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Molecule Parameter List for GTP.Ga | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| 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 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| GTP.Ga 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 | 0 | 0 | 2 | 1 |
Accession and Pathway Details |
| Accession Name | Accession No. | Accession Type | Pathway Link |
| cAMP_pathway | 25 | Network | Shared_Object_cAMP_pathway, PKA, AC, Gs |
| This is a model of the canonical cAMP signaling pathway: Ligand->Receptor->G-protein->Cyclase->cAMP->PKA. It also includes phosphodiesterases to balance out cAMP formation.Bhalla US Methods Enzymol. 2002;345:3-23 | |||
GTP.Ga acting as a Molecule in cAMP_pathway Network
| Name | Accession Name | Pathway Name | Initial Conc. (uM) | Volume (fL) | Buffered | |
| GTP.Ga | cAMP_pathway Accession No. : 25 | cAMP_pathway Pathway No. : 134 | 0 | 1000 | No | |
| Activated G protein. Supposed to be 15-40% of total Gs when max stim. | ||||||
GTP.Ga acting as a Substrate in a reaction in cAMP_pathway 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 | |
| 1 | Gs-bind-AC | cAMP_pathway Accession No. : 25 | AC Pathway No. : 136 | 499.998 (uM^-1 s^-1) | 1 (s^-1) | Kd(bf) = 0.002(uM) | - | Substrate AC GTP.Ga Product Gs.AC |
| Half-max at around 3nM = kb/kf from fig 5 in Feinstein et al PNAS USA 88 10173-10177 1991 kf = kb/1800 = 5.56e-4 kb Ofer Jacobowitz thesis (Mount Sinai 1995) data indicates it is more like 2 nM. | ||||||||
| 2 | GTPase | cAMP_pathway Accession No. : 25 | Gs Pathway No. : 137 | 0.0667 (s^-1) | 0 (s^-1) | - | - | Substrate GTP.Ga Product GDP.Ga |
| From Brandt and Ross JBC 261(4):1656-1664, rate is 4/min and is agonist independent. I treat this as irreversible. | ||||||||
GTP.Ga acting as a Product in a reaction in cAMP_pathway 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 |
| Activate-Gs | cAMP_pathway Accession No. : 25 | Gs Pathway No. : 137 | 0.025 (s^-1) | 0 (uM^-2 s^-1) | - | - | Substrate L.R.GDP.Gabc Product GTP.Ga Gbg L.R |
| This step combines several stages in GTP.Galpha release. From Berstein et al activation is at .35 - 0.7/min From Fay et al Biochem 30 5066-5075 1991 kf = .01/sec. From Brandt and Ross JBC 261(4):1656-1664 (1986) and Ransan et al Biochem J 283(2):519-524 (1992) rates around 2.5/min to 1.5/min are better. | |||||||
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