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Molecule Parameter List for craf-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 |
Accession and Pathway Details | |
craf-1* acting as a Molecule in MAPK-bistability-fig1c Network
| Name | Accession Name | Pathway Name | Initial Conc.
(uM) | Volume
(fL) | Buffered | | craf-1* | MAPK-bistability
-fig1c
Accession No. : 35 | MAPK
Pathway No. : 182 | 0 | 1000 | No | | Singly phosphorylated form of c-raf-1. This is the form that gets best activated by GTP.Ras. |
craf-1* acting as a Substrate for an Enzyme in MAPK-bistability-fig1c Network
craf-1* acting as a Product of an Enzyme in MAPK-bistability-fig1c Network
| | Enzyme Molecule /
Enzyme Activity | Accession Name | Pathway Name | Km (uM) | kcat (s^-1) | Ratio | Enzyme Type | Reagents | | 1 | PKC-active /
PKC-act-raf | MAPK-bistability
-fig1c
Accession No. : 35 | Shared_Object_
MAPK-bistability
-fig1c
Pathway No. : 179 | 66.6667 | 4 | 4 | explicit E-S complex | Substrate
craf-1
Product
craf-1*
| | | Rate consts from Chen et al Biochem 32, 1032 (1993) k3 = 4 Km for this substrate is trickier. Specific substrates are in the uM range, so we use a higher Km here. This may be too conservative in which case PKC would have a still higher effect on raf. The presence of this phosphorylation and activation step is from Kolch et al 1993 Nature 364:249 | | 2 | PPhosphatase2A /
craf**-deph | MAPK-bistability
-fig1c
Accession No. : 35 | Shared_Object_
MAPK-bistability
-fig1c
Pathway No. : 179 | 15.6566 | 6 | 4.16667 | explicit E-S complex | Substrate
craf-1**
Product
craf-1*
| | | Ueki et al JBC 269(22) pp 15756-15761 1994 show hyperphosphorylation of craf, so this is there to dephosphorylate it. Identity of phosphatase is assumed to be PP2A. |
craf-1* acting as a Substrate in a reaction in MAPK-bistability-fig1c Network
| Kd is calculated only for second order reactions, like nA+nB <->nC or nA<->nC+nD, where n is number and A,B,C,D are molecules, where as for first order reactions Keq is calculated.
Kd for higher order reaction are not consider. |
| Name | Accession Name | Pathway Name | Kf | Kb | Kd | tau | Reagents | | Ras-act-craf | MAPK-bistability
-fig1c
Accession No. : 35 | Shared_Object_
MAPK-bistability
-fig1c
Pathway No. : 179 | 60
(uM^-1 s^-1) | 0.5
(s^-1) | Kd(bf) = 0.0083(uM) | - | Substrate
GTP-Ras
craf-1*
Product
Raf*-GTP-Ras
| | Assume binding is fast and limited only by available Ras*. So kf = kb/[craf-1] If kb is 1/sec, then kf = 1/0.2 uM = 1/(0.2 * 6e5) = 8.3e-6 Later: Raise it by 10 X to about 1e-4, giving a Kf of 60 for Kb of 0.5 and a tau of approx 2 sec. Based on: Hallberg et al JBC 269:6 3913-3916 1994, 3% of cellular Raf is complexed with Ras. This step needed to memb-anchor and activate Raf: Leevers et al Nature 369 411-414. Also see Koide et al 1993 PNAS USA 90(18):8683-8686 |
| Database compilation and code copyright (C) 2022, Upinder S. Bhalla and NCBS/TIFR
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