A bacterial chitinase acts as catalyst for synthesis of the N-linked oligosaccharide core trisaccharide by employing a sugar oxazoline substrate

Atsushi Kobayashi, Hideyuki Kuwata, Michinari Kohri, Ryuko Izumi, Takeshi Watanabe, Shin Ichiro Shoda

Research output: Contribution to journalArticle

6 Citations (Scopus)

Abstract

A chitinolytic enzyme, chitinase A1 from Bacillus circulans WL-12, was found to catalyze a glycosyl-transferring reaction to form the N-linked oligosaccharide core structure, Man(β1-4)-GlcNAc(β1-4)-GlcNAc, by employing Man(β1-4)-GlcNAc-oxazoline as glycosyl donor. When the reaction was carried out in the presence of 20 v/v% acetone, the trisaccharide was obtained in 32% yield. It has been shown for the first time that a chitinase behaves like an endo-β-N-acetylglucosaminidase in spite of low structural similarity between them.

Original languageEnglish
Pages (from-to)533-541
Number of pages9
JournalJournal of Carbohydrate Chemistry
Volume25
Issue number7
DOIs
Publication statusPublished - 2006 Sep 1

Keywords

  • Endo-β-N-acetylglucosaminidase
  • Family 18 chitinase
  • N-linked oligosaccharide
  • Sugar oxazoline
  • Transition state analog

ASJC Scopus subject areas

  • Biochemistry
  • Organic Chemistry

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