Substrate specificity of FUT8 and chemoenzymatic synthesis of core-fucosylated asymmetric N-glycans

Angie D Calderon; Yunpeng Liu; Xu Li; Xuan Wang; Xi Chen; Lei Li; Peng G Wang

doi:10.1039/c6ob00586a

Substrate specificity of FUT8 and chemoenzymatic synthesis of core-fucosylated asymmetric N-glycans

Org Biomol Chem. 2016 Apr 26;14(17):4027-31. doi: 10.1039/c6ob00586a.

Authors

Angie D Calderon¹, Yunpeng Liu², Xu Li¹, Xuan Wang¹, Xi Chen³, Lei Li¹, Peng G Wang¹

Affiliations

¹ Department of Chemistry and Center for Diagnostics & Therapeutics, Georgia State University, Atlanta, GA 30303, USA. lli22@gsu.edu pwang11@gsu.edu.
² Department of Chemistry and Center for Diagnostics & Therapeutics, Georgia State University, Atlanta, GA 30303, USA. lli22@gsu.edu pwang11@gsu.edu and Chemily LLC, Atlanta, GA 30303, USA.
³ Department of Chemistry, University of California, One Shields Avenue, Davis, CA 95616, USA.

Abstract

Substrate specificity studies of human FUT8 using 77 structurally-defined N-glycans as acceptors showed a strict requirement towards the α1,3-mannose branch, but a great promiscuity towards the α1,6-mannose branch. Accordingly, a chemoenzymatic strategy was developed for the efficient synthesis of core-fucosylated asymmetric N-glycans.

MeSH terms

Biocatalysis
Fucose / chemistry*
Fucose / metabolism
Fucosyltransferases / chemistry*
Fucosyltransferases / metabolism
Humans
Polysaccharides / biosynthesis*
Polysaccharides / chemistry
Substrate Specificity

Substances

Polysaccharides
Fucose
Fucosyltransferases
Glycoprotein 6-alpha-L-fucosyltransferase

Abstract

MeSH terms

Substances

Grants and funding