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Literature summary for 5.3.1.1 extracted from

  • Gonzalez-Mondragon, E.; Zubillaga, R.A.; Hernandez-Arana, A.
    Effect of a specific inhibitor on the unfolding and refolding kinetics of dimeric triosephosphate isomerase: establishing the dimeric and similarly structured nature of the main transition states on the forward and backward reactions (2007), Biophys. Chem., 125, 172-178.
    View publication on PubMed

Inhibitors

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

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
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Renatured (Commentary)

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