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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

MAPKK 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	2	1	0	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.

MAPKK acting as a Molecule in  MAPK-bistability-fig1c Network

Name	Accession Name	Pathway Name	Initial Conc. (uM)	Volume (fL)	Buffered
MAPKK	MAPK-bistability -fig1c Accession No. : 35	MAPK Pathway No. : 182	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  MAPK-bistability-fig1c Network

	Enzyme Molecule / Enzyme Activity	Accession Name	Pathway Name	Km (uM)	kcat (s^-1)	Ratio	Enzyme Type	Reagents
1	RGR  / RGR.1	MAPK-bistability -fig1c Accession No. : 35	MAPK Pathway No. : 182	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=5.5e-6, k2=.42, k3 =0.105 These are based on Force et al PNAS USA 91 1270-1274 1994.
2	Raf*-GTP-Ras  / Raf*-GTP-Ras.1	MAPK-bistability -fig1c Accession No. : 35	MAPK Pathway No. : 182	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. They report Km for MAPKK of 0.8 uM. and a Vmax of ~500 fm/min/ug. These parms cannot reach the observed 4X stimulation of MAPK. So we increase the affinity, ie, raise k1 5x to 5.5e-6 which is equivalent to 5-fold reduction in Km to about 0.16. This is, of course, dependent on the amount of MAPKK present.

MAPKK 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  / MAPKK-deph-ser	MAPK-bistability -fig1c Accession No. : 35	Shared_Object_ MAPK-bistability -fig1c Pathway No. : 179	15.6566	6	4.16667	explicit E-S complex	Substrate MAPKK-ser Product MAPKK
See parent PPhostphatase2A description for rate details