Strict Order of (Fuc to Asn-linked GlcNAc) Fucosyltransferases Forming Core-difucosylated Structures

Overview

Journal Glycoconj J

Publisher Springer

Specialties Biochemistry
Endocrinology

Date 1998 Jun 5

PMID 9613822

Citations 7

Authors

E Staudacher

L Marz

Affiliations

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Abstract

In insect cells fucose can be either alpha1,6- or alpha1,3-linked to the asparagine-bound GlcNAc residue of N-glycans. Difucosylated glycans have also been found. Kinetic studies and acceptor competition experiments demonstrate that two different enzymes are responsible for this alpha1,6- and alpha1,3-linkage of fucose. Using dansylated acceptor substrates a strict order of these enzymes can be established for the formation of difucosylated structures. First, the alpha1,6-fucosyltransferase catalyses the transfer of fucose into alpha1,6-linkage to the non-fucosylated acceptor and then the alpha1,3-fucosyltransferase completes the difucosylation.

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