Description: The GlycoEnzDB is a manually curated glycoEnzyme database, primarily focused on humans. It covers 390 enzymes across 28 pathway maps. Facilities are also available to create custom glycosylation reaction pathways using experimental data in SBML format and for pathway simulation
Contacts: Sriram Neelamegham (email@example.com), Yusen Zhou (firstname.lastname@example.org) or Ted Groth (email@example.com).
• This functions as a heterodimeric enzyme complex GANAB (active part)/PRKCHS (inactive part) to provide a-glucosidase II activity.
• This removes the second and third α(1-3)Glc from Glc2Man9GlcNAc2-Asn during N-glycosylation processing to produce Man9GlcNAc2-Asn.
• In addition to N-glycan processing, α-Glucosidase II is also involved in protein folding quality control in the ER.
• Glycoproteins containing a single α(1-3)Glc residue is recognized by the ER lectin chaperones, calreticulin (CRT) and calnexin (CNX), that are complexed with protein disulfide isomerase isoforms and aid in folding and maturation of glycoproteins.
• Upon transient release from the lectin chaperones, α-Glucosidase II clips the remaining Glc and the protein moves to the next steps of processing provided it is well folded.
• If the glycoprotein is incompletely folded, the misfolded protein is recognized in the context of its N-glycan by the folding sensor UGGT. UGGT puts back one α(1-3)Glc that is removed by GANAB, and refolding is again attempted by CNX/CRT.
• This enzyme activity is inhibited by 1-deoxynojirimycin, N-5-carboxypentyl-dNM, and castanospermine.
• Mutations in PRKCSH were detected in patients with autosomal dominant polycystic liver disease (ADPLD).