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Combination of Glycosyltransferases and a Glycosynthase in Sequential and One‐Pot Reactions for the Synthesis of Type 1 and Type 2 N ‐Acetyllactosamine Oligomers
Author(s) -
Henze Manja,
Schmidtke Simon,
Hoffmann Natalie,
Steffens Hanna,
Pietruszka Jörg,
Elling Lothar
Publication year - 2015
Publication title -
chemcatchem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.497
H-Index - 106
eISSN - 1867-3899
pISSN - 1867-3880
DOI - 10.1002/cctc.201500645
Subject(s) - glycosyltransferase , bacillus circulans , chemistry , glycan , stereochemistry , type (biology) , galactose , biochemistry , enzyme , biology , glycoprotein , ecology
The disaccharide units of N ‐acetyllactosamine (LacNAc) types 1 and 2 and poly‐LacNAc are involved in many biological recognition events. We report the modular design of type 1 (3Galβ1‐3GlcNAcβ1‐; Gal= d ‐galactose, GlcNAc= N ‐acetyl d ‐glucosamine) and type 2 (3Galβ1‐4GlcNAcβ1‐) LacNAc oligomers by combination of two recombinant glycosyltransferases, β1,3‐ N ‐acetylglucosaminyltransferase from Helicobacter pylori and human β1,4‐galactosyltransferase‐1, with galactosynthase His 6 BgaC/Glu233Gly from Bacillus circulans . Combination of His 6 BgaC/Glu233Gly and β1,3‐ N ‐acetylglucosaminyltransferase in sequential or one‐pot mode results in LacNAc type 1 oligomers with up to four LacNAc units. Moreover, sequential use of all three enzymes gives access to a variety of neo‐LacNAc oligomers. We present oligomers composed of alternating type 1 and 2 units and type 1‐terminated LacNAc type 2 oligomers. These glycan structures are valuable compounds for testing carbohydrate–protein interactions.