 |  |  PKA |
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Reaction List for pathway PLC_g (Pathway Number 356) | | 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 |
Ca_act_PLC_g | 180
(uM^-1 s^-1) | 10
(s^-1) | Kd(bf) = 0.0556(uM) | - | PLC_g
Ca
| Ca.PLC_g
| | | Nice curves from Homma et al JBC 263:14 6592-6598 1988 Fig 5c. The activity falls above 10 uM, but that is too high to reach physiologically anyway, so we'll ignore the higher pts and match the lower ones only. Half-max at 1 uM. But Wahl et al JBC 267:15 10447-10456 1992 have half-max at 56 nM which is what I'll use. | | 2 |
Ca_act_PLC_g* | 11.9997
(uM^-1 s^-1) | 10
(s^-1) | Kd(bf) = 0.8334(uM) | - | Ca
PLC_G*
| Ca.PLC_g*
| | | Again, we refer to Homma et al and Wahl et al, for preference using Wahl. Half-Max of the phosph form is at 316 nM. Use kb of 10 as this is likely to be pretty fast. Did some curve comparisons, and instead of 316 nM giving a kf of 5.27e-5, we will use 8e-5 for kf. 16 Sep 97. As we are now phosphorylating the Ca-bound form, equils have shifted. kf should now be 2e-5 to match the curves. | | 3 |
dephosph_PLC_g | 0.05
(s^-1) | 0
(s^-1) | - | - | Ca.PLC_g*
| Ca.PLC_g
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Pathway Details Molecule List Enzyme List Reaction List
| Database compilation and code copyright (C) 2022, Upinder S. Bhalla and NCBS/TIFR
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