General Stability | Organism |
---|---|
the stability and folding of yeast hexokinase isoenzyme ScHxk2 consisting of two domains with a discontinuous peptide sequence is analysed. Thermodynamic and spectroscopic analyses of urea-induced structural transitions indicate a thermodynamically stable folding intermediate, which is enzymatically inactive. Both structural domains are partially denatured in this central intermediate, even though tryptophan fluorescence, dynamic light scattering (DLS) and one-dimensional 1H NMR indicate a still compact but non-native structure | Saccharomyces cerevisiae |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
54000 | - |
- |
Saccharomyces cerevisiae |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharomyces cerevisiae | P04807 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + D-glucose | - |
Saccharomyces cerevisiae | ADP + D-glucose 6-phosphate | - |
? |
Subunits | Comment | Organism |
---|---|---|
monomer | - |
Saccharomyces cerevisiae |
Synonyms | Comment | Organism |
---|---|---|
ScHXK2 | - |
Saccharomyces cerevisiae |