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Molecule Parameter List for Ca.PLC_g* | 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_MKP3_
Tuning | 77 | Network |
Shared_Object_Ajay_Bhalla_2004_PKM_MKP3_Tuning, PKC, PLA2,
PLCbeta, Ras, Gq,
MAPK, EGFR, Sos,
PLC_g, CaMKII, CaM,
PP1, PP2B, PKA,
AC, MKP3, PKM | | This model is based on Ajay SM, Bhalla US. Eur J Neurosci. 2004 Nov;20(10):2671-80. This is the feedforward model with MPK3 from figure 8a. |
Ca.PLC_g* acting as a Molecule in Ajay_Bhalla_2004_PKM_MKP3_Tuning Network
Ca.PLC_g* acting as an Enzyme in Ajay_Bhalla_2004_PKM_MKP3_Tuning Network
Enzyme Molecule /
Enzyme Activity | Accession Name | Pathway Name | Km (uM) | kcat (s^-1) | Ratio | Enzyme Type | Reagents | Ca.PLC_g* /
PIP2_hydrolysis
| Ajay_Bhalla_
2004_PKM_MKP3_
Tuning
Accession No. : 77 | PLC_g
Pathway No. : 338 | 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. |
Ca.PLC_g* acting as a Product of an Enzyme in Ajay_Bhalla_2004_PKM_MKP3_Tuning Network
Enzyme Molecule /
Enzyme Activity | Accession Name | Pathway Name | Km (uM) | kcat (s^-1) | Ratio | Enzyme Type | Reagents | L.EGFR /
phosph_PLC_g | Ajay_Bhalla_
2004_PKM_MKP3_
Tuning
Accession No. : 77 | EGFR
Pathway No. : 336 | 0.333337 | 0.2 | 4 | explicit E-S complex | Substrate
Ca.PLC_g
Product
Ca.PLC_g*
| | Hsu et al JBC 266:1 603-608 1991 Km = 385 +- 100 uM, Vm = 5.1 +-1 pmol/min/ug for PLC-771. Other sites have similar range, but are not stim as much by EGF. k1 = 2.8e-2/385/6e5 = 1.2e-10. Phenomenally slow. But Sherrill and Kyte say turnover # for angiotensin II is 5/min for cell extt, and 2/min for placental. Also see Okada et al for Shc rates which are much faster. |
Ca.PLC_g* acting as a Substrate in a reaction in Ajay_Bhalla_2004_PKM_MKP3_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. |
Ca.PLC_g* acting as a Product in a reaction in Ajay_Bhalla_2004_PKM_MKP3_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 | | Ca_act_PLC_g* | Ajay_Bhalla_
2004_PKM_MKP3_
Tuning
Accession No. : 77 | PLC_g
Pathway No. : 338 | 11.9997
(uM^-1 s^-1) | 10
(s^-1) | Kd(bf) = 0.8334(uM) | - | Substrate
Ca
PLC_G*
Product
Ca.PLC_g*
| | Again, we refer to Homma et al and Wahl et al, for preference using Wahl. Half-Max of the phosph form is at 316 nM. Use kb of 10 as this is likely to be pretty fast. Did some curve comparisons, and instead of 316 nM giving a kf of 5.27e-5, we will use 8e-5 for kf. 16 Sep 97. As we are now phosphorylating the Ca-bound form, equils have shifted. kf should now be 2e-5 to match the curves. |
| 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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