This eukaryotic enzyme cleaves off sequentially the two alpha-1,3-linked glucose residues from the Glc2Man9GlcNAc2 oligosaccharide precursor of immature N-glycosylated proteins.
prkcsh, ganab, giibeta, er glucosidase ii, alpha glucosidase ii, glucosidase ii beta-subunit, endoplasmic reticulum glucosidase ii, plant glucosidase, more
This eukaryotic enzyme cleaves off sequentially the two alpha-1,3-linked glucose residues from the Glc2Man9GlcNAc2 oligosaccharide precursor of immature N-glycosylated proteins.
the interaction of the mannose 6-phosphate receptor homologous domain present in GIIbeta with mannoses in the B and/or C arms of the glycans mediates glycan hydrolysis enhancement
interaction of the beta-subunit MRH domain with mannosyl-alpha-(1,2)-mannose, mannose 6-phosphate, mannosyl-N-acetylglucsamine, or glucose 6-phosphate, ligand binding structures, overview
the interaction of the mannose 6-phosphate receptor homologous domain present in GIIbeta with mannoses in the B and/or C arms of the glycans mediates glycan hydrolysis enhancement
the inability of beta-subunit MRH domain to efficiently recognize glucose eliminates the potential for the beta-subunit to compete with the catalytic alpha-subunit of GII for glucose present in arm A of the N-glycan, ligand binding structures, overview. Possible models for the influence of Trp409 in enzyme activity
glucosidase II plays a key role in glycoprotein biogenesis in the endoplasmic reticulum. It is responsible for the sequential removal of the two innermost glucose residues from the glycan, Glc3Man9GlcNAc2, transferred to Asn residues in proteins. The enzyme participates in the calnexin/calreticulin cycle, it removes the single glucose unit added to folding intermediates and misfolded glycoproteins by the UDP-Glc:glycoprotein glucosyltransferase
the interaction of the mannose 6-phosphate receptor homologous domain present in GIIbeta with mannoses in the B and/or C arms of the glycans mediates glycan hydrolysis enhancement
the enzyme is a heterodimer whose alpha-subunit GIIalpha bears the glycosyl hydrolase active site, whereas its beta-subunit GIIbeta is involved in GIIbeta endoplasmic reticulum retention and folding, but does not efficiently deglucosylate the physiological substrates Glc2Man9GlcNAc2 and GlcMan9GlcNAc2. GIIbeta is required for an efficient in vitro glucose trimming from G2M9 and G1M9, and processing of both middle and innermost glucoses
the alpha subunit bears the active site, and the beta subunit modulates the subunit alpha activity through its C-terminal mannose 6-phosphate receptor homologous domain
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
mannose 6-phosphate receptor homology domain of GII beta subunit bound to mannose, to 1.6 A resolution. No major difference in the overall fold of ligand-bound and unbound structures, but a repositioning of side chains throughout the binding pocket, including Y372
construction of alpha or beta-subunit deletion mutant strains, disruption of subunit GIIalpha leads to complete loss of enzyme activity, while in the absence of GIIbeta, the catalytic subunit GIIalpha of Schizosaccharomyces pombe folds to an active conformation able to hydrolyze 4-nitrophenyl alpha-D-glucopyranoside, phenotypes, overview
mutations of the primary binding pocket residues and adjacent W409, all inhibit the activity of GII both in vitro and in vivo, they do not cause a significant change in the overall fold of the GII beta subunit mannose 6-phosphate receptor homology domain but impact locally the stability of the binding pocket
beta-subunit, DNA and amino acid sequence determination and analysis, recombinant expression as His-tagged protein in Escherichia coli strain BL21(pREP4)
Structure of the lectin mannose 6-phosphate receptor homology (MRH) domain of glucosidase II, an enzyme that regulates glycoprotein folding quality control in the endoplasmic reticulum