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Molecule Parameter List for MKP-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

MKP-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	1	2	0	1	2	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-1** acting as a Molecule in mkp1_feedback_effects Network

Name	Accession Name	Pathway Name	Initial Conc. (uM)	Volume (fL)	Buffered
MKP-1**	mkp1_feedback_ effects Accession No. : 4	MAPK Pathway No. : 35	0	1000	No
Same enzyme activity as MKP-1, but different degradation rates. Brondello et al Science 286:2514 1999 This form is doubly phosphorylated.

MKP-1** acting as a Summed Molecule in mkp1_feedback_effects Network

Accession Name	Pathway Name	Target	Input
mkp1_feedback_ effects Accession No. : 4	Shared_Object_ mkp1_feedback_ effects Pathway No. : 32	tot_MKP1	MKP-1 MKP-1-ser359* MKP-1**
Total available active MKP-1. This sums the levels of the non-phosphorylated, singly phosphorylated and doubly phosphorylated forms. It is used primarily for graphing the total MKP-1 level.

MKP-1** 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-1** / MKP1*-tyr-deph	mkp1_feedback_ effects Accession No. : 4	MAPK Pathway No. : 35	0.0666667	1	4	Classical Michaelis-Menten V = Etot.S.Kcat/Km+S	Substrate MAPK-tyr Product MAPK
	3 Feb 2000. Same rates as MKP-1.
2	MKP-1** / MKP1*-thr-deph	mkp1_feedback_ effects Accession No. : 4	MAPK Pathway No. : 35	0.0666667	1	4	Classical Michaelis-Menten V = Etot.S.Kcat/Km+S	Substrate MAPK* Product MAPK-tyr
	3 Feb 2000. Same rates as MKP1

MKP-1** acting as a Product of an Enzyme in mkp1_feedback_effects Network

Enzyme Molecule / Enzyme Activity	Accession Name	Pathway Name	Km (uM)	kcat (s^-1)	Ratio	Enzyme Type	Reagents
MAPK* / MKP-1-phosph2	mkp1_feedback_ effects Accession No. : 4	Shared_Object_ mkp1_feedback_ effects Pathway No. : 32	25.641	1	4	explicit E-S complex	Substrate MKP-1-ser359* Product MKP-1**
3 Feb 2000. MAPK rates based on Sanghera JS, Paddon HB, Bader SA, Pelech SL. (1990) 265(1):52-57. The Vmax is scaled down 10 fold to match the time-course of phosph by MAPK, from Brondello JM, Pouyssegur J, McKenzie FR. (1999) Science 286(5449):2514-2517.

MKP-1** acting as a Substrate in a reaction in mkp1_feedback_effects 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
1	turnover_MKP1**	mkp1_feedback_ effects Accession No. : 4	MAPK Pathway No. : 35	0.0001 (s^-1)	0 (s^-1)	-	-	Substrate MKP-1 Product** Ubiquitination
	Rate of turnover of phosph form of MKP1 is from Brondello et al Science 286:2514 1999. Tau is about 150 min though it is not a clean exponential falloff.
2	MKP-1**dephosph	mkp1_feedback_ effects Accession No. : 4	MAPK Pathway No. : 35	0.0001 (s^-1)	0 (s^-1)	-	-	Substrate MKP-1 Product** MKP-1-ser359*
	24 Apr 2K, based on 12 Feb 2K: Scaled up 10x to kf=0.01, kb=0 13 Apr 2001. Slowing down to 0.0001 to match turnover rates.

Database compilation and code copyright (C) 2022, Upinder S. Bhalla and NCBS/TIFR
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