| |
Reaction
Name | Pathway Name /
Pathway No. | Kf | Kb | Kd | tau | Reagents |
| 1 | dephosph-GEF | Ras
Pathway No. 367 | 1
(s^-1) | 0
(s^-1) | - | - | Substrate:
GEF*
Products:
inact-GEF
|
| 2 | Ras-intrinsic-GT
Pase | Ras
Pathway No. 367 | 0.0001
(s^-1) | 0
(s^-1) | - | - | Substrate:
GTP-Ras
Products:
GDP-Ras
|
| This is extremely slow (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 kf = 1e-4 | | 3 | dephosph-GAP | Ras
Pathway No. 367 | 0.1
(s^-1) | 0
(s^-1) | - | - | Substrate:
GAP*
Products:
GAP
|
| Assume a reasonably good rate for dephosphorylating it, 1/sec | | 4 | CaM-bind-GEF | Ras
Pathway No. 367 | 199.999
(uM^-1 s^-1) | 1
(s^-1) | Kd(bf) = 0.005(uM) | - | Substrate:
inact-GEF
CaM-Ca4
Products:
CaM-GEF
|
| We have no numbers for this. It is probably between the two extremes represented by the CaMKII phosph states, and I have used guesses based on this. kf=1e-4 kb=1 The reaction is based on Farnsworth et al Nature 376 524-527 1995 28 Feb 2006: Increased affinity 36-fold to account for Ca input to MAPK cascade, possibly folding in other pathway inputs. 21 April 2006: Altered affinity to same level as pkm_mapk21.g model to prevent spontaneous turnon. Kf = 200, Kb = 1. |
and 
color.
indicates that ordering is done according to ascending or descending order.