In recent years, sugars with a unique chemical handle have been used to detect and
elucidate the function of glycoconjugates. Such chemical handles have generally been part …

The enzyme N-acetylglucosaminyltransferase-V (GlcNAcT-V) transfers GlcNAc from UDP-
GlcNAc to the OH-6′ group of oligosaccharides terminating in the sequence β-d-GlcpNAc …

Using a purified protein and bisected acceptor oligosaccharides, we demonstrate that N‐
acetylglucosaminyltransferase (GnT)‐V transfers a N‐acetylglucosamine residue via a β1, 6 …

LEC18 and LEC14 cells are gain-of-function glycosylation mutants isolated from Chinese
hamster ovary cells for resistance to pea lectin. Structural studies have shown that LEC18 …

Abstract UDP-N-acetylglucosamine: o-mannoside ß (1-6) N-acetylglucos-aminyltransferase
V (GlcNAcT-V)(EC 2.4. 1. 155) is a membranebound, Golgi enzyme which transfers GlcNAc …

N-acetylglucosaminyltransferase-V (GnT-V or MGAT5) catalyzes the formation of an N-
glycan β1, 6-GlcNAc branch on selective target proteins in the Golgi apparatus and is …

The mutant β1, 4-galactosyltransferase (β4Gal-T1), β4Gal-T1-Y289L, in contrast to wild-type
β4Gal-T1, can transfer GalNAc from the sugar donor UDP-GalNAc to the acceptor, GlcNAc …

Complex and hybrid N-linked carbohydrates synthesized by mammalian cells may possess
a N-acetylglucosamine residue known as the bisecting GlcNAc. The transfer of this residue …

Abstract N-acetylglucosaminyltransferase (GnT)-IV catalyzes the formation of the GlcNAcβ1-
4 branch on the GlcNAcβ1-2Manα1-3 arm of the core structure of N-glycans. Two human …

N-Acetylglucosaminyltransferase I (GlcNAcT-I, EC 2.4. 1.101) is the enzyme which initiates
the formation of complex N-linked glycans in eukaryotes by transforming GlcNAc to the oligo …