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CamKII found in these Models |
| | Name /
Accession No. | Accession
Type /
Entry Date | Model Type | Accession Statistics | CamKII Statistic | Species /
Tissue | Cell Compartment /
Source | Methodology /
Model_Implementation | Model in which CamKII acting as a molecule or reaction or enzyme are listed here. | 11 | MAPK_network_
2003/
Accession No. : 50 | Network /
2003-04-28 00:00:00 | Chemical | Molecule = 133
Enzyme = 62
Reaction = 79
| Molecule = 7
Enzyme = 4
Reaction = 1
| Generic mammalian /
Brain - Neuronal | Synapse /
Bhalla US Biophys J. 2004 Aug;87(2):745-53. ( peer-reviewed publication ) | Qualitative /
Exact GENESIS implementation | | | This is a network model of many pathways present at the neuronal synapse. The network has properties of temporal tuning as well as steady-state computational properties. In its default form the network is bistable.Bhalla US Biophys J. 2004 Aug;87(2):745-53 | | 12 | AMPAR_traff_
model0/
Accession No. : 59 | Network /
2005-07-19 00:00:00 | Chemical | Molecule = 130
Enzyme = 156
Reaction = 52
| Molecule = 21
Enzyme = 22
Reaction = 5
| General Mammalian /
Neuronal | Synaptic Spine, Postsynaptic Density /
Hayer A, Bhalla US PLoS Comput Biol. 2005 Jul;1(2):137-54. Epub 2005 Jul 29. ( Peer-reviewed publication ) | Quantitative match to experiments /
Exact GENESIS implementation | | | This is model 0 from Hayer and Bhalla, PLoS Comput Biol 2005. It has a bistable model of AMPAR traffick, plus a
non-bistable model of CaMKII. This differs from the reference model (model 1) in that model0 lacks degradation and turno
ver reactions for AMPAR. | | 13 | AMPAR_traff_
model1/
Accession No. : 60 | Network /
2005-07-19 00:00:00 | Chemical | Molecule = 132
Enzyme = 156
Reaction = 57
| Molecule = 21
Enzyme = 22
Reaction = 5
| General Mammalian /
Neuronal | Synaptic Spine, Postsynaptic Density /
Hayer A, Bhalla US PLoS Comput Biol. 2005 Jul;1(2):137-54. Epub 2005 Jul 29. ( Peer-reviewed publication ) | Quantitative match to experiments /
Exact GENESIS implementation | | | This is the basic model of AMPAR trafficking bistability. It is based on Hayer and Bhalla, PLoS Comput. Biol. 2005. It includes the degradation and turnover of AMPARs. The CaMKII portion of the model is not bistable. | | 14 | CaMKII_noPKA_
model3/
Accession No. : 62 | Network /
2005-07-19 00:00:00 | Chemical | Molecule = 53
Enzyme = 32
Reaction = 26
| Molecule = 21
Enzyme = 7
Reaction = 5
| General Mammalian /
Neuronal | Synaptic Spine, Postsynaptic Density /
Hayer A, Bhalla US PLoS PLoS Comput Biol. 2005 Jul;1(2):137-54. Epub 2005 Jul 29. ( Peer-reviewed publication ) | Quantitative match to experiments, Qualitative /
Exact GENESIS implementation | | | This is the model of CaMKII bistability, model 3. It exhibits bistability in CaMKII activation due to autophosphorylation at the PSD and local saturation of PP1. This version of model 3 does not include the full PKA regulatory pathway, and instead has a predefined initial amount of active PKA. | | 15 | CaMKII_model3/
Accession No. : 63 | Network /
2005-07-19 00:00:00 | Chemical | Molecule = 76
Enzyme = 40
Reaction = 39
| Molecule = 21
Enzyme = 7
Reaction = 5
| General Mammalian /
Neuronal | Synaptic Spine, Postsynaptic Density /
Hayer A, Bhalla US PLoS Comput Biol. 2005 Jul;1(2):137-54. Epub 2005 Jul 29. ( Peer-reviewed publication ) | Quantitative match to experiments, Qualitative /
Exact GENESIS implementation | | | This is the complete model of CaMKII bistability, model 3. It exhibits bistability in CaMKII activation due to autophosphorylation at the PSD and local saturation of PP1. This version of model 3 includes PKA regulatory input. This has little effect on the deterministic calculations, but the PKA pathway introduces a lot of noise which causes a difference in stochastic runs. |
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|  |
CamKII found in these Pathways |
| | Pathway
Name | Accession
Name | Model Type /
Accession Type | Pathway Statistics | CamKII Statistics | Source /
Entry
Date | Pathway in which CamKII acting as a molecule or reaction or enzyme are listed here. | 11 | NOS
Pathway No. : 90 | NOS_Phosph_
regulation
Accession No. : 20 | Chemical /
Pathway | Molecule = 10
Enzyme = 4
Reaction = 2
| Molecule = 1
Enzyme = 1
Reaction = 0
| In-house /
2001-12-25 00:00:00 | | | Related Pathway :
65, 66 | | | This model features the phosphorylation of rat brain neuronal NOS expressed in E. coli or Sf9 cells, which leads to a decrease in Vmax of the phosphorylated enzyme, with little change of both the Km for L-arginine and Kact for CaM. This is based on Hayashi Y. et al. J Biol Chem. (1999) 274(29):20597-602. They report of phosphorylatin being carried out by CaM kinases I alpha, II alpha and IV. The rates used have been obtained from their paper and from other reported experimental data. | | 12 | CaMKII
Pathway No. : 106 | NonOsc_Ca_
IP3metabolism
Accession No. : 23 | Chemical /
Network | Molecule = 10
Enzyme = 13
Reaction = 3
| Molecule = 8
Enzyme = 8
Reaction = 1
| Mishra J, Bhalla US. Biophys J. 2002 Sep;83(3):1298-316. ( peer-reviewed publication ) /
2002-01-07 00:00:00 | | | Related Pathway :
13, 26, 80, 121, 145, 159, 174, 202, 216, 235, 245, 258, 264, 272, 282, 322, 339, 357 | | | 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. | | 13 | CaMKII
Pathway No. : 121 | Osc_Ca_
IP3metabolism
Accession No. : 24 | Chemical /
Network | Molecule = 10
Enzyme = 13
Reaction = 3
| Molecule = 8
Enzyme = 8
Reaction = 1
| Mishra J, Bhalla US. Biophys J. 2002 Sep;83(3):1298-316. ( peer-reviewed publication ) /
2002-01-08 00:00:00 | | | Related Pathway :
13, 26, 80, 106, 145, 159, 174, 202, 216, 235, 245, 258, 264, 272, 282, 322, 339, 357 | | | 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. | | 14 | CaMKII
Pathway No. : 145 | NonOsc_Ca_
IP3metabolism
Accession No. : 31 | Chemical /
Network | Molecule = 10
Enzyme = 13
Reaction = 3
| Molecule = 8
Enzyme = 8
Reaction = 1
| Mishra J, Bhalla US. Biophys J. 2002 Sep;83(3):1298-316. ( peer-reviewed publication ) /
2002-04-03 00:00:00 | | | Related Pathway :
13, 26, 80, 106, 121, 159, 174, 202, 216, 235, 245, 258, 264, 272, 282, 322, 339, 357 | | | 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. It is similar to the NonOsc_Ca_IP3metab model (accession 23) except that some enzymes have been modified to have reversible kinetics rather than Michaelis-Menten kinetics. These modified enzymes belong to the groups: IP4-system, IP3-3K, 145_dephos and 134_dephos. Mishra J, Bhalla US. Biophys J. 2002 Sep;83(3):1298-316. | | 15 | CaMKII
Pathway No. : 159 | Osc_Ca_
IP3metabolism
Accession No. : 32 | Chemical /
Network | Molecule = 10
Enzyme = 13
Reaction = 3
| Molecule = 8
Enzyme = 8
Reaction = 1
| Mishra J, Bhalla US. Biophys J. 2002 Sep;83(3):1298-316. ( peer-reviewed publication ) /
2002-04-03 00:00:00 | | | Related Pathway :
13, 26, 80, 106, 121, 145, 174, 202, 216, 235, 245, 258, 264, 272, 282, 322, 339, 357 | | | This network models an oscillatory calcium response to GPCR mediated PLCbeta activation, alongwith detailed InsP3 metabolism in the neuron. It is similar to the Osc_Ca_IP3metab model (accession 24) except that some enzymes in the InsP3 metabolism network have been modified to have reversible kinetics rather than Michaelis-Menten kinetics. The modified enzymes belong to the groups: IP4-system, IP3-3K, 145_dephos and 134_dephos. Mishra J, Bhalla US. Biophys J. 2002 Sep;83(3):1298-316. |
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| |
CamKII acting as a Molecule |
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| |
CamKII acting as Summed Molecule |
| | Accession Name
Accession No. | Pathway Name
Pathway No. | Target | Input | | 11 | Osc_Ca_
IP3metabolism
Accession No. 24 | CaMKII
Pathway No. 121 | tot_CaM_CaMKII
| CaMKII-CaM
CaMKII-thr286*-C
aM
| | | This pool sums the levels of the CaM-bound forms of CaMKII: CaMKII-CaM + CaMKII-thr286*-CaM. Although their phosphorylation states are different, the level of activity is about the same so it makes sense to sum the levels. Hanson et al 1994 Neuron 12:943-956 | | 12 | 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*** | | 13 | NonOsc_Ca_
IP3metabolism
Accession No. 31 | CaMKII
Pathway No. 145 | tot_CaM_CaMKII
| CaMKII-CaM
CaMKII-thr286*-C
aM
| | | This pool sums the levels of the CaM-bound forms of CaMKII: CaMKII-CaM + CaMKII-thr286*-CaM. Although their phosphorylation states are different, the level of activity is about the same so it makes sense to sum the levels. Hanson et al 1994 Neuron 12:943-956 | | 14 | NonOsc_Ca_
IP3metabolism
Accession No. 31 | CaMKII
Pathway No. 145 | 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*** | | 15 | Osc_Ca_
IP3metabolism
Accession No. 32 | CaMKII
Pathway No. 159 | tot_CaM_CaMKII
| CaMKII-CaM
CaMKII-thr286*-C
aM
| | | This pool sums the levels of the CaM-bound forms of CaMKII: CaMKII-CaM + CaMKII-thr286*-CaM. Although their phosphorylation states are different, the level of activity is about the same so it makes sense to sum the levels. Hanson et al 1994 Neuron 12:943-956 |
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| |
CamKII acting as an Enzyme |
| | Enzyme Molecule /
Enzyme Activity | Accession Name
Accession No. | Pathway Name
Pathway No. | Km (uM) | kcat (s^-1) | Ratio | Enzyme Type | Reagents | | 11 | 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 | | 12 | tot_autonomous_
CaMKII
/
auton_286
| Synaptic_
Network
Accession No. 16 | CaMKII
Pathway No. 80 | 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 | | 13 | CaMKIIalpha
/
kenz
| NOS_Phosph_
regulation
Accession No. 20 | NOS
Pathway No. 90 | 5 | 28.5 | 4 | explicit E-S complex | Substrate:
nNOS
Product:
NOS*
| | | Hayashi et al., 1999, JBC,274(29):20597-20602. and from various other literature datas. | | 14 | 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. | | 15 | tot_CaM_CaMKII
/
CaM_act_286
| NonOsc_Ca_
IP3metabolism
Accession No. 23 | CaMKII
Pathway No. 106 | 0.00000270563 | 0.5 | 4 | explicit E-S complex | Substrate:
CaMKII-CaM
Product:
CaMKII-thr286*-C
aM
| | | See Hanson and Schulman 1992 JBC 267(24):17216-17224 |
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| |
CamKII acting as a Subtrate for an Enzyme |
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| |
CamKII acting as a Product for an Enzyme |
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| |
CamKII acting as a Reaction |
| | Name | Accession Name
Accession No. | Pathway Name
Pathway No. | Kf | Kb | Kd | tau | Reagents | Keq is calculated only for first order reactions.
Kd is calculated only for second order reactions. [ nA+nB <->nC or nA<->nC+nD, where n is number and A,B,C,D are molecules] | 11 | CaMKII-bind-CaM | AMPAR_traff_
model0
Accession No. 59 | CaMKII
Pathway No. 235 | 49.9997
uM^-1 s^-1 | 5
s^-1 | Kd(bf) = 0.1(uM) | - | Substrate:
CaM-Ca4
CaMKII
Product:
CaMKII-CaM
| | | This is tricky. There is some cooperativity here arising from interactions between the subunits of the CAMKII holoenzyme. However, the stoichiometry is 1. Kb/Kf = 6e4 #/cell. Rate is fast (see Hanson et al Neuron 12 943-956 1994) so lets say kb = 10. This gives kf = 1.6667e-4 H&S AnnRev Biochem 92 give tau for dissoc as 0.2 sec at low Ca, 0.4 at high. Low Ca = 100 nM = physiol. | | 12 | CaMKII-bind-CaM | AMPAR_traff_
model1
Accession No. 60 | CaMKII
Pathway No. 245 | 49.9997
uM^-1 s^-1 | 5
s^-1 | Kd(bf) = 0.1(uM) | - | Substrate:
CaM-Ca4
CaMKII
Product:
CaMKII-CaM
| | | This is tricky. There is some cooperativity here arising from interactions between the subunits of the CAMKII holoenzyme. However, the stoichiometry is 1. Kb/Kf = 6e4 #/cell. Rate is fast (see Hanson et al Neuron 12 943-956 1994) so lets say kb = 10. This gives kf = 1.6667e-4 H&S AnnRev Biochem 92 give tau for dissoc as 0.2 sec at low Ca, 0.4 at high. Low Ca = 100 nM = physiol. | | 13 | CaMKII-bind-CaM | CaMKII_noPKA_
model3
Accession No. 62 | CaMKII
Pathway No. 258 | 49.9997
uM^-1 s^-1 | 5
s^-1 | Kd(bf) = 0.1(uM) | - | Substrate:
CaM-Ca4
CaMKII
Product:
CaMKII-CaM
| | | This is tricky. There is some cooperativity here arising from interactions between the subunits of the CAMKII holoenzyme. However, the stoichiometry is 1. Kb/Kf = 6e4 #/cell. Rate is fast (see Hanson et al Neuron 12 943-956 1994) so lets say kb = 10. This gives kf = 1.6667e-4 H&S AnnRev Biochem 92 give tau for dissoc as 0.2 sec at low Ca, 0.4 at high. Low Ca = 100 nM = physiol. | | 14 | CaMKII-bind-CaM | CaMKII_model3
Accession No. 63 | CaMKII
Pathway No. 264 | 49.9997
uM^-1 s^-1 | 5
s^-1 | Kd(bf) = 0.1(uM) | - | Substrate:
CaM-Ca4
CaMKII
Product:
CaMKII-CaM
| | | This is tricky. There is some cooperativity here arising from interactions between the subunits of the CAMKII holoenzyme. However, the stoichiometry is 1. Kb/Kf = 6e4 #/cell. Rate is fast (see Hanson et al Neuron 12 943-956 1994) so lets say kb = 10. This gives kf = 1.6667e-4 H&S AnnRev Biochem 92 give tau for dissoc as 0.2 sec at low Ca, 0.4 at high. Low Ca = 100 nM = physiol. | | 15 | CaMKII-bind-CaM | AMPAR_CaMKII_
strong_coupling
Accession No. 64 | CaMKII
Pathway No. 272 | 49.9997
uM^-1 s^-1 | 5
s^-1 | Kd(bf) = 0.1(uM) | - | Substrate:
CaM-Ca4
CaMKII
Product:
CaMKII-CaM
| | | This is tricky. There is some cooperativity here arising from interactions between the subunits of the CAMKII holoenzyme. However, the stoichiometry is 1. Kb/Kf = 6e4 #/cell. Rate is fast (see Hanson et al Neuron 12 943-956 1994) so lets say kb = 10. This gives kf = 1.6667e-4 H&S AnnRev Biochem 92 give tau for dissoc as 0.2 sec at low Ca, 0.4 at high. Low Ca = 100 nM = physiol. |
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| |
CamKII acting as a Substrate in a Reaction |
| | Name | Accession Name
Accession No. | Pathway Name
Pathway No. | Kf | Kb | Kd | tau | Reagents | Keq is calculated only for first order reactions.
Kd is calculated only for second order reactions. [ nA+nB <->nC or nA<->nC+nD, where n is number and A,B,C,D are molecules] | 11 | CaMK-thr286-bind
-CaM | NonOsc_Ca_
IP3metabolism
Accession No. 23 | CaMKII
Pathway No. 106 | 1000.2
uM^-1 s^-1 | 0.1
s^-1 | Kd(bf) = 0.0001(uM) | - | Substrate:
CaMKII-thr286
CaM-Ca4
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. | | 12 | basal-activity | NonOsc_Ca_
IP3metabolism
Accession No. 23 | CaMKII
Pathway No. 106 | 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. | | 13 | CaMKII-bind-CaM | Osc_Ca_
IP3metabolism
Accession No. 24 | CaMKII
Pathway No. 121 | 49.9998
uM^-1 s^-1 | 5
s^-1 | Kd(bf) = 0.1(uM) | - | Substrate:
CaM-Ca4
CaMKII
Product:
CaMKII-CaM
| | | This is tricky. There is some cooperativity here arising from interactions between the subunits of the CAMKII holoenzyme. However, the stoichiometry is 1. Kd = 0.1 uM. Rate is fast (see Hanson et al Neuron 12 943-956 1994) Hanson and Schulman 1992 AnnRev Biochem 61:559-601 give tau for dissoc as 0.2 sec at low Ca, 0.4 at high. Low Ca = 100 nM = physiol. | | 14 | CaMK-thr286-bind
-CaM | Osc_Ca_
IP3metabolism
Accession No. 24 | CaMKII
Pathway No. 121 | 1000.2
uM^-1 s^-1 | 0.1
s^-1 | Kd(bf) = 0.0001(uM) | - | Substrate:
CaMKII-thr286
CaM-Ca4
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. | | 15 | basal-activity | Osc_Ca_
IP3metabolism
Accession No. 24 | CaMKII
Pathway No. 121 | 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. |
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| |
CamKII acting as a Product in a Reaction |
| | Name | Accession Name
Accession No. | Pathway Name
Pathway No. | Kf | Kb | Kd | tau | Reagents | Keq is calculated only for first order reactions.
Kd is calculated only for second order reactions. [ nA+nB <->nC or nA<->nC+nD, where n is number and A,B,C,D are molecules] | 11 | CaMK-thr286-bind
-CaM | NonOsc_Ca_
IP3metabolism
Accession No. 23 | CaMKII
Pathway No. 106 | 1000.2
uM^-1 s^-1 | 0.1
s^-1 | Kd(bf) = 0.0001(uM) | - | Substrate:
CaMKII-thr286
CaM-Ca4
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. | | 12 | basal-activity | NonOsc_Ca_
IP3metabolism
Accession No. 23 | CaMKII
Pathway No. 106 | 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. | | 13 | CaMKII-bind-CaM | Osc_Ca_
IP3metabolism
Accession No. 24 | CaMKII
Pathway No. 121 | 49.9998
uM^-1 s^-1 | 5
s^-1 | Kd(bf) = 0.1(uM) | - | Substrate:
CaM-Ca4
CaMKII
Product:
CaMKII-CaM
| | | This is tricky. There is some cooperativity here arising from interactions between the subunits of the CAMKII holoenzyme. However, the stoichiometry is 1. Kd = 0.1 uM. Rate is fast (see Hanson et al Neuron 12 943-956 1994) Hanson and Schulman 1992 AnnRev Biochem 61:559-601 give tau for dissoc as 0.2 sec at low Ca, 0.4 at high. Low Ca = 100 nM = physiol. | | 14 | CaMK-thr286-bind
-CaM | Osc_Ca_
IP3metabolism
Accession No. 24 | CaMKII
Pathway No. 121 | 1000.2
uM^-1 s^-1 | 0.1
s^-1 | Kd(bf) = 0.0001(uM) | - | Substrate:
CaMKII-thr286
CaM-Ca4
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. | | 15 | basal-activity | Osc_Ca_
IP3metabolism
Accession No. 24 | CaMKII
Pathway No. 121 | 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. |
| Statistics | To see the complete set of data Click here | To see Previous or Next set of entry click here |
| |
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