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Molecule Parameter List for MAPKK* | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| 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 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| MAPKK* 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 | 1 | 1 | 0 | 0 |
Accession and Pathway Details |
| Accession Name | Accession No. | Accession Type | Pathway Link |
2004_PKM_MKP3_ Tuning | 77 | Network | Shared_Object_Ajay_Bhalla_2004_PKM_MKP3_Tuning, PKC, PLA2, PLCbeta, Ras, Gq, MAPK, EGFR, Sos, PLC_g, CaMKII, CaM, PP1, PP2B, PKA, AC, MKP3, PKM |
| This model is based on Ajay SM, Bhalla US. Eur J Neurosci. 2004 Nov;20(10):2671-80. This is the feedforward model with MPK3 from figure 8a. | |||
MAPKK* acting as a Molecule in Ajay_Bhalla_2004_PKM_MKP3_Tuning Network
| Name | Accession Name | Pathway Name | Initial Conc. (uM) | Volume (fL) | Buffered | |
| MAPKK* | 2004_PKM_MKP3_ Tuning Accession No. : 77 | MAPK Pathway No. : 335 | 0 | 1.5 | No | |
| MAPKK phosphorylates MAPK on both the tyr and thr residues, first tyr then thr. Refs: Seger et al JBC267:20 pp 14373 1992 The MAPKK itself is phosphorylated on ser as well as thr residues. Let us assume that the ser goes first, and that the sequential phosphorylation is needed. See Kyriakis et al Nature 358 417-421 1992 | ||||||
MAPKK* acting as an Enzyme in Ajay_Bhalla_2004_PKM_MKP3_Tuning Network
| Enzyme Molecule / Enzyme Activity | Accession Name | Pathway Name | Km (uM) | kcat (s^-1) | Ratio | Enzyme Type | Reagents | |
| 1 | MAPKK* / MAPKKtyr | 2004_PKM_MKP3_ Tuning Accession No. : 77 | MAPK Pathway No. : 335 | 0.0462963 | 0.3 | 4 | explicit E-S complex | Substrate MAPK Product MAPK-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 | MAPKK* / MAPKKthr | 2004_PKM_MKP3_ Tuning Accession No. : 77 | MAPK Pathway No. : 335 | 0.0462963 | 0.3 | 4 | explicit E-S complex | Substrate MAPK-tyr Product MAPK* |
| Rate consts same as for MAPKKtyr. | ||||||||
MAPKK* acting as a Substrate for an Enzyme in Ajay_Bhalla_2004_PKM_MKP3_Tuning Network
| Enzyme Molecule / Enzyme Activity | Accession Name | Pathway Name | Km (uM) | kcat (s^-1) | Ratio | Enzyme Type | Reagents |
| PPhosphatase2A / MAPKK-deph | 2004_PKM_MKP3_ Tuning Accession No. : 77 | Ajay_Bhalla_ 2004_PKM_MKP3_ Tuning Pathway No. : 329 | 15.6568 | 6 | 4 | explicit E-S complex | Substrate MAPKK* Product MAPKK-ser |
| See: Kyriakis et al Nature 358 pp 417-421 1992 Ahn et al Curr Op Cell Biol 4:992-999 1992 for this pathway. See parent PPhosphatase2A for parms. | |||||||
MAPKK* acting as a Product of an Enzyme in Ajay_Bhalla_2004_PKM_MKP3_Tuning Network
| Enzyme Molecule / Enzyme Activity | Accession Name | Pathway Name | Km (uM) | kcat (s^-1) | Ratio | Enzyme Type | Reagents |
| Raf*-GTP-Ras / Raf*-GTP-Ras.2 | 2004_PKM_MKP3_ Tuning Accession No. : 77 | MAPK Pathway No. : 335 | 0.159094 | 0.3 | 4 | explicit E-S complex | Substrate MAPKK-ser Product MAPKK* |
| Same kinetics as other c-raf activated forms. See Force et al PNAS 91 1270-1274 1994. k1 = 1.1e-6, k2 = .42, k3 = 1.05 raise k1 to 5.5e-6 | |||||||
color.