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
N1 - Copyright:
Copyright 2008 Elsevier B.V., All rights reserved.
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
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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 -