Topological and enzymatic analysis of human Alg2 mannosyltransferase reveals its role in lipid-linked oligosaccharide biosynthetic pathway

Abstract

Despite the conservation of N-glycosylation, human and yeast Alg2 structures have diverged with distinct ER-binding topologies. The human enzyme is more stable than the yeast orthologue, and its activity is modulated by the concentration of donor or acceptor substrate.