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Molecule Parameter List for MKP-1 | 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 |
MKP-1 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 | 2 | 0 | 0 | 0 | 0 |
Accession and Pathway Details | |
Accession Name | Accession No. | Accession Type | Pathway Link | MAPK_network_ 2003 | 50 | Network | Shared_Object_MAPK_network_2003, PKC, PLA2, PLCbeta, Gq, MAPK, Ras, EGFR, Sos, PLC_g, CaMKII, CaM, PP1, PP2B, PKA, AC | This is a network model of many pathways present at the neuronal synapse. The network has properties of temporal tuning as well as steady-state computational properties. In its default form the network is bistable.Bhalla US Biophys J. 2004 Aug;87(2):745-53 |
MKP-1 acting as a Molecule in MAPK_network_2003 Network
Name | Accession Name | Pathway Name | Initial Conc. (uM) | Volume (fL) | Buffered | MKP-1 | MAPK_network_ 2003 Accession No. : 50 | Shared_Object_ MAPK_network_ 2003 Pathway No. : 206 | 0.0024 | 1000 | No | MKP-1 dephosphoryates and inactivates MAPK in vivo: Sun et al Cell 75 487-493 1993. Levels of MKP-1 are regulated, and rise in 1 hour. Kinetics from Charles et al PNAS 90:5292-5296 1993. They refer to Charles et al Oncogene 7 187-190 who show that half-life of MKP1/3CH134 is 40 min. 80% deph of MAPK in 20 min Sep 17 1997: CoInit now 0.4x to 0.0032. See parm searches from jun96 on. |
MKP-1 acting as an Enzyme in MAPK_network_2003 Network
| Enzyme Molecule / Enzyme Activity | Accession Name | Pathway Name | Km (uM) | kcat (s^-1) | Ratio | Enzyme Type | Reagents | 1 | MKP-1 / MKP1-tyr-deph
| MAPK_network_ 2003 Accession No. : 50 | Shared_Object_ MAPK_network_ 2003 Pathway No. : 206 | 0.0666667 | 1 | 4 | explicit E-S complex | Substrate MAPK-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 | 2 | MKP-1 / MKP1-thr-deph
| MAPK_network_ 2003 Accession No. : 50 | Shared_Object_ MAPK_network_ 2003 Pathway No. : 206 | 0.0666667 | 1 | 4 | explicit E-S complex | Substrate MAPK*
Product MAPK-tyr
| | See MKP1-tyr-deph |
| 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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