TY - JOUR
T1 - Transfer of high-mannose-type oligosaccharides to disaccharides by Endo-β-N-acetylglucosaminidase from Arthrobacter protophormiae
AU - Fujita, Kiyotaka
AU - Miyamura, Tsuyoshi
AU - Sano, Mutsumi
AU - Kato, Ikunoshin
AU - Takegawa, Kaoru
N1 - Funding Information:
We would like to thank Drs. Hideharu Ishida, Makoto Kiso (Gifu University), Akihiro Kondo (Takara Shuzo), Masahiko Endo (Hirosaki University), and Yuan C. Lee (Johns Hopkins University) for many helpful discussions during the course of this work. This work was supported in part by grants from the Ministry of Education, Culture, Sports, Science and Technology of Japan (to K. T.).
PY - 2002
Y1 - 2002
N2 - Endo-β-N-acetylglucosaminidase from Arthrobacter protophormiae (Endo-A) has transglycosylation activity, and high-mannose-type oligosaccharides are transferred to suitable glycosides as acceptor substrates. The acceptor specificity of Endo-A-catalyzed transglycosylation toward various disaccharides was investigated. To identify an effective acceptor for the transglycosylation by Endo-A, the reaction was carried out using various disaccharides. Endo-A transferred high-mannose-type oligosaccharides more efficiently to β-linked disaccharides (cellobiose, gentiobiose, sophorose, and laminaribiose) than to α-linked disaccharides (isomaltose, maltose, nigerose, kojibiose, and trehalose) as acceptor substrates. The transglycosylation products, (Man)6GlcNAc-Glcβ-Glc, were more rapidly hydrolyzed than (Man)6GlcNAc-Glc-α-Glc. These results indicate that Endo-A recognizes the anomeric configuration of the acceptor substrates, and β-linked glycosides are suitable for the synthesis of transglycosylation products.
AB - Endo-β-N-acetylglucosaminidase from Arthrobacter protophormiae (Endo-A) has transglycosylation activity, and high-mannose-type oligosaccharides are transferred to suitable glycosides as acceptor substrates. The acceptor specificity of Endo-A-catalyzed transglycosylation toward various disaccharides was investigated. To identify an effective acceptor for the transglycosylation by Endo-A, the reaction was carried out using various disaccharides. Endo-A transferred high-mannose-type oligosaccharides more efficiently to β-linked disaccharides (cellobiose, gentiobiose, sophorose, and laminaribiose) than to α-linked disaccharides (isomaltose, maltose, nigerose, kojibiose, and trehalose) as acceptor substrates. The transglycosylation products, (Man)6GlcNAc-Glcβ-Glc, were more rapidly hydrolyzed than (Man)6GlcNAc-Glc-α-Glc. These results indicate that Endo-A recognizes the anomeric configuration of the acceptor substrates, and β-linked glycosides are suitable for the synthesis of transglycosylation products.
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U2 - 10.1016/S1389-1723(02)80247-X
DO - 10.1016/S1389-1723(02)80247-X
M3 - Article
C2 - 16233259
AN - SCOPUS:0036302055
SN - 1389-1723
VL - 93
SP - 614
EP - 617
JO - Journal of Bioscience and Bioengineering
JF - Journal of Bioscience and Bioengineering
IS - 6
ER -