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. 2013 Aug 29;9(8):e1003207. doi: 10.1371/journal.pcbi.1003207

Table 1. Reactions that were changed in the background of the G38D mutation.

Na Reaction Equation Descriptionb O.P.c Mind Maxd Effecte
1 Inline graphic Intrinsic GαGTP GTPase activity 0.05 ×2 0 None
2 Inline graphic Intrinsic GαGTP-PDE GTPase activity 0.033 ×2 0 Slowed recovery when = 0
2 Inline graphic Intrinsic GαGTP-PDE- GαGTP GTPase activity 0.033 ×2 0 Slowed recovery when = 0
3 Inline graphic Binding of GαGTP to inactive PDE 5.5e-2 ×2 ×109 Slowed activation, lower sensitivity and recovery with changes >×106
4 Inline graphic Activation of one PDE catalytic subunit 940.7 ×2 ×104 Slowed activation phase with changes >×103
5 Inline graphic Binding of GαGTP to GαGTP-PDE 1.498e-9 ×2 ×105 None
6 Inline graphic Activation of the PDE tetramer 21.09 ×2 ×105 None
7 Inline graphic Binding of RGS9 to GαGTP-PDE 1.57e-7 ×2 ×15 Slowed recovery phase
7 Inline graphic Binding of RGS9 to GαGTP-PDE-GαGTP 1.57e-7 ×2 ×15 Slowed recovery phase
8 Inline graphic GAP activity and disruption of the complexes 256.07 ×2 ×105 Increase in saturating phase for bright flashes with changes >102
8 Inline graphic GAP activity and disruption of the complexes 256.07 ×2 ×105 Increase in saturating phase for bright flashes with changes >102
a

Reaction number, corresponding to that in Figure 1.

b

Type of reaction.

c

Original value of the parameter governing the reaction kinetics in the mathematical model (s−1) [14].

d

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.

e

Effect of these reductions.