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Molecule Parameter List for R2-cAMP4 | 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 |
R2-cAMP4 participated as | Molecule | Sum total of | Enzyme | Substrate of an enzyme | Product of an enzyme | Substrate in Reaction | Product in Reaction | No. of occurrences | 1 | 0 | 0 | 0 | 0 | 0 | 1 |
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. |
R2-cAMP4 acting as a Molecule in AMPAR_CaMKII_strong_coupling Network
Name | Accession Name | Pathway Name | Initial Conc. (uM) | Volume (fL) | Buffered | R2-cAMP4 | AMPAR_CaMKII_ strong_coupling Accession No. : 64 | PKA Pathway No. : 277 | 0 | 0.09 | No | Starts at 0.15 for the test of fig 6 in Smith et al, but we aren't using that paper any more. |
R2-cAMP4 acting as a Product 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. |
| 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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