EC Number   |
General Information |
Reference |
|---|
    2.4.1.260 | malfunction |
loss-of-function mutations in EBS4 results in transfer of incompletely assembled glycans to polypeptides. The complete assembly of the lipid-linked glycans is essential for successful quality control of defective glycoproteins in Arabidopsis |
710276 |
| 2.4.1.260 | malfunction |
the alg12 mutant accumulates Manalpha1,2Manalpha1,2Manalpha1,3(Manalpha1,2Manalpha1,3Manalpha1,6)-Manbeta1,4-GlcNAcbeta1-4GlcNAcalpha/beta |
638572 |
| 2.4.1.260 | malfunction |
the variant surface glycoprotein sVSG221 synthesized by the ALG12-/- parasites shows different glycosylation patterns to that synthesized by wild-type cells, changes in sVSG221 glycosylation induced by the deletion of the ALG12 gene, overview |
722365 |
| 2.4.1.260 | physiological function |
generation of a HepG2 cell model of Alg12-congenital disorders of glycosylation by down-regulating dolichyl-P-mannose Man7GlcNAc2-PP-dolichol mannosyltransferase (Alg12), in order to provoke the accumulation of Man7GlcNAc2-PP-dolichol. The accumulation of Man7GlcNAc2-PP-dolichol in ALG12-downregulated cells coincides with the inhibition in cell growth noted between 4 and 8 days posttransfection. In down-regulated cells, brefeldin A provokes Golgi apparatus-endomannosidase trimming of Glc3Man9GlcNAc2-PP dolichol to yield a Man8GlcNAc2-PP-dolichol structure that does not give rise to cytoplasmic Man8GlcNAc2-P. Brefeldin A also strikingly increases oligosaccharyl phosphates derived from mature diphosphodolichol within the endomembrane system without affecting levels of Man7GlcNAc2-PP-dolichol or cytoplasmic Man7GlcNAc2-P |
736608 |
| 2.4.1.260 | physiological function |
oligosaccharyltransferase TbSTT3A is able to transfer Man7GlcNAc2 as well as Man5GlcNAc2 to its preferred acidic glycosylation site at residue Asn263 of variant surface protein. In a mutant lacking enzymic activity, i.e. in the absence of Man9GlcNAc2-PP-Dol, oligosaccharyltransferase TbSTT3B transfers both Man7GlcNAc2 and Man5GlcNAc2 to the remaining site at Asn428 of variant surface protein, albeit with low efficiency |
722365 |
| 2.4.1.260 | physiological function |
overexpression of enzyme in a dwarf mutant, bri1-9, the phenotypes of which are caused by endoplasmic reticulum retention and endoplasmic reticulum-associated degradation of a brassinosteroid receptor, BRASSINOSTEROID-INSENSITIVE 1, and a mutant lacking EBS3 activity, which catalyzes the ER luminal addition of two terminal alpha1,2 mannose residues in assembling the three-branched N-glycan precursor [glucose(Glc)]3(Man)9[N-acetylglucosamine(GlcNAc)]2, adds an alpha1,6-mannose to the truncated N-glycan precursor accumulated in the double mutant, promotes the bri1-9 endoplasmic reticulum-associated degradation, and neutralizes the EBS3 mutant suppressor phenotype |
723648 |
| 2.4.1.260 | physiological function |
the TbALG12 gene encodes the alpha1-6-mannosyltransferase that converts Man7GlcNAc2-PP-Dol to Man8GlcNAc2-PP-Dol |
722365 |
