|
Enter a Search String | | Special character and space not allowed in the query term.
Search string should be at least 2 characters long. |
Molecule Parameter List for CaMK-thr306 | 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. |
CaMK-thr306 acting as a Molecule in Osc_Ca_IP3metabolism Network
| Name | Accession Name | Pathway Name | Initial Conc.
(uM) | Volume
(fL) | Buffered | | CaMK-thr306 | Osc_Ca_
IP3metabolism
Accession No. : 32 | CaMKII
Pathway No. : 159 | 0 | 1000 | No | | This forms due to basal autophosphorylation, but I think it has to be considered as a pathway even if some CaM is floating around. In either case it will tend to block further binding of CaM, and will not display any enzyme activity. See Hanson and Schulman JBC 267:24 pp17216-17224 1992 |
CaMK-thr306 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 | PP1-active /
Deph-thr306 | Osc_Ca_
IP3metabolism
Accession No. : 32 | CaMKII
Pathway No. : 159 | 5.09907 | 0.35 | 4 | explicit E-S complex | Substrate
CaMK-thr306
Product
CaMKII
| | 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. |
CaMK-thr306 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-thr286c | Osc_Ca_
IP3metabolism
Accession No. : 32 | CaMKII
Pathway No. : 159 | 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. |
| 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. |
|
