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Enzyme List for pathway Ras (Pathway Number 76)
| Molecule Name/ Site Name | Km (uM) | kcat (1/s) | Ratio (k2/k3) | Enzyme Type | Substrate | Product | |
| 1 | Enzyme Activity: CaM-GEF-act-ras Enzyme Molecule: CaM-GEF | 0.5051 | 0.02 | 4 | explicit E-S complex | GDP-Ras | GTP-Ras |
| Kinetics same as GEF-bg_act-ras | |||||||
| 2 | Enzyme Activity: GAP-inact-ras Enzyme Molecule: GAP | 1.0104 | 10 | 100 | explicit E-S complex | GTP-Ras | 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. | |||||||
| 3 | Enzyme Activity: GEF*-act-ras Enzyme Molecule: GEF* | 0.5051 | 0.02 | 4 | explicit E-S complex | GDP-Ras | 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. | |||||||
| 4 | Enzyme Activity: GEF-bg_act-ras Enzyme Molecule: GEF-Gprot-bg | 0.5051 | 0.02 | 4 | explicit E-S complex | GDP-Ras | GTP-Ras |
| Kinetics based on the activation of Gq by the receptor complex in the Gq model (in turn based on the Mahama and Linderman model) k1 = 2e-5, k2 = 1e-10, k3 = 10 (I do not know why they even bother with k2). Lets put k1 at 2e-6 to get a reasonable equilibrium More specific values from, eg.g: Orita et al JBC 268(34) 25542-25546 from rasGRF and smgGDS: k1=3.3e-7; k2 = 0.08, k3 = 0.02 | |||||||
| Pathway Detail | Molecule List | Enzyme List | Reaction List |