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Molecule Parameter List for CaM | The statistics table lists the distribution of a molecule acting either as a substrate, product, enzyme or as a molecule within the network.
The text color of a molecule is highlighted by  color. | | Statistics |
Accession and Pathway Details | |
| Accession Name | Accession No. | Accession Type | Pathway Link | AMPAR_CaMKII_
strong_coupling | 64 | Network |
Shared_Object_AMPAR_CaMKII_strong_coupling, CaMKII, CaM,
PP1, AMPAR_memb, PP2B,
PKA, AC, PP1_PSD,
AMPAR | | This is a model of tight coupling between the AMPAR trafficking bistability, and the CaMKII autophosphorylation bistability. In this model, the CaMKII activity is self sustaining only when AMPAR is turned on. Further, CaMKII turns on when AMPAR is turned on. |
CaM acting as a Molecule in AMPAR_CaMKII_strong_coupling Network
| Name | Accession Name | Pathway Name | Initial Conc.
(uM) | Volume
(fL) | Buffered | | CaM | AMPAR_CaMKII_
strong_coupling
Accession No. : 64 | CaM
Pathway No. : 273 | 26.3333 | 0.09 | No | | There is a LOT of this in the cell: upto 1% of total protein mass. (Alberts et al) Say 25 uM. Meyer et al Science 256 1199-1202 1992 refer to studies saying it is comparable to CaMK levels. |
CaM acting as a Product of an Enzyme in AMPAR_CaMKII_strong_coupling Network
CaM acting as a Substrate in a reaction in AMPAR_CaMKII_strong_coupling Network
| 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 reaction are not consider. |
| | Name | Accession Name | Pathway Name | Kf | Kb | Kd | tau | Reagents | | 1 | CaM-TR2-bind-Ca | AMPAR_CaMKII_
strong_coupling
Accession No. : 64 | CaM
Pathway No. : 273 | 71.999
(uM^-2 s^-1) | 72
(s^-1) | Kd(af) = 1(uM) | - | Substrate
Ca
Ca
CaM
Product
CaM-TR2-Ca2
| | | Lets use the fast rate consts here. Since the rates are so different, I am not sure whether the order is relevant. These correspond to the TR2C fragment. We use the Martin et al rates here, plus the Drabicowski binding consts. All are scaled by 3X to cell temp. kf = 2e-10 kb = 72 Stemmer & Klee: K1=.9, K2=1.1. Assume 1.0uM for both. kb/kf=3.6e11. If kb=72, kf = 2e-10 (Exactly the same !).... | | 2 | neurogranin-bind
-CaM | AMPAR_CaMKII_
strong_coupling
Accession No. : 64 | CaM
Pathway No. : 273 | 0.3
(uM^-1 s^-1) | 1
(s^-1) | Kd(bf) = 3.3333(uM) | - | Substrate
CaM
neurogranin
Product
neurogranin-CaM
| | | Surprisingly, no direct info on rates from neurogranin at this time. These rates are based on GAP-43 binding studies. As GAP-43 and neurogranin share near identity in the CaM/PKC binding regions, and also similarity in phosph and dephosph rates, I am borrowing GAP-43 kinetic info. See Alexander et al JBC 262:13 6108-6113 1987 |
| Database compilation and code copyright (C) 2022, Upinder S. Bhalla and NCBS/TIFR
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