Contributed equally to this work.
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Communication
Enzyme-Catalyzed Synthesis of a Hybrid N-Linked Oligosaccharide using N-Acetylglucosaminyltransferase I
Article first published online: 9 JUL 2008
DOI: 10.1002/adsc.200800265
Copyright © 2008 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Additional Information
How to Cite
Chen, R., Pawlicki, Mark A., Hamilton, Brian S. and Tolbert, Thomas J. (2008), Enzyme-Catalyzed Synthesis of a Hybrid N-Linked Oligosaccharide using N-Acetylglucosaminyltransferase I. Adv. Synth. Catal., 350: 1689–1695. doi: 10.1002/adsc.200800265
Publication History
- Issue published online: 31 JUL 2008
- Article first published online: 9 JUL 2008
- Manuscript Revised: 16 JUN 2008
- Manuscript Received: 2 MAY 2008
Keywords:
- enzyme catalysis;
- enzymes;
- glycosylation;
- oligosaccharides
Abstract
The soluble catalytic domain of human N-acetylglucosaminyltransferase I was purified from Escherichia coli and utilized in the enzyme-catalyzed conversion of high mannose N-linked oligosaccharide 1 into the rare hybrid oligosaccharide 2. Analysis of the reaction showed that the conversion of high mannose 1 into hybrid oligosaccharide 2 proceeded to 100% completion as assessed by MALDI-TOF-MS. Purification of the large polar oligosaccharide by gel filtration and silica gel chromatography afforded a 42% isolated yield of oligosaccharide 2. This enzyme-catalyzed reaction can be utilized to produce rare hybrid oligosaccharides for biochemical and structural studies.