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Molecule Parameter List for MAPK-tyr

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

MAPK-tyr 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	2	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.

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

Name	Accession Name	Pathway Name	Initial Conc. (uM)	Volume (fL)	Buffered
MAPK-tyr	MAPK-bistability -fig1c Accession No. : 35	MAPK Pathway No. : 182	0	1000	No
Haystead et al FEBS Lett. 306(1) pp 17-22 show that phosphorylation is strictly sequential, first tyr185 then thr183.

MAPK-tyr 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	MAPKK*  / MAPKKthr	MAPK-bistability -fig1c Accession No. : 35	MAPK Pathway No. : 182	0.0462963	0.15	4	explicit E-S complex	Substrate MAPK-tyr Product MAPK*
	Rate consts same as for MAPKKtyr.
2	MKP-2  / MKP2-tyr-deph	MAPK-bistability -fig1c Accession No. : 35	Shared_Object_ MAPK-bistability -fig1c Pathway No. : 179	0.0666667	1	4	explicit E-S complex	Substrate MAPK-tyr Product MAPK
	22 Apr 2001: Based on MKP1 parms. The original kinetics have been modified to obey the k2 = 4 * k3 rule, while keeping kcat and Km fixed. The only constraining data point is the time course of MAPK dephosphorylation, which this model satisfies. The rates are treated as the same as for MKP-1, based on Chu et al 1995 JBC 271(11):6497-6501

MAPK-tyr 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	MAPKK*  / MAPKKtyr	MAPK-bistability -fig1c Accession No. : 35	MAPK Pathway No. : 182	0.0462963	0.15	4	explicit E-S complex	Substrate MAPK Product MAPK-tyr
	The actual MAPKK is 2 forms from Seger et al JBC 267:20 14373(1992) Vmax = 150nmol/min/mg From Haystead et al FEBS 306(1):17-22 we get Km=46.6nM for at least one of the phosphs. Putting these together: k3=0.15/sec, ratio of 4 to get k2=0.6. k1=0.75/46.6nM=2.7e-5 In terms of Michaelis-Menten rates, Km = 0.046, Vmax = 0.15, ratio = 4.
2	MKP-2  / MKP2-thr-deph	MAPK-bistability -fig1c Accession No. : 35	Shared_Object_ MAPK-bistability -fig1c Pathway No. : 179	0.0666667	1	4	explicit E-S complex	Substrate MAPK* Product MAPK-tyr
	See MKP2-tyr-deph