|
Enter a Search String | Special character and space not allowed in the query term.
Search string should be at least 2 characters long. |
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 | 97.2222 | 14 | 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 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. |
Ca.PLC_g acting as a Substrate for 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 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 | 1 | Ca_act_PLC_g | MAPK_network_ 2003 Accession No. : 50 | PLC_g Pathway No. : 215 | 180 (uM^-1 s^-1) | 10 (s^-1) | Kd(bf) = 0.0556(uM) | - | Substrate Ca PLC_g
Product Ca.PLC_g
| | Nice curves from Homma et al JBC 263:14 6592-6598 1988 Fig 5c. The activity falls above 10 uM, but that is too high to reach physiologically anyway, so we'll ignore the higher pts and match the lower ones only. Half-max at 1 uM. But Wahl et al JBC 267:15 10447-10456 1992 have half-max at 56 nM which is what I'll use. | 2 | 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
|
| 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. |
|