| | Ras |
| | Molecule |
| | Enzyme |
| | Reaction |
Enter a Search String | Special character and space not allowed in the query term.
Search string should be at least 2 characters long. |
Reaction List for pathway Ras (Pathway Number 184) | Kd is calculated only for second order reactions, like nA+nB <->nC or nA<->nC+nD, where n is number and A,B,C,D are molecules, where as for first order reactions Keq is calculated. Kd for higher order reactions is not considered. |   | Name | Kf | Kb | Kd | tau | Substrate | Product | 1 |
dephosph-GAP | 0.1 (s^-1) | 0 (s^-1) | - | - | GAP*
| GAP
| | Assume a reasonably good rate for dephosphorylating it, 0.1/sec. This fits well with resting levels of active kinase and the degree of activation as well as time-course of turnoff of Ras activation, but data is quite indirect. | 2 |
dephosph-GEF | 0.1 (s^-1) | 0 (s^-1) | - | - | GEF*
| inact-GEF
| | This rate is based on the known ratio of GDP-Ras to GTP-Ras. Basal: Ras.GTP = 7% Stimulated 15% Time course is within 10 min, probably much faster as not all early data points are there. See Gibbs et al JBC 265(33):20437-20422 | 3 |
Ras-intrinsic-GT Pase | 0.0001 (s^-1) | 0 (s^-1) | - | - | GTP-Ras
| GDP-Ras
| | This is extremely slow (kf = 1e-4), but it is significant as so little GAP actually gets complexed with it that the total GTP turnover rises only by 2-3 X (see Gibbs et al, JBC 265(33) 20437-20422) and Eccleston et al JBC 268(36) 27012-27019 There is no back reaction as we assume this to be a regular irreversible Michaelis-Menten zeroth order hydrolysis. |
Pathway Details Molecule List Enzyme List Reaction List
| Database compilation and code copyright (C) 2022, Upinder S. Bhalla and NCBS/TIFR This Copyright is applied to ensure that the contents of this database remain freely available. Please see FAQ for details. |
|