EC Number |
General Information |
Reference |
---|
2.7.1.60 | metabolism |
rate-limiting in the sialic acid biosynthetic pathway |
705073 |
2.7.1.60 | metabolism |
sialic acid biosynthesis pathway |
706438 |
2.7.1.60 | metabolism |
the bifunctional enzyme UDP-GlcNAc 2-epimerase/ManNAc kinase, GNE, catalyzes the first two committed steps in sialic acid synthesis |
-, 722375 |
2.7.1.60 | metabolism |
the enzyme catalyzes the second step of the sialic acid catabolic pathway |
-, 758597 |
2.7.1.60 | metabolism |
UDP-GlcNAc 2-epimerase/ManNAc kinase (GNE) catalyzes the first two committed steps in sialic acid synthesis |
721653 |
2.7.1.60 | metabolism |
UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase is the key enzyme in the sialic acid biosynthetic pathway |
716189 |
2.7.1.60 | more |
active site structure of the N-acetylmannosamine kinase domain, ligand binding and reaction mechanism, catalytic role of Asp517, overview. The side chain of Asp-413 does not directly bind one of the oxygens of the beta-phosphate but is necessary for Mg2+ coordination and consequently crucial for ATP binding |
722749 |
2.7.1.60 | more |
epimerase enzymatic activity of isozymes GNE3 and GNE8 is likely absent, since the deleted fragment contains important substrate binding residues in homologous bacterial epimerases. Isozymes hGNE5-hGNE8 have a 53-residue deletion, which is assigned a role in substrate(UDP-GlcNAc) binding |
721653 |
2.7.1.60 | physiological function |
GNE exerts transcriptional control on genes related to endoplasmic reticulum stress. Association of low GNE activity and anoikis susceptibility |
722220 |
2.7.1.60 | physiological function |
the bifunctional UDP-N-acetylglucosamine-2-epimerase/N-acetylmannosamine kinase transforms UDP-N-acetylglucosamine to N-acetylmannosamine followed by its phosphorylation to ManNAc 6-phosphate and has a direct impact on the sialylation of cell surface components |
722749 |