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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
mkp1_feedback_ effects	4	Network	Shared_Object_mkp1_feedback_effects,  Sos,  PKC,   MAPK,  PLA2,  Ras,   PDGFR
This is a network involving the MAPK-PKC feedback loop with input from the PDGFR in the synapse. The distinctive feature of this model is that it includes MKP-1 induction by MAPK, and the consequent inhibitory regulation of MAPK and the feedback loop. Lots of interesting dynamics arise from this. This link provides supplementary material for the paper Bhalla US et al. Science (2002) 297(5583):1018-23. In the form of several example simulations and demos for the figures in the paper.

MKP-2 acting as a Molecule in  mkp1_feedback_effects Network

Name	Accession Name	Pathway Name	Initial Conc. (uM)	Volume (fL)	Buffered
MKP-2	mkp1_feedback_ effects Accession No. : 4	Shared_Object_ mkp1_feedback_ effects Pathway No. : 32	0.002	1000	No
MKP2 is modeled to act as a relatively steady, unregulated phosphatase for controlling MAPK activity. From Brondello JM, Brunet A, Pouyssegur J, McKenzie FR (1997) J Biol Chem. 272(2):1368-1376, 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 Y, Solski PA, Khosravi-Far R, Der CJ, Kelly K (1996) J Biol Chem. 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.

MKP-2 acting as an Enzyme in  mkp1_feedback_effects Network

	Enzyme Molecule / Enzyme Activity	Accession Name	Pathway Name	Km (uM)	kcat (s^-1)	Ratio	Enzyme Type	Reagents
1	MKP-2 / MKP2-tyr-deph	mkp1_feedback_ effects Accession No. : 4	Shared_Object_ mkp1_feedback_ effects Pathway No. : 32	0.0666667	1	4	explicit E-S complex	Substrate MAPK-tyr Product MAPK
	22 Apr 2001: Based on MKP1 parameters. 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 Y, Solski PA, Khosravi-Far R, Der CJ, Kelly K. (1996) J Biol Chem. 271(11):6497-6501.
2	MKP-2 / MKP2-thr-deph	mkp1_feedback_ effects Accession No. : 4	Shared_Object_ mkp1_feedback_ effects Pathway No. : 32	0.0666667	1	4	explicit E-S complex	Substrate MAPK* Product MAPK-tyr
	See MKP2-tyr-deph