EC Number   |
General Information |
Reference |
|---|
   3.2.1.183 | malfunction |
defective GNE inhibition by CMP-Neu5Ac causes cytoplasmic accumulation and increased excretion of free sialic acid. Sialuria is an autosomal dominant disorder which is related to GNE mutation in one of the two arginine residues 263 and 266 (R263L, R266Q or R266W), the mutations in Arg263 and Arg266 can cause sialuria by hindering the enzyme inhibition through CMP-Neu5Ac binding |
749313 |
| 3.2.1.183 | malfunction |
distal myopathy with rimmed vacuoles (DMRV) is an autosomal recessive genetic disease characterized by weakness of the anterior compartment of the lower limbs, sparing the quadriceps muscle, and rimmed vacuoles in muscle biopsies. The disease is caused by a mutation in the UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase (GNE) gene located on chromosome 9p13.3. We present two cases of Chinese patients with progressive lower extremity weakness, phenotypes, overview |
748765 |
| 3.2.1.183 | malfunction |
GNE myopathy is autosomal recessive inherited and characterized by adult onset, slowly progressive muscle weakness and atrophy |
-, 722375 |
| 3.2.1.183 | malfunction |
hereditary inclusion body myopathy (GNE myopathy) is a neuromuscular disorder due to mutation in key sialic acid biosynthetic enzyme gene, GNE, D176V and V572L. Mutation in GNE affects beta1-integrin-mediated cell adhesion process in GNE mutant cells |
728341 |
| 3.2.1.183 | malfunction |
hereditary inclusion body myopathy (GNE myopathy) is a neuromuscular disorder due to mutation in key sialic acid biosynthetic enzyme, GNE. The subcellular distribution of recombinant GNE and its mutant shows differential localization in the cell. The enzyme mutation leads to hyposialylation of cell membrane receptor, beta1-integrin. Hyposialylated beta1-integrin localized to internal vesicles that is restored upon supplementation with sialic acid. Fibronectin stimulation causes migration of hyposialylated beta1-integrin to the cell membrane and colocalization with focal adhesion kinase (FAK) leading to increased focal adhesion formation. This further activates FAK and Src, downstream signaling molecules and leads to increased cell adhesion. The mutation in GNE affects beta1-integrin-mediated cell adhesion process in GNE mutant cells. Activation of endoplasmic reticulum stress response due to accumulation of misfolded mutated GNE protein |
748689 |
| 3.2.1.183 | malfunction |
impaired feed-back inhibition of the enzyme by CMP-Neu5Ac to regulate the GNE activity can result in sialuria |
748227 |
| 3.2.1.183 | malfunction |
isozymes hGNE3 and hGNE8 contain a 53-residue N-terminal deletion, epimerase enzymatic activity of isozymes GNE3 and GNE8 is likely absent, because the deleted fragment contains important substrate binding residues in homologous bacterial epimerases. Isozymes hGNE5-hGNE8 have a 53-residue deletion, which was assigned a role in substrate UDP-GlcNAc binding |
721653 |
| 3.2.1.183 | malfunction |
mutation M743T of enzyme GNE leads to GNE myopathy (i.e. hereditary inclusion body myopathy, HIBM), a unique muscle pathophysiology disorder |
748690 |
| 3.2.1.183 | malfunction |
neuC is deleted from the chromosome of EV36, a K-12-K1 hybrid, by allelic exchange. Exogenously added sialic acid restores capsule expression to the deletion strain, confirming that NeuC is necessary for sialic acid synthesis. The NeuC homologue from serotype III Streptococcus agalactiae complements deletion mutant |
-, 651736 |
| 3.2.1.183 | malfunction |
phenotype-genotype analysis of GNE myopathy index patients of a kohort, overview |
754462 |
