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Reaction List for pathway PKA (Pathway Number 30) |
| 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) | - | R2C2-cAMP2 cAMP | R2C2-cAMP3 |
| Kf = 75 /sec/uM, Kb = 110 /sec; This site has higher Kd for cAMP (kinetics within bovine myocardium) Dagfinn Ogreid and Stein Ove Doskeland (1981) FEBS Lett. 129(2):287-292 | |||||||
| 2 | cAMP-bind-site-A 2 | 75 (uM^-1 s^-1) | 32.5 (s^-1) | Kd(bf) = 0.4333(uM) | - | cAMP R2C2-cAMP3 | R2C2-cAMP4 |
| Now cAMP shows effects of cooperativity and PKA has a low Kd for cAMP. | |||||||
| 3 | cAMP-bind-site-B 1 | 54 (uM^-1 s^-1) | 33 (s^-1) | Kd(bf) = 0.6111(uM) | - | R2C2 cAMP | R2C2-cAMP |
| Kf = 54 /sec/uM, Kb = 33 /sec; PKA in normal human T lymphocytes. Hasler et al (1992) FASEB J 6:2735-2741 Kd =1e-07 M for type II, 5.6e-08 M for type I; Stephen B. Smith et al (1981) PNAS, USA 78: 1591-1595 Ka1 = 2.1e+07 /M which gives Kd = 47 nM, Kan = 5e+08 /M or Kd of 2nM from Fig.7 | |||||||
| 4 | cAMP-bind-site-B 2 | 54 (uM^-1 s^-1) | 33 (s^-1) | Kd(bf) = 0.6111(uM) | - | R2C2-cAMP cAMP | R2C2-cAMP2 |
| Kf = 54 /sec/uM, Kb = 33 /sec; Same Km (1e-07M) assumed as site B1. kf/kb = 0.7e-07M*1e06/(6e05^02) = 2e-13:2.77e-12 | |||||||
| 5 | inhib-PKA | 60 (uM^-1 s^-1) | 1 (s^-1) | Kd(bf) = 0.0167(uM) | - | PKA-active PKA-inhibitor | inhibited-PKA |
| 6 | Release-C1 | 60 (s^-1) | 18 (uM^-1 s^-1) | Kd(cb) = 0.3(uM) | - | R2C2-cAMP4 | PKA-active R2C-cAMP4 |
| The complex starts to dissociate and release catalytic subunit C. This has to be fast, as the activation of PKA by cAMP is also fast. | |||||||
| 7 | Release-C2 | 60 (s^-1) | 18 (uM^-1 s^-1) | Kd(cb) = 0.3(uM) | - | R2C-cAMP4 | PKA-active R2-cAMP4 |
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