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Molecule Parameter List for CaMKII-CaM | 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 | Osc_Ca_
IP3metabolism | 32 | 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 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. |
CaMKII-CaM acting as a Molecule in Osc_Ca_IP3metabolism Network
| Name | Accession Name | Pathway Name | Initial Conc.
(uM) | Volume
(fL) | Buffered | | CaMKII-CaM | Osc_Ca_
IP3metabolism
Accession No. : 32 | CaMKII
Pathway No. : 159 | 0 | 1000 | No | | This is the regular, CaM-activated form of CaMKII. See the review Hanson and Schulman 1992 Ann. Rev. Biochem 60:559-601 |
CaMKII-CaM acting as a Summed Molecule in Osc_Ca_IP3metabolism Network
| Accession Name | Pathway Name | Target | Input | 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 |
CaMKII-CaM acting as a Substrate for 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_CaM_CaMKII /
CaM_act_286 | Osc_Ca_
IP3metabolism
Accession No. : 32 | CaMKII
Pathway No. : 159 | 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 | | 2 | tot_autonomous_
CaMKII /
auton_286 | Osc_Ca_
IP3metabolism
Accession No. : 32 | CaMKII
Pathway No. : 159 | 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 |
CaMKII-CaM acting as a Product of an Enzyme in Osc_Ca_IP3metabolism Network
Enzyme Molecule /
Enzyme Activity | Accession Name | Pathway Name | Km (uM) | kcat (s^-1) | Ratio | Enzyme Type | Reagents | PP1-active /
Deph-thr286 | Osc_Ca_
IP3metabolism
Accession No. : 32 | CaMKII
Pathway No. : 159 | 5.09907 | 0.35 | 4 | explicit E-S complex | Substrate
CaMKII-thr286*-C
aM
Product
CaMKII-CaM
| | 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-CaM acting as a Product in a reaction in Osc_Ca_IP3metabolism 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 | | CaMKII-bind-CaM | Osc_Ca_
IP3metabolism
Accession No. : 32 | CaMKII
Pathway No. : 159 | 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. |
| Database compilation and code copyright (C) 2022, Upinder S. Bhalla and NCBS/TIFR
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