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Molecule Parameter List for IP4(1345) | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| 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. | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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| IP4(1345) 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 | 0 | 2 | 3 | 1 | 3 |
Accession and Pathway Details |
| Accession Name | Accession No. | Accession Type | Pathway Link |
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. | |||
IP4(1345) acting as a Molecule in NonOsc_Ca_IP3metabolism Network
| Name | Accession Name | Pathway Name | Initial Conc. (uM) | Volume (fL) | Buffered | |
| IP4(1345) | IP3metabolism Accession No. : 31 | IP3-3K Pathway No. : 148 | 1 | 1000 | No | |
| Inositol(1345)tetrakisphosphate | ||||||
IP4(1345) 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 | |
| 1 | IP_5pase1 / ip4_5pase | IP3metabolism Accession No. : 31 | 145_dephos Pathway No. : 153 | 0.80003 | 0.09 | 4 | explicit E-S complex | Substrate IP4(1345) Product IP3(134) |
| Ins(1345)P4 5-phosphatase activity of InsP 5-phosphatase1 from Hansen et al, JBC 262; 1987 vmax for IP4 substrate is approx 0.1 times vmax for IP3 | ||||||||
| 2 | 1345_3pase / ip4_3pase | IP3metabolism Accession No. : 31 | 1345_dephos Pathway No. : 156 | 0.400007 | 0.0012 | 4 | explicit E-S complex | Substrate IP4(1345) Product IP3(145) |
| Ins(1345)P4 3-phosphatase from Nogimori et al, JBC 266; 1991 | ||||||||
IP4(1345) 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 | IP3_3K / ip3-3k | IP3metabolism Accession No. : 31 | IP3-3K Pathway No. : 148 | 1.40001 | 3.0475 | 4 | explicit E-S complex | Substrate IP3(145) Product IP4(1345) |
| from Johanson et al, JBC 263; 1988 Original Vmax scaled up by 50% to obtain value at 37C, as enzyme assay was done at 30C Km increased from 0.2 to 1.4 as per various other reports (Shears Review, BiochemJ 260; 1989) | ||||||||
| 2 | IP3_3K*1 / ip3-3k*1 | IP3metabolism Accession No. : 31 | IP3-3K Pathway No. : 148 | 1.40004 | 0.76187 | 4.00003 | explicit E-S complex | Substrate IP3(145) Product IP4(1345) |
| from Sim et al, JBC 265; 1990 | ||||||||
| 3 | IP3_3K* / ip3-3k* | IP3metabolism Accession No. : 31 | IP3-3K Pathway No. : 148 | 1.40001 | 3.0475 | 4 | explicit E-S complex | Substrate IP3(145) Product IP4(1345) |
| from Communi et al, EMBO J 16; 1997 In absence of CaM binding, activity same as that of non-phosphorylated enzyme | ||||||||
IP4(1345) 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 |
| ip4(1345)_trp | IP3metabolism Accession No. : 31 | MIPP Pathway No. : 144 | 0.001 (s^-1) | 1 (s^-1) | Not applicable** | - | Substrate IP4(1345) Product IP4(1345)_ER |
| Ins(1345)P4 ER-cytosol transport | |||||||
IP4(1345) 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 | 3k-CaM*-off | IP3metabolism Accession No. : 31 | IP3-3K Pathway No. : 148 | 45 (s^-1) | 0.4148 (uM^-1 s^-1) | Kd(cb) = 0.0092(uM) | - | Substrate cmplx Product IP3_3K_CaM* IP4(1345) |
| Kf = Vmax for enzyme (Communi et al, EMBO J 16(8)) Vmax is such that enzyme activity is 9 fold above basal. Kb derived from Keq value when reaction free energy = -10 kJ/mol | ||||||||
| 2 | 3k-CaM-off | IP3metabolism Accession No. : 31 | IP3-3K Pathway No. : 148 | 10.5 (s^-1) | 0.0968 (uM^-1 s^-1) | Kd(cb) = 0.0092(uM) | - | Substrate 3kCaM_ip3_cmplx Product IP3_3K_CaM IP4(1345) |
| Kf = Vmax for enzyme: Erneux et al, Biochem 214; 1993 Enzyme is 2-2.5 fold more active than basal enzyme. Kb derived from equilibrium conditions for dG = -10 kJ/mol | ||||||||
| 3 | 5kinase | 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 | ||||||||
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