EC Number   |
General Information |
Reference |
|---|
   2.4.1.143 | more |
Rossmann-like fold that employs conserved divalent cation-dependent substrate interactions with the UDP-GlcNAc donor. MGAT2 interactions with the extended glycan acceptor are distinct from other related glycosyltransferases. These interactions are composed of a catalytic subsite that binds the Man-(alpha1,6)- monosaccharide acceptor and a distal exosite pocket that binds the GlcNAc-beta1,2Man-alpha1,3Manbeta- substrate recognition arm. Substrate binding by MGAT2 employs both conserved and convergent catalytic subsite modules to provide substrate selectivity and catalysis. More broadly, the MGAT2 active-site architecture demonstrates how glycosyltransferases create complementary modular templates for regiospecific extension of glycan structures in mammalian cells. The enzyme MGAT2 employs a UDP-GlcNAc donor in a Mn2+-dependent inverting catalytic mechanism. structural basis for substrate recognition by MGAT2, structure-function analysis, structure comparisons, catalytic mechanism, detailed overview |
760070 |
| 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 |
beta-1,2-N-acetylglucosaminyltransferase II (GnTII) catalyzes the transfer of GlcNAc from a UDP-GlcNAc donor to the alpha1-6 arm of MGn glycan to produce biantennary complex-type glycans in mammalian cells |
759523 |
| 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 | 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 |
