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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 | MAPK_network_
2003 | 50 | Network |
Shared_Object_MAPK_network_2003, PKC, PLA2,
PLCbeta, Gq, MAPK,
Ras, EGFR, Sos,
PLC_g, CaMKII, CaM,
PP1, PP2B, PKA,
AC | | This is a network model of many pathways present at the neuronal synapse. The network has properties of temporal tuning as well as steady-state computational properties. In its default form the network is bistable.Bhalla US Biophys J. 2004 Aug;87(2):745-53 |
Ca.PLC_g* acting as a Molecule in MAPK_network_2003 Network
| Name | Accession Name | Pathway Name | Initial Conc.
(uM) | Volume
(fL) | Buffered | | Ca.PLC_g* | MAPK_network_
2003
Accession No. : 50 | PLC_g
Pathway No. : 215 | 0 | 1000 | No | | |
Ca.PLC_g* acting as an Enzyme in MAPK_network_2003 Network
Enzyme Molecule /
Enzyme Activity | Accession Name | Pathway Name | Km (uM) | kcat (s^-1) | Ratio | Enzyme Type | Reagents | Ca.PLC_g* /
PIP2_hydrolysis
| MAPK_network_
2003
Accession No. : 50 | PLC_g
Pathway No. : 215 | 19.7917 | 57 | 4 | Classical Michaelis-Menten
V = Etot.S.Kcat/Km+S | 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 MAPK_network_2003 Network
Enzyme Molecule /
Enzyme Activity | Accession Name | Pathway Name | Km (uM) | kcat (s^-1) | Ratio | Enzyme Type | Reagents | L.EGFR /
phosph_PLC_g | MAPK_network_
2003
Accession No. : 50 | EGFR
Pathway No. : 213 | 0.333333 | 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 MAPK_network_2003 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 | | dephosph_PLC_g | MAPK_network_
2003
Accession No. : 50 | PLC_g
Pathway No. : 215 | 0.05
(s^-1) | 0
(s^-1) | - | - | Substrate
Ca.PLC_g*
Product
Ca.PLC_g
|
Ca.PLC_g* acting as a Product in a reaction in MAPK_network_2003 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* | MAPK_network_
2003
Accession No. : 50 | PLC_g
Pathway No. : 215 | 12
(uM^-1 s^-1) | 10
(s^-1) | Kd(bf) = 0.8333(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
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