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Molecule Parameter List for IP3-56Kcmplx | 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 | Osc_Ca_ IP3metabolism | 32 | 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 is similar to the Osc_Ca_IP3metab model (accession 24) except that some enzymes in the InsP3 metabolism network have been modified to have reversible kinetics rather than Michaelis-Menten kinetics. The 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. |
IP3-56Kcmplx acting as a Molecule in Osc_Ca_IP3metabolism Network
Name | Accession Name | Pathway Name | Initial Conc. (uM) | Volume (fL) | Buffered | IP3-56Kcmplx | Osc_Ca_ IP3metabolism Accession No. : 32 | IP4-system Pathway No. : 167 | 0 | 1000 | No | enzyme substrate complex of IP3 56-K and Ins(134)P3. Complex exclusively modeled as reaction generates ratio of products, and because 5-kinase is reversible due to large Ins(1345)P4 backflux |
IP3-56Kcmplx acting as a Substrate in a reaction in Osc_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 | Osc_Ca_ IP3metabolism Accession No. : 32 | IP4-system Pathway No. : 167 | 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 | Osc_Ca_ IP3metabolism Accession No. : 32 | IP4-system Pathway No. : 167 | 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 |
IP3-56Kcmplx acting as a Product in a reaction in Osc_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 | IP3-Kcmplx-on | Osc_Ca_ IP3metabolism Accession No. : 32 | IP4-system Pathway No. : 167 | 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 |
| 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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