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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_traff_ model0 | 59 | Network | Shared_Object_AMPAR_traff_model0, CaMKII, CaM, PP1, PP2B, PP1_PSD, PKA, AC, AMPAR, AMPAR_memb | This is model 0 from Hayer and Bhalla, PLoS Comput Biol 2005. It has a bistable model of AMPAR traffick, plus a
non-bistable model of CaMKII. This differs from the reference model (model 1) in that model0 lacks degradation and turno
ver reactions for AMPAR. |
CaM acting as a Molecule in AMPAR_traff_model0 Network
Name | Accession Name | Pathway Name | Initial Conc. (uM) | Volume (fL) | Buffered | CaM | AMPAR_traff_ model0 Accession No. : 59 | CaM Pathway No. : 236 | 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_traff_model0 Network
CaM acting as a Substrate in a reaction in AMPAR_traff_model0 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_traff_ model0 Accession No. : 59 | CaM Pathway No. : 236 | 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_traff_ model0 Accession No. : 59 | CaM Pathway No. : 236 | 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 |
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