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Molecule Parameter List for MKP-2

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

MKP-2 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	2	0	0	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.

MKP-2 acting as a Molecule in  MAPK-bistability-fig1c Network

Name	Accession Name	Pathway Name	Initial Conc. (uM)	Volume (fL)	Buffered
MKP-2	MAPK-bistability -fig1c Accession No. : 35	Shared_Object_ MAPK-bistability -fig1c Pathway No. : 179	0.0024	1000	No
MKP2 is modeled to act as a relatively steady, unregulated phosphatase for controlling MAPK activity. From Brondello et al JBC 272(2):1368-1376 (1997), the blockage of MKP-1 induction increases MAPK activity by no more than 2x. So this phosphatase will play the steady role and the fully stimulated MKP-1 can come up to the level of this steady level. From Chu et al 1995 JBC 271(11):6497-6501 it looks like both MKP-1 and MKP-2 have similar activities in dephosphorylating ERK2. So I use the same enzymatic rates for both. 31 Jan 2002: For the purposes of making a bistable model without the complications of MKP-1 induction, I simply set the initial conc of MKP-2 up by 0.0004 uM which was the starting level of MKP-1.

MKP-2 acting as 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	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
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