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Reaction List for pathway AC (Pathway Number 85) | | 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 | 49.9998
(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 Assume a rapid CaM binding of 1/sec. | | 2 |
CaM_bind_PDE1 | 720
(uM^-1 s^-1) | 5
(s^-1) | Kd(bf) = 0.0069(uM) | - | PDE1
CaM-Ca4
| CaM.PDE1
| | | Borisy et al J Neurosci 12(3):915-923 For olf epithelium PDE1, affinity is 7 nM CaM and about 2 uM Ca which is consistent with it binding Ca4.CaM at 7 nM. Assume same for brain. Reaction should be pretty fast. Assume kb = 5/sec. | | 3 |
dephosph-AC2 | 0.1
(s^-1) | 0
(s^-1) | - | - | AC2*
| AC2
| | | Rate constrained by balancing levels of phosphorylated form, especially given resting PKC levels. | | 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 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 Also assume rapid binding of 1/sec. | | 6 |
Gs-bind-AC2 | 499.998
(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 Jacobowitz's thesis data indicates it is more like 2 nM. Jacobowitz, PhD Thesis, Mount Sinai School of Medicine. | | 7 |
Gs-bind-AC2* | 833.28
(uM^-1 s^-1) | 1
(s^-1) | Kd(bf) = 0.0012(uM) | - | Gs-alpha
AC2*
| AC2*-Gs
| | | Various references: Jacobowitz et al JBC 268(6):3829-3892 show that AC2 has a 2x rise in basal activation on phosphorylation, and a 2x rise in forskolin stimulated activation. Yoshimura and Cooper JBC 1993 268(7):4604-4607 say that type II is stimulated 9x over basal. Lustig et al 1993 JBC 268(19):13900-13905 syow a 2x activation by PDBu, and the Gs stimulated response is increased 2x-4x by PDBu. To match all these results with the binding of the unphosphorylated form we use a Kd of 1.2 nM here as compared with the Kd of 2 nM for the unphosphorylated reaction. |
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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