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Molecule Parameter List for I1* | 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 |
I1* acting as a Molecule in MAPK_network_2003 Network
| Name | Accession Name | Pathway Name | Initial Conc.
(uM) | Volume
(fL) | Buffered | | I1* | MAPK_network_
2003
Accession No. : 50 | PP1
Pathway No. : 218 | 0.001 | 1000 | No | | Dephosph is mainly by PP2B |
I1* 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 | CaM(Ca)n-CaNAB /
dephosph_inhib1 | MAPK_network_
2003
Accession No. : 50 | Shared_Object_
MAPK_network_
2003
Pathway No. : 206 | 4.97076 | 0.34 | 4 | explicit E-S complex | Substrate
I1*
Product
I1
| | 2 | PP2A /
PP2A-dephosph-I1
| MAPK_network_
2003
Accession No. : 50 | Shared_Object_
MAPK_network_
2003
Pathway No. : 206 | 7.82828 | 6 | 4.16667 | explicit E-S complex | Substrate
I1*
Product
I1
| | | PP2A does most of the dephosph of I1 at basal Ca levels. See the review by Cohen in Ann Rev Biochem 1989. For now, lets halve Km. k1 was 3.3e-6, now 6.6e-6 | | 3 | CaNAB-Ca4 /
dephosph_
inhib1_noCaM
| MAPK_network_
2003
Accession No. : 50 | Shared_Object_
MAPK_network_
2003
Pathway No. : 206 | 4.97076 | 0.034 | 4 | explicit E-S complex | Substrate
I1*
Product
I1
| | | The rates here are so slow I do not know if we should even bother with this enz reacn. These numbers are from Liu and Storm. Other refs suggest that the Km stays the same but the Vmax goes to 10% of the CaM stim levels. Prev: k1=2.2e-9, k2 = 0.0052, k3 = 0.0013 New : k1=5.7e-8, k2=.136, k3=.034 |
I1* 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 | PKA-active /
PKA-phosph-I1 | MAPK_network_
2003
Accession No. : 50 | Shared_Object_
MAPK_network_
2003
Pathway No. : 206 | 7.5 | 9 | 4 | explicit E-S complex | Substrate
I1
Product
I1*
| | #s from Bramson et al CRC crit rev Biochem 15:2 93-124. They have a huge list of peptide substrates and I have chosen high-ish rates. These consts give too much PKA activity, so lower Vmax 1/3. Now, k1 = 3e-5, k2 = 36, k3 = 9 (still pretty fast). Also lower Km 1/3 so k1 = 1e-5 Cohen et al FEBS Lett 76:182-86 1977 say rate =30% PKA act on phosphokinase beta. |
I1* 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 | | Inact-PP1 | MAPK_network_
2003
Accession No. : 50 | PP1
Pathway No. : 218 | 499.98
(uM^-1 s^-1) | 0.1
(s^-1) | Kd(bf) = 0.0002(uM) | - | Substrate
I1*
PP1-active
Product
PP1-I1*
| | K inhib = 1nM from Cohen Ann Rev Bioch 1989, 4 nM from Foukes et al Assume 2 nM. kf /kb = 8.333e-4 |
| Database compilation and code copyright (C) 2022, Upinder S. Bhalla and NCBS/TIFR
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