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Reaction List for pathway PKA (Pathway Number 135) | | 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 |
cAMP-bind-site-A
1 | 75
(uM^-1 s^-1) | 110
(s^-1) | Kd(bf) = 1.4667(uM) | - | cAMP2.R2C2
cAMP
| cAMP3.R2C2
| | 2 |
cAMP-bind-site-A
2 | 75
(uM^-1 s^-1) | 32.5
(s^-1) | Kd(bf) = 0.4333(uM) | - | cAMP
cAMP3.R2C2
| cAMP4.R2C2
| | 3 |
cAMP-bind-site-B
1 | 54
(uM^-1 s^-1) | 33
(s^-1) | Kd(bf) = 0.6111(uM) | - | R2C2
cAMP
| cAMP.R2C2
| | | Hasler et al FASEB J 6:2734-2741 1992 say Kd =1e-7M for type II, 5.6e-8 M for type I. Take mean which comes to 2e-13 #/cell Smith et al PNAS USA 78:3 1591-1595 1981 have better data. First kf/kb=2.1e7/M = 3.5e-5 (#/cell). Ogreid and Doskeland Febs Lett 129:2 287-292 1981 have figs suggesting time course of complete assoc is < 1 min. | | 4 |
cAMP-bind-site-B
2 | 54
(uM^-1 s^-1) | 33
(s^-1) | Kd(bf) = 0.6111(uM) | - | cAMP.R2C2
cAMP
| cAMP2.R2C2
| | | For now let us set this to the same Km (1e-7M) as site B. This gives kf/kb = .7e-7M * 1e6 / (6e5^2) : 1/(6e5^2) = 2e-13:2.77e-12 Smith et al have better values. They say that this is cooperative, so the consts are now kf/kb =8.3e-4 | | 5 |
inhib-PKA | 60
(uM^-1 s^-1) | 1
(s^-1) | Kd(bf) = 0.0167(uM) | - | PKA-active
PKA-inhibitor
| inhibited-PKA
| | | This has to be set to zero for matching the expts in vitro. In vivo we need to consider the inhibition though. | | 6 |
Release-C1 | 60
(s^-1) | 18
(uM^-1 s^-1) | Kd(cb) = 0.3(uM) | - | cAMP4.R2C2
| PKA-active
cAMP4.R2C
| | | This has to be fast, as the activation of PKA by cAMP is also fast. kf was 10 | | 7 |
Release-C2 | 60
(s^-1) | 18
(uM^-1 s^-1) | Kd(cb) = 0.3(uM) | - | cAMP4.R2C
| PKA-active
cAMP4.R2
|
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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