Enter a Search String |
| Special character and space not allowed in the query term. Search string should be at least 2 characters long. |
Molecule Parameter List for MAPKK_star | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| 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_star 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 |
| mTOR_pathway | 92 | Network | Shared_Object_mTOR_pathway, AKT_mod, S6Kinase, PI3K_mod, TrKB_mod, mTOR_model, MAPK, PKC, 4E-BP_mod, Ras, Sos, 43S_complex, CaM |
| This model consists of various sub-modules. They are as follows: 1) BDNF receptor signaling 2) AKT signaling 3) 4E-BP model 4) S6 Kinase model 5) CaMKIII model 6) Protein synthesis model 7) CaM 8) PKC 9) MAPK model. | |||
MAPKK_star acting as a Molecule in mTOR_pathway Network
| Name | Accession Name | Pathway Name | Initial Conc. (uM) | Volume (fL) | Buffered | |
| MAPKK_star | mTOR_pathway Accession No. : 92 | MAPK Pathway No. : 1103 | 0 | 1000 | 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_star acting as an Enzyme in mTOR_pathway Network
| Enzyme Molecule / Enzyme Activity | Accession Name | Pathway Name | Km (uM) | kcat (s^-1) | Ratio | Enzyme Type | Reagents | |
| 1 | MAPKK_star / MAPKKtyr | mTOR_pathway Accession No. : 92 | MAPK Pathway No. : 1103 | 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_star / MAPKKthr | mTOR_pathway Accession No. : 92 | MAPK Pathway No. : 1103 | 0.0462963 | 0.3 | 4 | explicit E-S complex | Substrate MAPK-tyr Product MAPK_star |
| Rate consts same as for MAPKKtyr. | ||||||||
MAPKK_star acting as a Substrate for an Enzyme in mTOR_pathway Network
| Enzyme Molecule / Enzyme Activity | Accession Name | Pathway Name | Km (uM) | kcat (s^-1) | Ratio | Enzyme Type | Reagents |
| PPhosphatase2A / MAPKK-deph | mTOR_pathway Accession No. : 92 | mTOR_pathway Pathway No. : 1097 | 15.6568 | 6 | 4 | explicit E-S complex | Substrate MAPKK_star 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_star acting as a Product of an Enzyme in mTOR_pathway Network
| Enzyme Molecule / Enzyme Activity | Accession Name | Pathway Name | Km (uM) | kcat (s^-1) | Ratio | Enzyme Type | Reagents |
star-GTP-Ras / star-GTP-Ras.2 | mTOR_pathway Accession No. : 92 | MAPK Pathway No. : 1103 | 0.159094 | 0.3 | 4 | explicit E-S complex | Substrate MAPKK-ser Product MAPKK_star |
| 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.