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Molecule Parameter List for MKKK-P | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| 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 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| MKKK-P 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 |
| MAPK_osc | 27 | Pathway | MAPK |
| This MAPK model is based on Boris N. Kholodenko Eur J Biochem. (2000) 267(6):1583-8 for data from Xenopus oocytes extracts. | |||
MKKK-P acting as a Molecule in MAPK_osc Network
| Name | Accession Name | Pathway Name | Initial Conc. (uM) | Volume (fL) | Buffered | |
| MKKK-P | MAPK_osc Accession No. : 27 | MAPK Pathway No. : 139 | 0 | 0.0016667 | No | |
| This is the phosphorylated form of MKKK which converts MKK to MKK-P and then to MKK-PP from Kholodenko, 2000. | ||||||
MKKK-P acting as an Enzyme in MAPK_osc Network
| Enzyme Molecule / Enzyme Activity | Accession Name | Pathway Name | Km (uM) | kcat (s^-1) | Ratio | Enzyme Type | Reagents | |
| 1 | MKKK-P / 3 | MAPK_osc Accession No. : 27 | MAPK Pathway No. : 139 | 0.0150001 | 0.025 | 4 | Classical Michaelis-Menten V = Etot.S.Kcat/Km+S | Substrate MKK Product MKK-P |
| Km is 15 nM and Vmax is 0.025s-1 from Kholodenko, 2000 | ||||||||
| 2 | MKKK-P / 4 | MAPK_osc Accession No. : 27 | MAPK Pathway No. : 139 | 0.0150001 | 0.025 | 4 | Classical Michaelis-Menten V = Etot.S.Kcat/Km+S | Substrate MKK-P Product MKK-PP |
| Km is 15nM and Vmax is 0.025s-1 from Kholodenko, 2000. | ||||||||
MKKK-P acting as a Substrate for an Enzyme in MAPK_osc Network
| Enzyme Molecule / Enzyme Activity | Accession Name | Pathway Name | Km (uM) | kcat (s^-1) | Ratio | Enzyme Type | Reagents |
| int1 / 2 | MAPK_osc Accession No. : 27 | MAPK Pathway No. : 139 | 0.008 | 0.25 | 4 | Classical Michaelis-Menten V = Etot.S.Kcat/Km+S | Substrate MKKK-P Product MKKK |
| Km is 8nM and Vmax is 0.25nM.s-1 from Kholodenko, 2000. | |||||||
MKKK-P acting as a Product of an Enzyme in MAPK_osc Network
| Enzyme Molecule / Enzyme Activity | Accession Name | Pathway Name | Km (uM) | kcat (s^-1) | Ratio | Enzyme Type | Reagents |
| Ras-MKKKK / 1 | MAPK_osc Accession No. : 27 | MAPK Pathway No. : 139 | 0.01 | 2.5 | 4 | Classical Michaelis-Menten V = Etot.S.Kcat/Km+S | Substrate MKKK Product MKKK-P |
| The Km is 10nM and Vmax is 2.5nM sec^-1. We assume that there is 1 nM of the Ras-MKKKK. From Kholodenko, 2000. If the enzymes are not flagged as Available, then this Km should be set to 0.1 to obtain oscillations. | |||||||
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