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Molecule Parameter List for tot_autonomous_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_autonomous_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 | 4 | 0 | 0 | 0 | 0 |
Accession and Pathway Details | |
Accession Name | Accession No. | Accession Type | Pathway Link | Osc_Ca_ IP3metabolism | 24 | Network | MIPP, CaMKII, CaM, PKC, IP3-3K, Gq, PLCbeta, 134_dephos, 145_dephos, IP4-system, IHP-system, 1345_dephos, CaRegulation, Othmer-Tang-model | This network models an oscillatory calcium response to GPCR mediated PLCbeta activation, alongwith detailed InsP3 metabolism in the neuron. It differs from the NonOsc_Ca_IP3metabolism network in the CaRegulation module and in InsP3 receptor kinetics. Details of InsP3 receptor kinetics have been adapted from the Othmer-Tang model for oscillatory Ca dynamics. Mishra J, Bhalla US. Biophys J. 2002 Sep;83(3):1298-316. |
tot_autonomous_CaMKII acting as a Molecule in Osc_Ca_IP3metabolism Network
Name | Accession Name | Pathway Name | Initial Conc. (uM) | Volume (fL) | Buffered | tot_autonomous_CaMKII | Osc_Ca_ IP3metabolism Accession No. : 24 | CaMKII Pathway No. : 121 | 0 | 1000 | No | This is the sum total of the various CaM-independent forms of the kinase. There are actually several possible states here, but I only consider the forms thr-286 phosphorylated form and the doubly/triply phosphorylated form including the thr305/306, represented here as CaMKII*** |
tot_autonomous_CaMKII acting as a Summed Molecule in Osc_Ca_IP3metabolism Network
Accession Name | Pathway Name | Target | Input | Osc_Ca_ IP3metabolism Accession No. : 24 | CaMKII Pathway No. : 121 | tot_autonomous_CaMKII | CaMKII-thr286 CaMKII***
| This is the sum total of the various CaM-independent forms of the kinase. There are actually several possible states here, but I only consider the forms thr-286 phosphorylated form and the doubly/triply phosphorylated form including the thr305/306, represented here as CaMKII*** |
tot_autonomous_CaMKII acting as an Enzyme in Osc_Ca_IP3metabolism Network
| Enzyme Molecule / Enzyme Activity | Accession Name | Pathway Name | Km (uM) | kcat (s^-1) | Ratio | Enzyme Type | Reagents | 1 | tot_autonomous_ CaMKII / auton_305
| Osc_Ca_ IP3metabolism Accession No. : 24 | CaMKII Pathway No. : 121 | 0.00000416667 | 6 | 4 | explicit E-S complex | Substrate CaMKII-thr286
Product CaMKII***
| | See Hanson and Schulman 1992 JBC 267(24):17216-17224 for afterburst rates of phosphorylation | 2 | tot_autonomous_ CaMKII / auton_286
| Osc_Ca_ IP3metabolism Accession No. : 24 | CaMKII Pathway No. : 121 | 0.00000416667 | 0.5 | 4 | explicit E-S complex | Substrate CaMKII-CaM
Product CaMKII-thr286*-C aM
| | The autonomous rate has a slightly higher Km than the CaM-bound rate, but Vmax is the same. Hanson and Schulman 1992 Ann Rev Biochem 61:559-601 and Hanson and Schulman 1992 JBC 267(24):17216-17224 | 3 | tot_autonomous_ CaMKII / CaMK-phos
| Osc_Ca_ IP3metabolism Accession No. : 24 | CaMKII Pathway No. : 121 | 2.49999 | 0.5 | 4 | explicit E-S complex | Substrate IP3_3K
Product IP3_3K*
| | rates referred from standard CaMKII phosphorylation rates | 4 | tot_autonomous_ CaMKII / CaMK-phos1
| Osc_Ca_ IP3metabolism Accession No. : 24 | CaMKII Pathway No. : 121 | 2.49995 | 0.5 | 4 | explicit E-S complex | Substrate IP3_3K_CaM
Product IP3_3K_CaM*
| | rates referred from standard CaMKII phosphorylation rates |
| 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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