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 188.8.131.52).
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
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