EC Number   |
General Information |
Reference |
|---|
    2.4.1.267 | malfunction |
alg6 mutants accumulate lipid-linked Man9GlcNAc2 |
708620 |
| 2.4.1.267 | malfunction |
alg6-1 mutants accumulate Man9GlcNAc2-P-P-dolichol as their largest lipid-linked oligosaccharide in vivo and in vitro. alg6-1 cells are unable to transfer glucose from dolichol phosphoglucose to the unglucosylated lipid-linked oligosaccharide |
708963 |
| 2.4.1.267 | physiological function |
ALG6 deficient MI8-5 cells express 2fold lower levels of oligosaccharyltransferase STT3B than the parental Chinese hamster ovary cells. The combination of reduced expression of STT3B and the lack of the optimal Dol-PP-GlcNAc2Man9Glc3 donor synergize to cause very severe hypoglycosylation of proteins in MI8-5 cells |
736204 |
| 2.4.1.267 | physiological function |
fibroblasts from an ALG6-congenital disorders of glycosylation patient that carries the A333V mutation on the maternal ALG6 allele and the S308R and Y131H mutations on the paternal ALG6 allele assemble Dol-PP-GlcNAc2Man9 as the largest oligosaccharide donor. 3040% of oligosaccharyltransferase STT3A-dependent glycosylation sites and 20% of oligosaccharyltransferase STT3B-dependent sites are skipped in ALG6-congenital disorders of glycosylation fibroblasts |
736204 |
| 2.4.1.267 | physiological function |
three-state mechanism, where Dol-P-Glc binds before the Man9-containing acceptor substrate, because the glucose moiety is at the bottom of the active site cavity. Donor and acceptor substrates bind sequentially and Asp69 acts as a general base that abstracts the proton of the 3-hydroxyl group of the terminal A-branch mannose of the acceptor substrate to activate it for a nucleophilic attack |
759846 |
