AI Article Synopsis
- The study explored how oligosaccharide modification impacts the function of human acid beta-glucosidase, an important lysosomal enzyme with five potential glycosylation sites.
- The research found that while the unglycosylated form of the enzyme was stable in certain environments, it did not exhibit any catalytic activity.
- It concluded that at least one occupied glycosylation site is necessary for the enzyme to maintain its active form, as complete removal of all glycosylation led to a significant loss of activity.
Article Abstract
The role of oligosaccharide modification in human acid beta-glucosidase function was investigated. This lysosomal enzyme has five putative N-glycosylation sites, four of which are occupied. The unglycosylated human protein was stable when expressed in bacteria or in Spodoptera frugiperda cells in the presence of tunicamycin but lacked catalytic activity. Deglycosylation of purified acid beta-glucosidase from human placenta with N-Glycanase under native conditions resulted in the removal of an accessible oligosaccharide chain from a single site with no effect on activity, whereas complete deglycosylation resulted in proportionate loss of activity. These studies demonstrate that occupancy of at least one glycosylation site is required for the formation and maintenance of acid beta-glucosidase in an active conformation.
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| http://dx.doi.org/10.1016/0006-291x(90)92388-g | DOI Listing |
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