Table 1. Reactions that were changed in the background of the G38D mutation.
Na | Reaction Equation | Descriptionb | O.P.c | Mind | Maxd | Effecte |
1 | Intrinsic GαGTP GTPase activity | 0.05 | ×2 | 0 | None | |
2 | Intrinsic GαGTP-PDE GTPase activity | 0.033 | ×2 | 0 | Slowed recovery when = 0 | |
2 | Intrinsic GαGTP-PDE- GαGTP GTPase activity | 0.033 | ×2 | 0 | Slowed recovery when = 0 | |
3 | Binding of GαGTP to inactive PDE | 5.5e-2 | ×2 | ×109 | Slowed activation, lower sensitivity and recovery with changes >×106 | |
4 | Activation of one PDE catalytic subunit | 940.7 | ×2 | ×104 | Slowed activation phase with changes >×103 | |
5 | Binding of GαGTP to GαGTP-PDE | 1.498e-9 | ×2 | ×105 | None | |
6 | Activation of the PDE tetramer | 21.09 | ×2 | ×105 | None | |
7 | Binding of RGS9 to GαGTP-PDE | 1.57e-7 | ×2 | ×15 | Slowed recovery phase | |
7 | Binding of RGS9 to GαGTP-PDE-GαGTP | 1.57e-7 | ×2 | ×15 | Slowed recovery phase | |
8 | GAP activity and disruption of the complexes | 256.07 | ×2 | ×105 | Increase in saturating phase for bright flashes with changes >102 | |
8 | GAP activity and disruption of the complexes | 256.07 | ×2 | ×105 | Increase in saturating phase for bright flashes with changes >102 |
Reaction number, corresponding to that in Figure 1.
Type of reaction.
Original value of the parameter governing the reaction kinetics in the mathematical model (s−1) [14].
Minimum and maximum reductions the considered parameters were subjected to in the present study, in order to model the mutated conditions; when “Max R” was 0, the parameter was ultimately set to zero.
Effect of these reductions.