EC Number   |
General Information |
Reference  |
|---|
   2.4.1.143 | metabolism |
part of N-glycan pathway |
704576 |
| 2.4.1.143 | metabolism |
the enzyme functions at the N-glycan processing branch point and is one of the major factors determining the net outcome of the insect cell N-glycosylation pathway |
722801 |
| 2.4.1.143 | evolution |
enzyme TbGT15 belongs to the trypanosome beta3-glycosyltransferase superfamily |
-, 759473 |
| 2.4.1.143 | malfunction |
deletion of TbGT15 is accompanied by the absence of complex N-glycans, as well as alterations in the biosynthesis of the giant poly-Lac-dently from prior TbGnTI action, which is in contrast to canonical GnTIIs that only use substrates after modification by GnTI, i.e. Manalpha1-6(GlcNAcbeta1-2Manalpha1-3)Manbeta1-4GlcNAcbeta1-4GlcNAc |
-, 759473 |
| 2.4.1.143 | metabolism |
N-acetylglucosaminyltransferase I or II initiate the elaboration of the Manalpha1-3 and Manalpha1-6 arms, respectively, of the conserved trimannosyl-N-acetylchitobiosyl core of N-linked glycans. Proposed scheme for poly-LacNAc-containing N-glycans of bloodstream form trypanosomes, overview |
-, 759473 |
| 2.4.1.143 | more |
the enzyme sequence contains a DXD motif, which is generally involved in catalytic activity of known GTs |
-, 759473 |
| 2.4.1.143 | physiological function |
TbGT15 is the glycosyltransferase responsible for the transfer of beta1-2-linked GlcNAc to the alpha1-6-linked alpha-D-mannopyranosyl residue of Manalpha1-6(Manalpha1-3)Manbeta1-4GlcNAcbeta1-4GlcNAc. The enzyme initiates the elaboration of the Manalpha1-6 arms of the conserved trimannosyl-N-acetylchitobiosyl core of N-linked glycans, structure and biosynthesis of complex N-glycans in the human pathogen are analyzed, and the adaptation by trypanosomes of beta3-glycosyltransferase family members to catalyze beta-1-2 glycosidic linkages is demonstrated. TbGT15 is a non-essential gene in Trypanosoma brucei bloodstream form cells |
-, 759473 |
| 2.4.1.143 | physiological function |
beta-1,2-N-acetylglucosaminyltransferase II (GnTII) is a Golgi-localized type II transmembrane enzyme that catalyzes the transfer of N-acetylglucosamine to the 6-arm of the trimanosyl core of N-glycans, an essential step in the conversion of oligomannose-type to complex-type N-glycans |
759522 |
| 2.4.1.143 | evolution |
compared with the structure of human GnTII, the amino acid residues involved in catalytic activity and substrate recognition are almost fully conserved in Bombyx mori GnTII, which is consistent with its enzymatic properties |
759523 |
| 2.4.1.143 | metabolism |
beta-1,2-N-acetylglucosaminyltransferase II is a key enzyme for complex-type N-glycan biosynthesis. Both insect and mammalian cells produce Man(alpha1->6)[GlcNAc(beta1->2)Man(alpha1->3)]Man(beta1->4)GlcNAc(beta1->4)GlcNAc (MGn) glycan as an intermediate during N-glycan processing. In insect cells, beta-N-acetylglucosaminidase (fused lobes, FDL) removes a GlcNAc residue of the alpha1-3 arm of MGn glycan to produce Man(alpha1->6)[Man(alpha1->3)]ManGlcNAc2 (MM), a core structure from paucimannose-type N-glycans |
759523 |
