EC Number   |
General Information |
Reference |
|---|
    2.4.1.256 | malfunction |
alg10 mutant strains accumulate lipid-linked Glc2Man9GlcNAc2. Hypoglycosylation of secreted proteins in alg10 deletion strains demonstrates that the terminal alpha-1,2-linked glucose residue is a key element in substrate recognition by the oligosaccharyltransferase. This ensures that primarily completely assembled oligosaccharide is transferred to protein |
708622 |
| 2.4.1.256 | physiological function |
a homozygous Arabidopsis T-DNA insertion mutant accumulates mainly lipid-linked Glc2Man9Glc-NAc2 and displays a severe protein underglycosylation defect. Mutant plants have altered leaf size when grown in soil. The inactivation of the enzyme gene in Arabidopsis results in the activation of the unfolded protein response, increased salt sensitivity and suppression of the phenotype of alpha-glucosidase I-deficient plants |
723427 |
| 2.4.1.256 | physiological function |
Alg10 gene deletion mutants, as well as endoplasmic reticulum lumenal mannosyltransferases (Alg3, Alg9, and Alg12), glucosyltransferases (Alg6, Alg8), or oligosaccharyltransferase subunits (Ost3, Ost5, and Ost6) deletion mutants, show decreased glycan occupancy and altered cell wall proteomes. Mutations in earlier mannosyltransferase or glucosyltransferase steps of glycan biosynthesis have stronger hypoglycosylation phenotypes, but glucosyltransferase defects are more severe |
736803 |
| 2.4.1.256 | physiological function |
alg10 mutant strains accumulate lipid-linked Glc2Man9GlcNAc2. Hypoglycosylation of secreted proteins in alg10 deletion strains demonstrates that the terminal alpha-1,2-linked glucose residue is a key element in substrate recognition by the oligosaccharyltransferase. This ensures that primarily completely assembled oligosaccharide is transferred to protein. The terminal alpha-1,2 glucose residue on the lipid-bound oligosaccharide serves as a signal to indicate complete assembly of the core oligosaccharide. Once transferred to protein, the removal of this signal by glucosidase I might ensure that glycosylation sites remain glycosylated and are not deglycosylated by the oligosaccharyltransferase complex |
708622 |
