Transfer of high-mannose-type oligosaccharides to disaccharides by endo-β- N-acetylglucosaminidase from Arthrobacter protophormiae
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...
Saved in:
Published in | Journal of bioscience and bioengineering Vol. 93; no. 6; pp. 614 - 617 |
---|---|
Main Authors | , , , , |
Format | Journal Article |
Language | English |
Published |
Amsterdarm
Elsevier B.V
2002
Elsevier Science |
Subjects | |
Online Access | Get full text |
Cover
Loading…
Summary: | 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-Glc-β-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. |
---|---|
Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 1389-1723 1347-4421 |
DOI: | 10.1016/S1389-1723(02)80247-X |