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dc.contributor.authorStrachan, Heather Anne
dc.description.abstractDrosophila melanogaster Golgi Mannosidase IIb (dGMIIb) is a class II (CAZy GH38) α-mannosidase involved in the processing of N-glycan structures in the insect secretory pathway. The enzyme activity of this 140-145 kDa protein is stimulated by cobalt, sensitive to furanose inhibitor mimics (swainsonine and 1,4-di-deoxy-mannitol), and has a pH optimum of 6.0. dGMIIb is an ortholog of the well-characterized Drosophila melanogaster Golgi Mannosidase II (dGMII). The preferred natural substrate for dGMII is GlcNAcMan5GlcNAc2 asparagine (N)-linked proteins, whereas the preferred natural substrate for dGMIIb is Man5GlcNAc2. dGMII has been crystallized and its active site extensively studied as a potential target for inhibition in cancer therapeutics. Modeling of dGMIIb using the crystal structure of dGMII as a template reveals differences in the GlcNAc - binding “anchoring site” which may account for the distinct substrate specificities of these processing enzymes.
dc.subjectDrosophila melanogaster Golgi Mannosidase IIb
dc.subjectDrosophila melanogaster Golgi mannosidase II
dc.subjectalpha mannosidase II
dc.subjectαlpha mannosidase IIb
dc.titleExpression, purification and characterization of a Drosophila melanogaster Mannosidase orthologous to Drosophila melanogaster Golgi Mannosidase II
dc.description.departmentBiochemistry and Molecular Biology
dc.description.majorBiochemistry and Molecular Biology
dc.description.advisorKelley Moremen
dc.description.committeeKelley Moremen
dc.description.committeeMichael Tiemeyer
dc.description.committeeMichael Pierce

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