Inhibitors | Comment | Organism | Structure |
---|---|---|---|
2-Phosphoglycolate | strong, competitive. Inhibition results in a large decrease in the unfolding rate constant of the protein. 2-phosphoglycolate shows similar binding affinities in the transition states for the rate-limiting steps of the forward and backward reactions, implicating that both transition states resemble each other in the active site architecture | Saccharomyces cerevisiae |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharomyces cerevisiae | - |
- |
- |
Renatured (Comment) | Organism |
---|---|
inhibitor 2-phosphoglycolate brings about a large decrease in the unfolding rate constant of the protein. Thermodynamics of binding reveal a dimeric transition state | Saccharomyces cerevisiae |