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

doi:10.1080/07328300600966448

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

ENG - Biomolecular Engineering

Research output: Contribution to journal › Article

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 language	English
Pages (from-to)	533-541
Number of pages	9
Journal	Journal of Carbohydrate Chemistry
Volume	25
Issue number	7
DOIs	https://doi.org/10.1080/07328300600966448
Publication status	Published - 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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10.1080/07328300600966448

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Kobayashi, A., Kuwata, H., Kohri, M., Izumi, R., Watanabe, T., & Shoda, S. I. (2006). A bacterial chitinase acts as catalyst for synthesis of the N-linked oligosaccharide core trisaccharide by employing a sugar oxazoline substrate. Journal of Carbohydrate Chemistry, 25(7), 533-541. https://doi.org/10.1080/07328300600966448

A bacterial chitinase acts as catalyst for synthesis of the N-linked oligosaccharide core trisaccharide by employing a sugar oxazoline substrate. / Kobayashi, Atsushi; Kuwata, Hideyuki; Kohri, Michinari; Izumi, Ryuko; Watanabe, Takeshi; Shoda, Shin Ichiro.

In: Journal of Carbohydrate Chemistry, Vol. 25, No. 7, 01.09.2006, p. 533-541.

Research output: Contribution to journal › Article

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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.",

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AU - Watanabe, Takeshi

AU - Shoda, Shin Ichiro

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