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Molecule Parameter List for GDP-Ras | 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 | |
GDP-Ras acting as a Molecule in MAPK-bistability-fig1c Network
Name | Accession Name | Pathway Name | Initial Conc. (uM) | Volume (fL) | Buffered | GDP-Ras | MAPK-bistability -fig1c Accession No. : 35 | Ras Pathway No. : 184 | 0.2 | 1000 | No | GDP bound form. See Rosen et al Neuron 12 1207-1221 June 1994. the activation loop is based on Boguski and McCormick Nature 366 643-654 93 Assume Ras is present at about the same level as craf-1, 0.2 uM. Hallberg et al JBC 269:6 3913-3916 1994 estimate upto 5-10% of cellular Raf is assoc with Ras. Given that only 5-10% of Ras is GTP-bound, we need similar amounts of Ras as Raf. |
GDP-Ras acting as a Substrate for an Enzyme in MAPK-bistability-fig1c Network
| Enzyme Molecule / Enzyme Activity | Accession Name | Pathway Name | Km (uM) | kcat (s^-1) | Ratio | Enzyme Type | Reagents | 1 | Shc*.Sos.Grb2 / Sos.Ras_GEF | MAPK-bistability -fig1c Accession No. : 35 | Shared_Object_ MAPK-bistability -fig1c Pathway No. : 179 | 0.505051 | 0.02 | 4 | explicit E-S complex | Substrate GDP-Ras
Product GTP-Ras
| | Rates from Orita et al JBC 268(34):25542-25546 | 2 | GEF* / GEF*-act-ras | MAPK-bistability -fig1c Accession No. : 35 | Ras Pathway No. : 184 | 0.505051 | 0.02 | 4 | explicit E-S complex | Substrate GDP-Ras
Product GTP-Ras
| | Kinetics from Orita et al JBC 268(34):25542-25546. Note that the Vmax is slow, but it does match the slow GTP hydrolysis rates. |
GDP-Ras acting as a Product of an Enzyme in MAPK-bistability-fig1c Network
Enzyme Molecule / Enzyme Activity | Accession Name | Pathway Name | Km (uM) | kcat (s^-1) | Ratio | Enzyme Type | Reagents | GAP / GAP-inact-ras | MAPK-bistability -fig1c Accession No. : 35 | Ras Pathway No. : 184 | 1.0104 | 10 | 100 | explicit E-S complex | Substrate GTP-Ras
Product GDP-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%). The two sets of values are reasonably close. k1 = 1.666e-3/sec, k2 = 1000/sec, k3 = 10/sec (note k3 is rate-limiting) This is one of the rare cases where we have direct info on the k3 being rate-limiting. Hence the ratio I use for the k2:k3 rates is 100 rather than the usual 4. |
GDP-Ras acting as a Product in a reaction in MAPK-bistability-fig1c 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 | Ras-intrinsic-GT Pase | MAPK-bistability -fig1c Accession No. : 35 | Ras Pathway No. : 184 | 0.0001 (s^-1) | 0 (s^-1) | - | - | Substrate GTP-Ras
Product GDP-Ras
| This is extremely slow (kf = 1e-4), but it is significant as so little GAP actually gets complexed with it that the total GTP turnover rises only by 2-3 X (see Gibbs et al, JBC 265(33) 20437-20422) and Eccleston et al JBC 268(36) 27012-27019 There is no back reaction as we assume this to be a regular irreversible Michaelis-Menten zeroth order hydrolysis. |
| 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. |
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