Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli | Homo sapiens |
Protein Variants | Comment | Organism |
---|---|---|
additional information | introduction of site-specific unnatural amino acids to facilitate crosslinking of monomeric subunits into predominantly obligate oligomeric species. Optimal crosslinking is achieved by encoding 4-benzoyl-L-phenylalanine at position 458, and exposing to long wavelength UV in the presence of substrate and cofactor. Purified hexameric complexes contain significant fractions of dimer and trimer (approximately 50%) along with another 10% tetramer and higher molecular mass species. Activity of the crosslinked enzyme is reduced by almost 60% relative to the uncrosslinked UGDH mutant | Homo sapiens |
General Stability | Organism |
---|---|
wild-type UGDH is relatively stable to proteolysis in the apoenzyme form but is further stabilized by addition of NADH cofactor, UDP-glucose substrate, or a combination of the two to form a ternary enzyme complex | Homo sapiens |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
120000 | - |
gel filtration, mutant containing 4-benzoyl-L-phenylalanine at position 96 | Homo sapiens |
360000 | - |
gel filtration, mutant containing 4-benzoyl-L-phenylalanine at position 458 | Homo sapiens |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | O60701 | - |
- |
Subunits | Comment | Organism |
---|---|---|
dimer | and trimer and hexamer, 2 * 60000, SDS-PAGE | Homo sapiens |
hexamer | and dimer and trimer, 6 * 60000, SDS-PAGE | Homo sapiens |
trimer | and dimer and hexamer, 3 * 60000, SDS-PAGE | Homo sapiens |