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Molecule Parameter List for CaMKII-thr286 | 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 | Synaptic_
Network | 16 | Network |
Shared_Object_Synaptic_Network, PKC, PLA2,
PLCbeta, Gq, MAPK,
Ras, EGFR, Sos,
PLC_g, CaMKII, CaM,
PP1, PP2B, PKA,
AC, CaRegulation | This model is an annotated version of the synaptic signaling network.
The primary reference is Bhalla US and Iyengar R. Science (1999) 283(5400):381-7 but several of the model pathways have been updated.
Bhalla US Biophys J. 2002 Aug;83(2):740-52
Bhalla US J Comput Neurosci. 2002 Jul-Aug;13(1):49-62 |
CaMKII-thr286 acting as a Molecule in Synaptic_Network Network
| Name | Accession Name | Pathway Name | Initial Conc.
(uM) | Volume
(fL) | Buffered | | CaMKII-thr286 | Synaptic_
Network
Accession No. : 16 | CaMKII
Pathway No. : 80 | 0 | 1000 | No | | The threonine-286 phosphorylated form of CaMKII. It is likely to be a short-lived intermediate, since it will be phosphorylated further as soon as the CAM falls off. |
CaMKII-thr286 acting as a Summed Molecule in Synaptic_Network Network
| Accession Name | Pathway Name | Target | Input | Synaptic_
Network
Accession No. : 16 | CaMKII
Pathway No. : 80 | 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-thr286 acting as a Substrate for an Enzyme in Synaptic_Network 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 | Synaptic_
Network
Accession No. : 16 | CaMKII
Pathway No. : 80 | 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 | Synaptic_
Network
Accession No. : 16 | CaMKII
Pathway No. : 80 | 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 | | 3 | PP1-active /
Deph_thr286b | Synaptic_
Network
Accession No. : 16 | Shared_Object_
Synaptic_
Network
Pathway No. : 70 | 5.09907 | 0.35 | 4 | explicit E-S complex | Substrate
CaMKII-thr286
Product
CaMKII
| | | Rates 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-thr286 acting as a Product of an Enzyme in Synaptic_Network Network
Enzyme Molecule /
Enzyme Activity | Accession Name | Pathway Name | Km (uM) | kcat (s^-1) | Ratio | Enzyme Type | Reagents | PP1-active /
Deph-thr305 | Synaptic_
Network
Accession No. : 16 | Shared_Object_
Synaptic_
Network
Pathway No. : 70 | 5.09907 | 0.35 | 4 | explicit E-S complex | Substrate
CaMKII***
Product
CaMKII-thr286
| | Dephosphorylation kinetics 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-thr286 acting as a Substrate in a reaction in Synaptic_Network 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 | CaMK-thr286-bind
-CaM | Synaptic_
Network
Accession No. : 16 | CaMKII
Pathway No. : 80 | 1000.2
(uM^-1 s^-1) | 0.1
(s^-1) | Kd(bf) = 0.0001(uM) | - | Substrate
CaM-Ca4
CaMKII-thr286
Product
CaMKII-thr286*-C
aM
| | Affinity is up 1000X over the unphosphorylated CaMKII, which makes the Kd of 0.1 nM. See Hanson et al 1994 Neuron 12:943-956. Time to release is about 20 sec, so the kb is OK at 0.1/sec. as tested by a few runs. |
CaMKII-thr286 acting as a Product in a reaction in Synaptic_Network 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 | | basal-activity | Synaptic_
Network
Accession No. : 16 | CaMKII
Pathway No. : 80 | 0.003
(s^-1) | 0
(s^-1) | - | - | Substrate
CaMKII
Product
CaMKII-thr286
| | This reaction represents one of the unknowns in CaMK-II biochemistry: what maintains the basal level of phosphorylation on thr 286 ? See Hanson and Schulman Ann Rev Biochem 1992 61:559-601, specially pg 580, for review. I have not been able to find any compelling mechanism in the literature, but fortunately the level of basal activity is well documented. Lisman et al propose that the levels of PP1 are very low in the postsynaptic density, and PP2A is excluded from the PSD, and this would lead to autophosphorylation at a sustained level. |
| Database compilation and code copyright (C) 2022, Upinder S. Bhalla and NCBS/TIFR
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