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Molecule Parameter List for GAP | 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 | | mRNA synthesis | 94 | Network |
kinetics, compartment_1, compartment_2 | | The model consists of three major pathways: Calcium-calmodulin dependent protein kinase IV (CaMKIV), Mitogen-activated protein kinase (MAPK) and Protein Phosphatase 1 (PP1). Each of these converged on CREB activation. We also modeled further interactions with Transducer of regulated CREB activity 1 (TORC1) and the protein kinase A (PKA) pathway. |
GAP acting as a Molecule in mRNA synthesis Network
| Name | Accession Name | Pathway Name | Initial Conc.
(uM) | Volume
(fL) | Buffered | | GAP | mRNA synthesis
Accession No. : 94 | kinetics
Pathway No. : 1112 | 0.01 | 1000 | No | | GTPase-activating proteins. See Boguski and McCormick. Turn off Ras by helping to hydrolyze bound GTP. This one is probably NF1, ie., Neurofibromin as it is inhibited by AA and lipids, and expressed in neural cells. p120-GAP is also a possible candidate, but is less regulated. Both may exist at similar levels. See Eccleston et al JBC 268(36) pp27012-19 Level=.002 16 May 2003: Increased level to 0.0036, in line with other concentration raises at the synapse. |
GAP acting as an Enzyme in mRNA synthesis Network
Enzyme Molecule /
Enzyme Activity | Accession Name | Pathway Name | Km (uM) | kcat (s^-1) | Ratio | Enzyme Type | Reagents | GAP /
GAP_dash_inact_
dash_ras
| mRNA synthesis
Accession No. : 94 | kinetics
Pathway No. : 1112 | 1.0104 | 10 | 4 | explicit E-S complex | Substrate
GTP_dash_Ras
Product
GDP_dash_Ras
| | From Eccleston et al JBC 268(36)pp27012-19 get Kd < 2uM, kcat - 10/sec From Martin et al Cell 63 843-849 1990 get Kd ~ 250 nM, kcat = 20/min I will go with the Eccleston figures as there are good error bars (10%). In general the values are reasonably close. k1 = 1.666e-3/sec, k2 = 1000/sec, k3 = 10/sec (note k3 is rate-limiting) 5 Nov 2002: Changed ratio term to 4 from 100. Now we have k1=8.25e-5; k2=40, k3=10. k3 is still rate-limiting. |
GAP acting as a Substrate for an Enzyme in mRNA synthesis Network
Enzyme Molecule /
Enzyme Activity | Accession Name | Pathway Name | Km (uM) | kcat (s^-1) | Ratio | Enzyme Type | Reagents | PKC_dash_active /
PKC_dash_inact_
dash_GAP
| mRNA synthesis
Accession No. : 94 | kinetics
Pathway No. : 1112 | 3.3333 | 4 | 4 | explicit E-S complex | Substrate
GAP
Product
GAP_star
| | Rate consts copied from PCK-act-raf This reaction inactivates GAP. The idea is from the Boguski and McCormick review. |
GAP acting as a Product in a reaction in mRNA synthesis 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_dash_
GAP | mRNA synthesis
Accession No. : 94 | kinetics
Pathway No. : 1112 | 0.1
(s^-1) | 0
(s^-1) | - | - | Substrate
GAP_star
Product
GAP
| | Assume a reasonably good rate for dephosphorylating it, 1/sec |
| Database compilation and code copyright (C) 2022, Upinder S. Bhalla and NCBS/TIFR
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