Enter a Search String

Special character and space not allowed in the query term. Search string should be at least 2 characters long.

Search in:

ALL Accession Pathway Molecule Enzyme Reaction Connected to

Search for

Match

Anything Exact Word Starting With

By

Name Notes Model

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

craf-1 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	0	1	1	1	0

Accession and Pathway Details

Accession Name	Accession No.	Accession Type	Pathway Link
MAPK-bistability -fig1c	35	Network	Shared_Object_MAPK-bistability-fig1c,  Sos,  PKC,   MAPK,  PLA2,  Ras,   PDGFR
Model for figure 1c in Bhalla US et al. Science (2002) 297(5583):1018-23. The demo for this figure is available here. This synaptic signaling model is without the MKP-1 feedback, so it is bistable and remains so over long periods.

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	0.2	1000	No
Strom et al 1990 Oncogene 5 pp 345-51 report high general expression in all tissues. Huang and Ferrell 1996 PNAS 93(19):10078 use a value of 3 nM for oocytes. Here we stick with a much higher expression based on the Strom report.

craf-1 acting as a Substrate for an Enzyme in  MAPK-bistability-fig1c Network

Enzyme Molecule / Enzyme Activity	Accession Name	Pathway Name	Km (uM)	kcat (s^-1)	Ratio	Enzyme Type	Reagents
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

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
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
See parent PPhosphatase2A for parms

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-unphosph -raf	MAPK-bistability -fig1c Accession No. : 35	Shared_Object_ MAPK-bistability -fig1c Pathway No. : 179	6 (uM^-1 s^-1)	1 (s^-1)	Kd(bf) = 0.1667(uM)	-	Substrate GTP-Ras craf-1 Product RGR
Based on rates of Ras-act-craf which has Kf=60, Kb= 0.5. This reaction was introduced to account for the PKC-independent activation of MAPK. This reac should have less affinity but similar tau as compared to the Ras-cat-craf, since the phosphorylated Raf form has a greater effect on MAPK.