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Molecule Parameter List for IP2_3pase1  |  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 | 
| IP2_3pase1 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 | 0 | 1 | 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. |  
  IP2_3pase1 acting as  a Molecule in  Osc_Ca_IP3metabolism Network
 | Name | Accession Name | Pathway Name | Initial Conc. (uM) | Volume (fL) | Buffered |  | IP2_3pase1 | Osc_Ca_ IP3metabolism Accession No. : 24 | 134_dephos Pathway No. : 127 | 0.0038 | 1000 | No |  |   from Caldwell et al, JBC 266(27); 1991: 18378-86 Enzyme is a homodimer with two catalytic subunits. Conc of enzyme increased 2 times from 1.9 nM to account for two monomeric subunit pools  |  
  IP2_3pase1 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 |  IP2_3pase1 / ip2_3pase1
  | Osc_Ca_ IP3metabolism Accession No. : 24 | 134_dephos Pathway No. : 127 | 0.799992 | 117.33 | 4 | explicit E-S complex | Substrate IP2(13)
  Product IP1(1)
  |  |   from Caldwell et al, JBC 266; 1991 enzyme activity was assayed for the monomeric form of the enzyme |   
  
 
  | 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. |   
  
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