Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.4.21.5 extracted from

  • De Filippis, V.; De Dea, E.; Lucatello, F.; Frasson, R.
    Effect of Na+ binding on the conformation, stability and molecular recognition properties of thrombin (2005), Biochem. J., 390, 485-492.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
Na+ binding of Na+ serves to stabilize the enzyme in a more open and rigid conformation. Na+-bound enzyme is more stable to denaturation by urea and more resistant to limited proteolysis by subtilisin Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens P00734 commercial preparation
-

Renatured (Commentary)

Renatured (Comment) Organism
denaturation by urea, 60% reversible at pH 8.0, completely reversible at pH 6.5. Na+-bound form of enzyme is more stable to urea denaturation than Na+-free form by 2 kcal/mol Homo sapiens