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 › peer-review

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

Access to Document

10.1080/07328300600966448

Cite this

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 › peer-review

@article{d26a041bb9b64a34985343ff27619b0f,

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

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.",

keywords = "Endo-β-N-acetylglucosaminidase, Family 18 chitinase, N-linked oligosaccharide, Sugar oxazoline, Transition state analog",

author = "Atsushi Kobayashi and Hideyuki Kuwata and Michinari Kohri and Ryuko Izumi and Takeshi Watanabe and Shoda, {Shin Ichiro}",

year = "2006",

month = sep,

day = "1",

doi = "10.1080/07328300600966448",

language = "English",

volume = "25",

pages = "533--541",

journal = "Journal of Carbohydrate Chemistry",

issn = "0732-8303",

publisher = "Taylor and Francis Ltd.",

number = "7",

}

TY - JOUR

T1 - A bacterial chitinase acts as catalyst for synthesis of the N-linked oligosaccharide core trisaccharide by employing a sugar oxazoline substrate

AU - Kobayashi, Atsushi

AU - Kuwata, Hideyuki

AU - Kohri, Michinari

AU - Izumi, Ryuko

AU - Watanabe, Takeshi

AU - Shoda, Shin Ichiro

PY - 2006/9/1

Y1 - 2006/9/1

N2 - 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.

AB - 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.

KW - Endo-β-N-acetylglucosaminidase

KW - Family 18 chitinase

KW - N-linked oligosaccharide

KW - Sugar oxazoline

KW - Transition state analog

UR - http://www.scopus.com/inward/record.url?scp=33750437404&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=33750437404&partnerID=8YFLogxK

U2 - 10.1080/07328300600966448

DO - 10.1080/07328300600966448

M3 - Article

AN - SCOPUS:33750437404

VL - 25

SP - 533

EP - 541

JO - Journal of Carbohydrate Chemistry

JF - Journal of Carbohydrate Chemistry

SN - 0732-8303

IS - 7

ER -

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

Abstract

Keywords

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this