Energy released by GTP hydrolysis in baby hamster kidney (BHK)

Value 11 Kcal/mol
Organism Hamster spp.
Reference Li G, Qian H. Kinetic timing: a novel mechanism that improves the accuracy of GTPase timers in endosome fusion and other biological processes. Traffic. 2002 Apr3(4):249-55. link p.252 caption to figure 3 PubMed ID11929606
Method Abstract:"Here, [investigators] describe a mathematical model that shows how a directional GTPase cycle, in a nonequilibrium steady-state driven by GTP hydrolysis, can significantly reduce the variance in the lifetime of an activated GTPase molecule and thereby increase the accuracy and efficiency of the timer."
Comments p.252 caption to figure 3:"With these parameters, the equilibrium constant for GTP hydrolysis Keq=10^8, and the free energy ΔG½=-11 kcal/mol, corresponding to approximately the energy for a phosphate bond at 2mM [Pi]."
Entered by iriska
ID 112163