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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 |
Accession and Pathway Details | |
MAPKK acting as a Molecule in 3d_fold_model Network
| Name | Accession Name | Pathway Name | Initial Conc.
(uM) | Volume
(fL) | Buffered | | MAPKK | 3d_fold_model
Accession No. : 8 | MAPK
Pathway No. : 56 | 0.18 | 1000 | No | | Conc is from Seger et al JBC 267:20 pp14373 (1992) mwt is 45/46 Kd We assume that phosphorylation on both ser and thr is needed for activiation. See Kyriakis et al Nature 358 417 1992 Init conc of total is 0.18 |
MAPKK acting as a Substrate for an Enzyme in 3d_fold_model Network
Enzyme Molecule /
Enzyme Activity | Accession Name | Pathway Name | Km (uM) | kcat (s^-1) | Ratio | Enzyme Type | Reagents | Raf-GTP-Ras* /
Raf-GTP-Ras*.1 | 3d_fold_model
Accession No. : 8 | MAPK
Pathway No. : 56 | 0.159091 | 0.105 | 4 | explicit E-S complex | Substrate
MAPKK
Product
MAPKK-ser
| | Kinetics are the same as for the craf-1* activity, ie., k1=1.1e-6, k2=.42, k3 =0.105 These are based on Force et al PNAS USA 91 1270-1274 1994. These parms cannot reach the observed 4X stim of MAPK. So lets increase the affinity, ie, raise k1 10X to 1.1e-5 Lets take it back down to where it was. Back up to 5X: 5.5e-6 |
MAPKK acting as a Product of an Enzyme in 3d_fold_model Network
| Database compilation and code copyright (C) 2022, Upinder S. Bhalla and NCBS/TIFR
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