|
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 tot_autonomous_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 |
| tot_autonomous_CaMKII participated as | Molecule | Sum total of | Enzyme | Substrate of an enzyme | Product of an enzyme | Substrate in Reaction | Product in Reaction | | No. of occurrences | 1 | 1 | 4 | 0 | 0 | 0 | 0 |
Accession and Pathway Details | |
| Accession Name | Accession No. | Accession Type | Pathway Link | NonOsc_Ca_
IP3metabolism | 31 | 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. 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. |
tot_autonomous_CaMKII acting as a Molecule in NonOsc_Ca_IP3metabolism Network
| Name | Accession Name | Pathway Name | Initial Conc.
(uM) | Volume
(fL) | Buffered | | tot_autonomous_CaMKII | NonOsc_Ca_
IP3metabolism
Accession No. : 31 | CaMKII
Pathway No. : 145 | 0 | 1000 | No | | 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*** |
tot_autonomous_CaMKII acting as a Summed Molecule in NonOsc_Ca_IP3metabolism Network
| Accession Name | Pathway Name | Target | Input | 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*** |
tot_autonomous_CaMKII acting as 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_autonomous_
CaMKII /
auton_305
| NonOsc_Ca_
IP3metabolism
Accession No. : 31 | CaMKII
Pathway No. : 145 | 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 | | 2 | tot_autonomous_
CaMKII /
auton_286
| NonOsc_Ca_
IP3metabolism
Accession No. : 31 | CaMKII
Pathway No. : 145 | 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 | | 3 | tot_autonomous_
CaMKII /
CaMK-phos
| NonOsc_Ca_
IP3metabolism
Accession No. : 31 | CaMKII
Pathway No. : 145 | 2.49999 | 0.5 | 4 | explicit E-S complex | Substrate
IP3_3K
Product
IP3_3K*
| | | rates referred from standard CaMKII phosphorylation rates | | 4 | tot_autonomous_
CaMKII /
CaMK-phos1
| NonOsc_Ca_
IP3metabolism
Accession No. : 31 | CaMKII
Pathway No. : 145 | 2.49995 | 0.5 | 4 | explicit E-S complex | Substrate
IP3_3K_CaM
Product
IP3_3K_CaM*
| | | rates referred from standard CaMKII phosphorylation rates |
| 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. |
|
