EC Number   |
General Information |
Reference |
|---|
   2.4.1.144 | physiological function |
N-acetylglucosaminyltransferase III catalyzes the addition of the bisecting GlcNAc branch on N-glycans, and is a metastasis suppressor with an important role of GnT-III in N-glycan biosynthesis and tumor cell behaviours. Increased expression of GnT-III in human hepatomas, glioma, and ovarian cancers. Overexpression of GnT-III significantly inhibits alpha2,3-sialylation but not alpha2,6-sialylation via post-transcriptional mechanisms. GnT-III plays an anti-migratory role in tumor cells without or with a low level of alpha2,6-linked sialic acids but not in those alpha2,6-hypersialylated |
736507 |
| 2.4.1.144 | physiological function |
N-acetylglucosaminyltransferase III is a glycosyltransferase which produces bisected N-glycans by transferring GlcNAc to the 4-position of core mannose. Bisected N-glycans are involved in physiological and pathological processes through the functional regulation of their carrier proteins |
735761 |
| 2.4.1.144 | physiological function |
N-acetylglucosaminyltransferase III is involved in formation of beta1,4 linkage between GlcNAc and beta-mannose residue within the core of oligosaccharide. The resulting bisected N-glycan acquires a characteristic conformation that renders inaccessibility to many other enzymes participating in biosynthetic pathways of hybrid and complex multiantennary N-glycans as well as to lectins |
735724 |
| 2.4.1.144 | physiological function |
N-acetylglucosaminyltransferases III (GnT-III) is one of the most important N-glycosyltransferases encoded by the MGAT3 gene. GnT-III catalyzes the addition of GlcNAc via b1-4 linkage to the b-mannose of the mannosyl core of N-glycans. N-acetylglucosaminyltransferase III (GnT-III) is correlated with tumor invasion and metastasis. GnT-III is an important regulator at the maternal-fetal interface during early pregnancy |
759591 |
| 2.4.1.144 | physiological function |
overexpression of GnT-III downregulates alpha5beta1 integrin-mediated cell spreading and migration, and the phosphorylation of the focal adhesion kinase. Overexpression of GnT-III slows E-cadherin turnover, resulting in increased E-cadherin expression on the surface of B16 melanoma cells. GnT-III inhibits GnT-V-induced cell migration. Overexpression of GnT-III inhibits cancer metastasis by at least two mechanisms: an enhancement in cell-cell adhesion and a downregulation of cell-ECM adhesion |
702516 |
| 2.4.1.144 | physiological function |
the enzyme induces a stabilizing effect on E-cadherin at the cell membrane by inducing a delay in the turnover rate of the protein, contributing for the formation of stable and functional adherens-junctions, and further preventing clathrin-dependent E-cadherin endocytosis. The enzyme plays a role on E-cadherin-mediated tumor suppression |
721738 |
| 2.4.1.144 | physiological function |
the enzyme plays an important role in the suppression of cancer metastasis. The enzyme influences epithelial-to-mesenchymal transition-like changes through not only prolongation of E-cadherin turnover but also suppression of beta-catenin-p-Smad complex formation. The enzyme plays important roles in transforming growth factor-beta-induced epithelial-to-mesenchymal transition-like changes. The enzyme does not significantly affect the expression of E-cadherin mRNA |
722755 |
