|
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 PIP2 | 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 |
| PIP2 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 | 0 | 4 | 0 | 0 | 0 |
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 |
PIP2 acting as a Molecule in MAPK_network_2003 Network
PIP2 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 | | 1 | PLC-Ca /
PLC-Ca | MAPK_network_
2003
Accession No. : 50 | PLCbeta
Pathway No. : 209 | 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 | MAPK_network_
2003
Accession No. : 50 | PLCbeta
Pathway No. : 209 | 5 | 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 | 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. | | 4 | 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. |
| 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. |
|
