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Reaction List for pathway AC (Pathway Number 362) | 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 |
CaM-bind-AC1 | 49.9995 (uM^-1 s^-1) | 1 (s^-1) | Kd(bf) = 0.02(uM) | - | CaM-Ca4 AC1
| AC1-CaM
| | Half-max at 20 nM CaM (Tang et al JBC 266:13 8595-8603 1991 kb/kf = 20 nM = 12000 #/cell so kf = kb/12000 = kb * 8.333e-5 | 2 |
CaM_bind_PDE1 | 720 (uM^-1 s^-1) | 5 (s^-1) | Kd(bf) = 0.0069(uM) | - | PDE1 CaM-Ca4
| CaM.PDE1
| | For olf epi PDE1, affinity is 7 nM. Assume same for brain. Reaction should be pretty fast. Assume kb = 5/sec. Then kf = 5 / (0.007 * 6e5) = 1.2e-3 | 3 |
dephosph-AC2 | 0.1 (s^-1) | 0 (s^-1) | - | - | AC2*
| AC2
| | Random rate. | 4 |
dephosph-PDE | 0.1 (s^-1) | 0 (s^-1) | - | - | cAMP-PDE*
| cAMP-PDE
| | The rates for this are poorly constrained. In adipocytes (probably a different PDE) the dephosphorylation is complete within 15 min, but there are no intermediate time points so it could be much faster. Identity of phosphatase etc is still unknown. | 5 |
Gs-bind-AC1 | 126 (uM^-1 s^-1) | 1 (s^-1) | Kd(bf) = 0.0079(uM) | - | Gs-alpha AC1
| AC1-Gs
| | Half-max 8nM from Tang et al JBC266:13 8595-8603 kb/kf = 8 nM = 4800#/cell so kf = kb * 2.08e-4 | 6 |
Gs-bind-AC2 | 499.995 (uM^-1 s^-1) | 1 (s^-1) | Kd(bf) = 0.002(uM) | - | AC2 Gs-alpha
| AC2-Gs
| | Half-max at around 3nM = kb/kf from fig 5 in Feinstein et al PNAS USA 88 10173-10177 1991 kf = kb/1800 = 5.56e-4 kb Ofer's thesis data indicates it is more like 2 nM. kf = kb/1200 = 8.33e-4 | 7 |
Gs-bind-AC2* | 833.283 (uM^-1 s^-1) | 1 (s^-1) | Kd(bf) = 0.0012(uM) | - | Gs-alpha AC2*
| AC2*-Gs
| | kb/kf = 1.2 nM so kf = kb/720 = 1.3888 * kb. |
Pathway Details Molecule List Enzyme List Reaction List
| Database compilation and code copyright (C) 2022, Upinder S. Bhalla and NCBS/TIFR This Copyright is applied to ensure that the contents of this database remain freely available. Please see FAQ for details. |
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