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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	0	2	0	0	0	0

Accession and Pathway Details

Accession Name	Accession No.	Accession Type	Pathway Link
Ajay_Bhalla_ 2007_Bistable	79	Network	Shared_Object_Ajay_Bhalla_2007_Bistable,  PKC,  PLA2,   MAPK,  Ras,  CaM
This is a model of ERKII signaling which is bistable due to feedback. The feedback occurs through ERKII phosphorylation of phospholipase A2 (PLA2), leading to increased production of arachidonic acid (AA), which activates protein kinase C (PKC) which activates c-Raf which is upstream of ERKII. The model is a highly simplified variant of more detailed bistable models of MAPK signaling (Bhalla US, Iyengar R. Science. 1999 Jan 15;283(5400):381-7, Ajay SM, Bhalla US. Eur J Neurosci. 2004 Nov;20(10):2671-80)

MKP-1 acting as a Molecule in  Ajay_Bhalla_2007_Bistable Network

Name	Accession Name	Pathway Name	Initial Conc. (uM)	Volume (fL)	Buffered
MKP-1	Ajay_Bhalla_ 2007_Bistable Accession No. : 79	Shared_Object_ Ajay_Bhalla_ 2007_Bistable Pathway No. : 363	0.024	125.7	No
MKP-1 dephosphoryates and inactivates MAPK in vivo: Sun et al Cell 75 487-493 1993. Levels of MKP-1 are regulated, and rise in 1 hour. Kinetics from Charles et al PNAS 90:5292-5296 1993. They refer to Charles et al Oncogene 7 187-190 who show that half-life of MKP1/3CH134 is 40 min. 80% deph of MAPK in 20 min Sep 17 1997: CoInit now 0.4x to 0.0032. See parm searches from jun96 on.

MKP-1 acting as an Enzyme in  Ajay_Bhalla_2007_Bistable Network

	Enzyme Molecule / Enzyme Activity	Accession Name	Pathway Name	Km (uM)	kcat (s^-1)	Ratio	Enzyme Type	Reagents
1	MKP-1 / MKP1-tyr-deph	Ajay_Bhalla_ 2007_Bistable Accession No. : 79	Shared_Object_ Ajay_Bhalla_ 2007_Bistable Pathway No. : 363	0.133331	4	4	explicit E-S complex	Substrate MAPK-tyr Product MAPK
	The original kinetics have been modified to obey the k2 = 4 * k3 rule, while keeping kcat and Km fixed. As noted in the NOTES, the only constraining data point is the time course of MAPK dephosphorylation, which this model satisfies. It would be nice to have more accurate estimates of rate consts and MKP-1 levels from the literature. Effective Km : 67 nM kcat = 1.43 umol/min/mg
2	MKP-1 / MKP1-thr-deph	Ajay_Bhalla_ 2007_Bistable Accession No. : 79	Shared_Object_ Ajay_Bhalla_ 2007_Bistable Pathway No. : 363	0.133331	4	4	explicit E-S complex	Substrate MAPK* Product MAPK-tyr
	See MKP1-tyr-deph