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Molecule Parameter List for PP-IP5  |  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 |  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. |  
  PP-IP5 acting as  a Molecule in  NonOsc_Ca_IP3metabolism Network
 | Name | Accession Name | Pathway Name | Initial Conc. (uM) | Volume (fL) | Buffered |  | PP-IP5 | NonOsc_Ca_ IP3metabolism Accession No. : 31 | IHP-system Pathway No. : 155 | 2 | 1000 | No |  |   Diphosphoinositol pentakisphosphate Conc from Huang et al, Biochem 37; 1998 |  
  PP-IP5 acting as a Substrate for an Enzyme in  NonOsc_Ca_IP3metabolism Network
 Enzyme Molecule / Enzyme Activity | Accession Name | Pathway Name | Km (uM) | kcat (s^-1) | Ratio | Enzyme Type | Reagents |  DIPP1  /  dipp_ip7 | NonOsc_Ca_ IP3metabolism Accession No. : 31 | IHP-system Pathway No. : 155 | 0.340006 | 5.1 | 4 | explicit E-S complex | Substrate PP-IP5
  Product IP6
  |  |   from Safrany et al, EMBO J 17(22); 1998 Vmax represents activity of recombinant human protein which is 20-50 fold greater than activity of the purified rat enzyme |  
  PP-IP5 acting as a Product of 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 | IP6_K2  /  ip6_k2 | NonOsc_Ca_ IP3metabolism Accession No. : 31 | IHP-system Pathway No. : 155 | 2.99999 | 1.633 | 4 | explicit E-S complex | Substrate IP6
  Product PP-IP5
  |  |     |   from Saiardi et al, Curr Biol 9; 1999 |  | 2 | DIPP1  /  dipp_ip8 | NonOsc_Ca_ IP3metabolism Accession No. : 31 | IHP-system Pathway No. : 155 | 0.0340035 | 0.6165 | 4 | explicit E-S complex | Substrate bisPP-IP4
  Product PP-IP5
  |  |     |   from Safrany et al, EMBO J 17(22); 1998 Vmax represents activity of human recombinant protein, which is 20-50 fold greater than activity of the purified rat enzyme |  
  PP-IP5 acting as a Substrate in a reaction in  NonOsc_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 |  | PP-IP5cmplx-on | NonOsc_Ca_ IP3metabolism Accession No. : 31 | IHP-system Pathway No. : 155 | 0.0027 (uM^-2 s^-1) | 2.5 (s^-1) | - | - | Substrate ATP PP-IP5 PP-IP5-K
  Product PP-IP5-K-complex
  |  |   from Huang et al, Biochem 37; 1998 Kf calculated using Km for PP-InsP5 and ATP, and Vmax of forward and backward reactions. Kb = Vmax of backward reaction  |  
  PP-IP5 acting as a Product in a reaction in  NonOsc_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 |  | IP6cmplx-off | NonOsc_Ca_ IP3metabolism Accession No. : 31 | IHP-system Pathway No. : 155 | 1.26 (s^-1) | 0.0012 (uM^-2 s^-1) | - | - | Substrate IP6-K-complex
  Product ADP IP6-K PP-IP5
  |  |   from Voglmaier et al, PNAS 93; 1996 Kf = Vmax of forward reaction Kb calculated from Km for InsP6 and ATP, and Vmax of forward and backward reactions |   
  
 
  | 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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