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Molecule Parameter List for IP3-56K_IP4-1K | 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. |
IP3-56K_IP4-1K acting as a Molecule in NonOsc_Ca_IP3metabolism Network
Name | Accession Name | Pathway Name | Initial Conc. (uM) | Volume (fL) | Buffered | IP3-56K_IP4-1K | NonOsc_Ca_ IP3metabolism Accession No. : 31 | IP4-system Pathway No. : 154 | 1.632 | 1000 | No | Combined Ins(134)P3 5,6-kinase and Ins(3456)P4 1-kinase: from Yang and Shears, Biochem J 2000, 351: 551-555. Conc from Wilson and Majerus, JBC 271(20); 1996: 11904-10 5,6K Reaction products Ins(1346)P4 and Ins(1345)P4 are generated in a ratio of 2.3-5 : 1 Enzyme inhibition by products, as depicted in previous versions of the model, removed because it is now shown that enzyme is multi-tasking and reversible with respect to these products: Ho et al, Curr Biol 2002, 12: 1-20. This non M-M ability has been incorporated. But cycling to Ins(346)P3 by this enzyme not included because rest of Ins(346)P3 network biology is unknown in mammals. |
IP3-56K_IP4-1K 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 | 1 | IP3-Kcmplx-on | NonOsc_Ca_ IP3metabolism Accession No. : 31 | IP4-system Pathway No. : 154 | 4.2666 (uM^-1 s^-1) | 1.024 (s^-1) | Kd(bf) = 0.24(uM) | - | Substrate IP3(134) IP3-56K_IP4-1K
Product IP3-56Kcmplx
| | Kf and Kb are equivalent to k1 and k2 for InsP3 56-K, calculated from enzyme Km and Vmax: Yang and Shears, BiochemJ 2000, 351: 551-555 | 2 | ip4-1k-on | NonOsc_Ca_ IP3metabolism Accession No. : 31 | IP4-system Pathway No. : 154 | 31.2001 (uM^-1 s^-1) | 2.496 (s^-1) | Kd(bf) = 0.08(uM) | - | Substrate IP3-56K_IP4-1K IP4(3456)
Product ip4_1k_cmplx
| | Rates derives from enzyme Km and Vmax values: Yang and Shears, Biochem J 2000, 351: 551-555. |
IP3-56K_IP4-1K 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 | 1 | 6kinase | NonOsc_Ca_ IP3metabolism Accession No. : 31 | IP4-system Pathway No. : 154 | 0.256 (s^-1) | 0 (uM^-1 s^-1) | - | - | Substrate IP3-56Kcmplx
Product IP3-56K_IP4-1K IP4(1346)
| | Kf = Vmax for IP3 56-K from Yang and Shears, Biochem J 2000; 351:551-555 Enzyme reversibility reported in Ho et al, Curr Biol 2002, 12: 1-20. But backflow calculations do not show that Kb needs to be incorporated | 2 | 5kinase | NonOsc_Ca_ IP3metabolism Accession No. : 31 | IP4-system Pathway No. : 154 | 0.0701 (s^-1) | 0.006 (uM^-1 s^-1) | Kd(cb) = 0.086(uM) | - | Substrate IP3-56Kcmplx
Product IP3-56K_IP4-1K IP4(1345)
| | Kf = 0.274 times Vmax of IP3 56-K as product ratio of Ins(1345)P4 : Ins(1346)P4 is 1 : 2.3-5 from Wilson and Majerus, JBC 271; 1996 Kb ascertained from dG calculations for equilibrium conditions., for a dG = -10 kJ/mol Also enzyme reversibility reported in Ho et al, Curr Biol 2002, 12: 1-20 | 3 | ip4-1k-off | NonOsc_Ca_ IP3metabolism Accession No. : 31 | IP4-system Pathway No. : 154 | 0.624 (s^-1) | 0.056 (uM^-1 s^-1) | Kd(cb) = 0.0897(uM) | - | Substrate ip4_1k_cmplx
Product IP3-56K_IP4-1K IP5(13456)
| | Kf = enzyme Vmax : Yang and Shears, Biochem J 2000, 351, 551-5. Kb ascertained from dG calculations for equilibrium product substrate conditions. Ho et al, Curr Biol 2002, 12: 1-20 report a Vmax for reverse reaction of 0.0656 /sec. But this cannot be exactly incorporated unless Km for InsP5 is also known. Simulations show that incorporation of this reverse reaction can maintain basal InsP4 levels but cannot achieve the stimulated InsP4 levels shown in Ho et al. Hence the separate InsP5 1pase is retained. |
| 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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