N-glycosylation is a widely occurring post-translational modification in which an
oligosaccharide is linked to the amide nitrogen of an Asn side chain in the sequence Asn-XThr/Ser
(where X≠Pro). This modification has been shown to play a role in protein folding,
trafficking, stability, and function. Here we use molecular dynamics simulations of
glycosylated and unglycosylated structures to address the role of N-glycosylation in the
regulation of enzymatic function in human γ-Glutamyltranspeptidase 1 (hGGT1; EC 18.104.22.168).
hGGT1 is a conserved enzyme known to play a role in maintaining cysteine levels in the
body and in regulating intra-cellular redox status. The crystal structure of hGGT1 indicates
that it is post-translationally modified by N-glycosylation at seven sites, and glycosylation at
N95 has been shown to be the most critical to the ability of the enzyme to undergo activation
The file is restricted for YU community access only.