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Molecule Parameter List for Tot-active-CaMKII | 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 |
Tot-active-CaMKII 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 | 1 | 2 | 0 | 0 | 0 | 0 |
Accession and Pathway Details | |
Tot-active-CaMKII acting as a Molecule in CaMKII Network
Name | Accession Name | Pathway Name | Initial Conc. (uM) | Volume (fL) | Buffered | Tot-active-CaMKII | CaMKII Accession No. : 33 | CaMKII Pathway No. : 174 | 0 | 0.1309 | No | |
Tot-active-CaMKII acting as a Summed Molecule in CaMKII Network
Tot-active-CaMKII acting as an Enzyme in CaMKII Network
| Enzyme Molecule / Enzyme Activity | Accession Name | Pathway Name | Km (uM) | kcat (s^-1) | Ratio | Enzyme Type | Reagents | 1 | Tot-active-CaMKI I / phosph_T286
| CaMKII Accession No. : 33 | CaMKII Pathway No. : 174 | 0.254651 | 10 | 0 | explicit E-S complex | Substrate CaMKII-CaMCa4
Product Trapped-T286
| | This enzyme represents an intra-holoenzyme reaction from one active subunit to its neighbor. k1 is now in units of 1/sec. The Km, Ratio and Vmax terms are pretty meaningless. The enzyme really is there just to represent the forward rate of 0.5 from CaMKII-CaMCa4 to Trapped-T285. We have a high k3 so that the reac is limited only by k1. The enzyme itself does not have much purpose other than to allow scaling of the overall rate by the proportion of adjacent molecules in the appropriate state. | 2 | Tot-active-CaMKI I / phosph_T305
| CaMKII Accession No. : 33 | CaMKII Pathway No. : 174 | 1.27325 | 10 | 0 | explicit E-S complex | Substrate Autonomous
Product Capped
| | This enzyme also represents an intra-holoenzyme reaction. So it is not really treated as an enzyme in Holme's model, more like a probability of reaction that scales according to the number of active CaMKII neighboring subunits. Here we approximate it as an enzyme rate limited by the k1=0.1 step, no back reaction, and with a scaling from Total_CaMKII such that the effective forward rate will simply be the fraction of CaMKII that are active, times 1/10 for nearest neigbors, times k1. |
| 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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