| 
 
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 |  Osc_Ca_ IP3metabolism | 24 | 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 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. |  
  tot_autonomous_CaMKII acting as  a Molecule in  Osc_Ca_IP3metabolism Network
 | Name | Accession Name | Pathway Name | Initial Conc. (uM) | Volume (fL) | Buffered |  | tot_autonomous_CaMKII | Osc_Ca_ IP3metabolism Accession No. : 24 | CaMKII Pathway No. : 121 | 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  Osc_Ca_IP3metabolism Network
 | Accession Name | Pathway Name | Target | Input |  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***  |  
  tot_autonomous_CaMKII acting as  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_autonomous_ CaMKII / auton_305
  | Osc_Ca_ IP3metabolism Accession No. : 24 | CaMKII Pathway No. : 121 | 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
  | Osc_Ca_ IP3metabolism Accession No. : 24 | CaMKII Pathway No. : 121 | 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
  | Osc_Ca_ IP3metabolism Accession No. : 24 | CaMKII Pathway No. : 121 | 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
  | Osc_Ca_ IP3metabolism Accession No. : 24 | CaMKII Pathway No. : 121 | 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. |   
  
 |