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Molecule Parameter List for MAPK_dash_tyr | 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 | Differential syn
thesis of mRNA | 95 | 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. |
MAPK_dash_tyr acting as a Molecule in Differential synthesis of mRNA Network
| Name | Accession Name | Pathway Name | Initial Conc.
(uM) | Volume
(fL) | Buffered | | MAPK_dash_tyr | Differential syn
thesis of mRNA
Accession No. : 95 | kinetics
Pathway No. : 1115 | 0 | 1000 | No | | Haystead et al FEBS Lett. 306(1) pp 17-22 show that phosphorylation is strictly sequential, first tyr185 then thr183. |
MAPK_dash_tyr acting as a Substrate for an Enzyme in Differential synthesis of mRNA Network
| | Enzyme Molecule /
Enzyme Activity | Accession Name | Pathway Name | Km (uM) | kcat (s^-1) | Ratio | Enzyme Type | Reagents | | 1 | MAPKK_star /
MAPKKthr | Differential syn
thesis of mRNA
Accession No. : 95 | kinetics
Pathway No. : 1115 | 0.0463 | 0.3 | 4 | explicit E-S complex | Substrate
MAPK_dash_tyr
Product
MAPK_star
| | | Rate consts same as for MAPKKtyr. | | 2 | MKP_dash_1 /
MKP1_dash_tyr_
dash_deph
| Differential syn
thesis of mRNA
Accession No. : 95 | kinetics
Pathway No. : 1115 | 0.1333 | 4 | 4 | explicit E-S complex | Substrate
MAPK_dash_tyr
Product
MAPK
| | | The original kinetics have been modified to obey the k2 = 4 * k3 rule, while keeping kcat and Km fixed. As noted in the NOTES, the only constraining data point is the time course of MAPK dephosphorylation, which this model satisfies. It would be nice to have more accurate estimates of rate consts and MKP-1 levels from the literature. Effective Km : 67 nM kcat = 1.43 umol/min/mg |
MAPK_dash_tyr acting as a Product of an Enzyme in Differential synthesis of mRNA Network
| | Enzyme Molecule /
Enzyme Activity | Accession Name | Pathway Name | Km (uM) | kcat (s^-1) | Ratio | Enzyme Type | Reagents | | 1 | MAPKK_star /
MAPKKtyr | Differential syn
thesis of mRNA
Accession No. : 95 | kinetics
Pathway No. : 1115 | 0.0463 | 0.3 | 4 | explicit E-S complex | Substrate
MAPK
Product
MAPK_dash_tyr
| | | The actual MAPKK is 2 forms from Seger et al JBC 267:20 14373(1992) Vmax = 150nmol/min/mg From Haystead et al FEBS 306(1):17-22 we get Km=46.6nM for at least one of the phosphs. Putting these together: k3=0.15/sec, scale to get k2=0.6. k1=0.75/46.6nM=2.7e-5 | | 2 | MKP_dash_1 /
MKP1_dash_thr_
dash_deph
| Differential syn
thesis of mRNA
Accession No. : 95 | kinetics
Pathway No. : 1115 | 0.1333 | 4 | 4 | explicit E-S complex | Substrate
MAPK_star
Product
MAPK_dash_tyr
| | | See MKP1-tyr-deph |
| Database compilation and code copyright (C) 2022, Upinder S. Bhalla and NCBS/TIFR
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