EC Number |
Subunits |
Reference |
---|
3.2.1.183 | ? |
x * 80000, recombinant wild-type and mutant enzymes, SDS-PAGE |
728341 |
3.2.1.183 | dimer |
- |
748227, 749313 |
3.2.1.183 | dimer |
2 * 75000, gel filtration |
-, 2280 |
3.2.1.183 | hexamer |
6 * 75000, gel filtration |
-, 2280 |
3.2.1.183 | More |
in the dimeric state GNE possess only kinase activity, in the hexameric state it displays both the epimerase and kinase activities while no activity is observed when GNE is present as a monomer |
748689 |
3.2.1.183 | More |
isozyme Gne2, secondary structure comparison with the human isozyme Gne2, the isozymes differ most in the N-terminal extension of 31 amino acids |
-, 722375 |
3.2.1.183 | More |
isozyme mGne1, secondary structure comparison with the human isozyme hGne1. The four homologous amino acid changes between mGne1 and hGNE1 are all located in the ManNAc kinase activity encoding domain of Gne; N447S and L523M in an alpha-helix domain, and R481Q and I484V in a coil domain, overview |
-, 722375 |
3.2.1.183 | More |
isozyme sequence comparisons, secondary structures, and structure modeling, overview. Isozymes hGNE2 and hGNE7 display a 31-residue N-terminal extension compared to isozyme hGNE1, isozymes hGNE3 and hGNE8 contain a 53-residue N-terminal deletion and a 50-residue N-terminal extension compared to hGNE1 |
721653 |
3.2.1.183 | More |
the epimerase part of the bifunctional UDP-GlcNAc 2-epimerase/ManNAc kinase (GNE) folds into two Rossmann-like domains and forms dimers and tetramers |
748227 |
3.2.1.183 | More |
the full-length enzyme can form a dimer or tetramer, depending on the presence of UDP-GlcNAc and CMP-Neu5Ac. GNE forms a closed tetramer in the presence of UDP-GlcNAc and CMP-Neu5Ac. The complex crystal structure of the N-terminal epimerase part of human GNE shows a tetramer in which UDP binds to the active site and CMP-Neu5Ac binds to the dimer-dimer interface. The enzyme is locked in a tightly closed conformation. Each dimer further forms a tetramer with a crystallographic dyad-related dimer |
749313 |