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Molecule Parameter List for 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 | Accession and Pathway Details | |
Accession Name | Accession No. | Accession Type | Pathway Link | NonOsc_Ca_ IP3metabolism | 23 | Network | MIPP, CaMKII, CaM, PKC, IP3-3K, CaRegulation, Gq, PLCbeta, 134_dephos, 145_dephos, IP4-system, IHP-system, 1345_dephos | This network models detailed metabolism of Ins(145)P3, integrated with GPCR mediated PLCbeta activation and Ca release by the InsP3 receptor in the neuron. The calcium response is non-oscillatory. Mishra J, Bhalla US. Biophys J. 2002 Sep;83(3):1298-316. |
CaMKII*** acting as a Molecule in NonOsc_Ca_IP3metabolism Network
Name | Accession Name | Pathway Name | Initial Conc. (uM) | Volume (fL) | Buffered | CaMKII*** | NonOsc_Ca_ IP3metabolism Accession No. : 23 | CaMKII Pathway No. : 106 | 0 | 1000 | No | From Hanson and Schulman, the CaMKII does a lot of autophosphorylation just after the CaM is released. This prevents further CaM binding and renders the enzyme quite independent of Ca. |
CaMKII*** acting as a Summed Molecule in NonOsc_Ca_IP3metabolism Network
Accession Name | Pathway Name | Target | Input | NonOsc_Ca_ IP3metabolism Accession No. : 23 | CaMKII Pathway No. : 106 | 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*** |
CaMKII*** acting as a Substrate for an Enzyme in NonOsc_Ca_IP3metabolism Network
| Enzyme Molecule / Enzyme Activity | Accession Name | Pathway Name | Km (uM) | kcat (s^-1) | Ratio | Enzyme Type | Reagents | 1 | PP1-active / Deph-thr305 | NonOsc_Ca_ IP3metabolism Accession No. : 23 | CaMKII Pathway No. : 106 | 5.09907 | 0.35 | 4 | explicit E-S complex | Substrate CaMKII***
Product CaMKII-thr286
| | Dephosphorylation tempkin are assumed to be the same for all phosphorylation sites on CaMKII. The rates are from Stralfors et al Eur J Biochem 149 295-303 giving Vmax = 5.7 umol/min giving k3 = 3.5/sec and k2 = 14. Foulkes et al Eur J Biochem 132 309-313 1983 give Km = 5.1 uM so k1 becomes 5.72e-6 Simonelli 1984 (Grad Thesis, CUNY) showed that other substrates are about 1/10 rate of phosphorylase a, so we reduce k1,k2,k3 by 10 to 5.72e-7, 1.4, 0.35. This gives the final Km of 5.1, and Vmax of 0.35/sec. | 2 | PP1-active / Deph-thr286c | NonOsc_Ca_ IP3metabolism Accession No. : 23 | CaMKII Pathway No. : 106 | 5.09907 | 0.35 | 4 | explicit E-S complex | Substrate CaMKII***
Product CaMK-thr306
| | Dephosphorylation tempkin are assumed to be the same for all phosphorylation sites on CaMKII. The rates are from Stralfors et al Eur J Biochem 149 295-303 giving Vmax = 5.7 umol/min giving k3 = 3.5/sec and k2 = 14. Foulkes et al Eur J Biochem 132 309-313 1983 give Km = 5.1 uM so k1 becomes 5.72e-6 Simonelli 1984 (Grad Thesis, CUNY) showed that other substrates are about 1/10 rate of phosphorylase a, so we reduce k1,k2,k3 by 10 to 5.72e-7, 1.4, 0.35. This gives the final Km of 5.1, and Vmax of 0.35/sec. |
CaMKII*** acting as a Product of an Enzyme in NonOsc_Ca_IP3metabolism Network
| Enzyme Molecule / Enzyme Activity | Accession Name | Pathway Name | Km (uM) | kcat (s^-1) | Ratio | Enzyme Type | Reagents | 1 | tot_CaM_CaMKII / CaM_act_305 | NonOsc_Ca_ IP3metabolism Accession No. : 23 | CaMKII Pathway No. : 106 | 0.00000270563 | 6 | 4 | explicit E-S complex | Substrate CaMKII-thr286
Product CaMKII***
| | Rates from autocamtide phosphorylation, from Hanson and Schulman JBC 267:24 17216-17224 1992. See especially Fig 5. | 2 | tot_autonomous_ CaMKII / auton_305 | NonOsc_Ca_ IP3metabolism Accession No. : 23 | CaMKII Pathway No. : 106 | 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 |
| 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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