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Molecule Parameter List for IP3 | 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 | Ajay_Bhalla_
2004_PKM_Tuning | 76 | Network |
PKC, Shared_Object_Ajay_Bhalla_2004_PKM_tuning, PLA2,
PLCbeta, Gq, MAPK,
Ras, EGFR, Sos,
PLC_g, CaMKII, CaM,
PP1, PP2B, PKA,
AC, PKM | | This model is taken from the Ajay SM, Bhalla US. Eur J Neurosci. 2004 Nov;20(10):2671-80. This is the reference feedforward model from Figure 8a. |
IP3 acting as a Molecule in Ajay_Bhalla_2004_PKM_Tuning Network
IP3 acting as a Product of an Enzyme in Ajay_Bhalla_2004_PKM_Tuning Network
| | Enzyme Molecule /
Enzyme Activity | Accession Name | Pathway Name | Km (uM) | kcat (s^-1) | Ratio | Enzyme Type | Reagents | | 1 | PLC-Ca /
PLC-Ca | Ajay_Bhalla_
2004_PKM_Tuning
Accession No. : 76 | PLCbeta
Pathway No. : 315 | 19.8413 | 10 | 4 | explicit E-S complex | Substrate
PIP2
Product
DAG
IP3
| | | From Sternweis et al Phil Trans R Soc Lond 1992, also matched by Homma et al. k1 = 1.5e-5, now 4.2e-6 k2 = 70/sec; now 40/sec k3 = 17.5/sec; now 10/sec Note that the wording in Sternweis et al is ambiguous re the Km. | | 2 | PLC-Ca-Gq /
PLCb-Ca-Gq | Ajay_Bhalla_
2004_PKM_Tuning
Accession No. : 76 | PLCbeta
Pathway No. : 315 | 5.00003 | 48 | 4 | explicit E-S complex | Substrate
PIP2
Product
DAG
IP3
| | | From Sternweis et al, Phil Trans R Soc Lond 1992, and the values from other refs eg Homma et al JBC 263(14) pp6592 1988 match. k1 = 5e-5/sec k2 = 240/sec; now 120/sec k3 = 60/sec; now 30/sec Note that the wording in Sternweis et al is ambiguous wr. to the Km for Gq vs non-Gq states of PLC. K1 is still a bit too low. Raise to 7e-5 9 Jun 1996: k1 was 0.0002, changed to 5e-5 | | 3 | Ca.PLC_g /
PIP2_hydrolysis | Ajay_Bhalla_
2004_PKM_Tuning
Accession No. : 76 | PLC_g
Pathway No. : 321 | 97.2222 | 14 | 4 | explicit E-S complex | Substrate
PIP2
Product
DAG
IP3
| | | Mainly Homma et al JBC 263:14 1988 pp 6592, but these parms are the Ca-stimulated form. It is not clear whether the enzyme is activated by tyrosine phosphorylation at this point or not. Wahl et al JBC 267:15 10447-10456 1992 say that the Ca_stim and phosph form has 7X higher affinity for substrate than control. This is close to Wahl's figure 7, which I am using as reference. | | 4 | Ca.PLC_g* /
PIP2_hydrolysis | Ajay_Bhalla_
2004_PKM_Tuning
Accession No. : 76 | PLC_g
Pathway No. : 321 | 19.7917 | 57 | 4 | explicit E-S complex | Substrate
PIP2
Product
DAG
IP3
| | | Mainly Homma et al JBC 263:14 1988 pp 6592, but these parms are the Ca-stimulated form. It is not clear whether the enzyme is activated by tyrosine phosphorylation at this point or not. Wahl et al JBC 267:15 10447-10456 1992 say that this has 7X higher affinity for substrate than control. |
IP3 acting as a Substrate in a reaction in Ajay_Bhalla_2004_PKM_Tuning 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 | | Degrade-IP3 | Ajay_Bhalla_
2004_PKM_Tuning
Accession No. : 76 | PLCbeta
Pathway No. : 315 | 2.5
(s^-1) | 0
(s^-1) | - | - | Substrate
IP3
Product
Inositol
| | The enzyme is IP3 5-phosphomonesterase. about 45K. Actual products are Ins(1,4)P2, and cIns(1:2,4,5)P3. review in Majerus et al Science 234 1519-1526, 1986. Meyer and Stryer 1988 PNAS 85:5051-5055 est decay of IP3 at 1-3/sec |
| Database compilation and code copyright (C) 2022, Upinder S. Bhalla and NCBS/TIFR
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