamine-1-phosphate pyrophosphorylase was identified from Campylobacter jejuni NCTC 11168. An unprecedented degree of substrate promiscuity has been revealed by systematic studies on its substrate specificities towards sugar-1-P and NTP. The yields of the synthetic reaction of seven kinds of sugar nucleotides catalyzed by the enzyme were up to 60%. In addition, the yields of the other nine were around 20%. With this enzyme, three novel sugar nucleotide analogs were synthesized on a preparative scale and well characterized.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetylglucosamine / analogs & derivatives
  • Acetylglucosamine / chemistry
  • Campylobacter jejuni / enzymology*
  • Carbohydrates / chemistry*
  • Nucleotides / chemical synthesis
  • Nucleotides / chemistry*
  • Nucleotides / metabolism
  • Nucleotidyltransferases / chemistry
  • Nucleotidyltransferases / metabolism*
  • Structure-Activity Relationship
  • Substrate Specificity

Substances

  • Carbohydrates
  • Nucleotides
  • N-acetylglucosamine-1-phosphate
  • Nucleotidyltransferases
  • Acetylglucosamine