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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. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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| Ca.PLC_g 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 | 1 | 1 | 0 | 0 | 2 |
Accession and Pathway Details |
| Accession Name | Accession No. | Accession Type | Pathway Link |
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
| Name | Accession Name | Pathway Name | Initial Conc. (uM) | Volume (fL) | Buffered |
| Ca.PLC_g | 2004_PKM_MKP3_ Tuning Accession No. : 77 | PLC_g Pathway No. : 338 | 0 | 1.5 | No |
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 | 2004_PKM_MKP3_ Tuning Accession No. : 77 | PLC_g Pathway No. : 338 | 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. | |||||||
Ca.PLC_g acting as a Substrate for 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 | 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 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 | |
| 1 | Ca_act_PLC_g | 2004_PKM_MKP3_ Tuning Accession No. : 77 | PLC_g Pathway No. : 338 | 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 | 2004_PKM_MKP3_ Tuning Accession No. : 77 | PLC_g Pathway No. : 338 | 0.05 (s^-1) | 0 (s^-1) | - | - | Substrate Ca.PLC_g* Product Ca.PLC_g |
color.