EC Number   |
General Information |
Reference |
|---|
    2.4.1.258 | malfunction |
alg3 yeast accumulates Man5GlcNAc2-P-P-dolichol due to a defective alphal,3-mannosyltransferase required for the next step in oligosaccharide-lipid elongation |
-, 636767 |
| 2.4.1.258 | malfunction |
Arabidopsis thaliana ALG3 mutant synthesizes immature oligosaccharides in the ER and accumulates unique N-glycans. Most of the proteins in alg3-T are not modified as high-mannose-type N-glycoproteins |
708617 |
| 2.4.1.258 | malfunction |
deletion of this gene in an och1 mutant background results in the secretion of glycoproteins with a Man5GlcNAc2 structure |
708601 |
| 2.4.1.258 | malfunction |
procyclic and bloodstream form null mutants of TbALG3 grow with normal kinetics, remain infectious to mice and tsetse flies, respectively, and have normal morphology. Both forms display aberrant N-glycosylation of their major surface glycoproteins, procylcin, and variant surface glycoprotein, respectively. The largest Dol-PP-linked oligosaccharide made by the TbALG3 null mutant is a biantennary Man5GlcNAc2 species |
708605 |
| 2.4.1.258 | malfunction |
the alg3 mutant accumulates D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol |
707606 |
| 2.4.1.258 | malfunction |
the inactivation of the nonessential ALG3 gene results in the accumulation of lipid-linked Man5GlcNAc2 and protein-bound carbohydrates which are completely Endo H resistant |
708619 |
| 2.4.1.258 | malfunction |
type IV of the carbohydrate deficient glycoprotein syndromes (CDGS) is characterized by microcephaly, severe epilepsy, minimal psychomotor development and partial deficiency of sialic acids in serum glycoproteins. The molecular defect in the index patient is a missense mutation in the gene encoding the mannosyltransferase that transfers mannose from dolichyl-phosphate mannose on to the lipid-linked oligosaccharide (LLO) intermediate Man(5)GlcNAc(2)-PP-dolichol. The defect results in the accumulation of the LLO intermediate and, due to its leaky nature, a residual formation of full-length LLOs. N-glycosylation is abnormal because of the transfer of truncated oligosaccharides in addition to that of full-length oligosaccharides and because of the incomplete utilization of N-glycosylation sites |
708327 |
| 2.4.1.258 | physiological function |
an the alg3 knockout strain displays decreased site-specific N-glycosylation occupancy preferentially at Asn-Xaa-Ser sequences located in secondary structural elements. Glycosylation sites are not uniformly affected in DELTAalg3 cells, with the subset of sites with lower affinity for oligosaccharyltransferase most strongly affected. 13 specific glycosylation sites are found which are underglycosylated in the DELTAalg3 strain compared to wild type cells. The features of these glycosylation sites suggest that they are the subset of normally modified sites that are more difficult for oligosaccharyltransferase to glycosylate. Under-glycosylated sites in the DELTAalg3 strain are likely to be present in secondary structural elements such as helices or sheets, whereas efficiently glycosylated sites are more likely present in flexible loops |
723056 |
| 2.4.1.258 | physiological function |
deletion of Alg3 results in the arrest of secondary infection hyphae and a significant reduction in virulence. Alg3 deletion mutants induce massive production of reactive oxygen species in host cells. Alg3-mediated N-glycosylation of the effector, Secreted LysM Protein1 (Slp1), is essential for its activity. Alg3 deletion mutants accumulate reactive oxygen species in a similar manner to Slp1 deletion mutants, which is a key factor responsible for arresting infection hyphae of the mutants |
736989 |
| 2.4.1.258 | physiological function |
deletion of the alg3+ gene in the och1 deletion mutant lacking alpha-1,6mannosyltransferase activity. Analysis of the detailed oligosaccharide structures in alg3och1 double mutant reveals that the N-linked oligosaccharides of Schizosaccharomyces pombe alg3och1 cells mainly consist of two or three alpha-galactose-capped M5B structures. Western blot analysis of recombinant human transferrin in alg3och1 cells suggests that heterologously expressed glycoproteins in this mutant have Endo H-resistant N-linked oligosaccharide structures similar to those of alg3och1 cell-surface glycoproteins |
722847 |
