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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
Synaptic_ Network	16	Network	Shared_Object_Synaptic_Network,  PKC,  PLA2,   PLCbeta,  Gq,  MAPK,   Ras,  EGFR,  Sos,   PLC_g,  CaMKII,  CaM,   PP1,  PP2B,  PKA,   AC,  CaRegulation
This model is an annotated version of the synaptic signaling network. The primary reference is Bhalla US and Iyengar R. Science (1999) 283(5400):381-7 but several of the model pathways have been updated. Bhalla US Biophys J. 2002 Aug;83(2):740-52 Bhalla US J Comput Neurosci. 2002 Jul-Aug;13(1):49-62

MKP-1 acting as a Molecule in  Synaptic_Network Network

Name	Accession Name	Pathway Name	Initial Conc. (uM)	Volume (fL)	Buffered
MKP-1	Synaptic_ Network Accession No. : 16	Shared_Object_ Synaptic_ Network Pathway No. : 70	0.0032	1000	No
MKP-1 dephosphorylates and inactivates MAPK in vivo: Sun et al Cell 75 487-493 1993. See Charles et al PNAS 90:5292-5296 1993 and Charles et al Oncogene 7 187-190 for half-life of MKP1/3CH is 40 min. 80% deph of MAPK in 20 min The protein is 40 KDa. The levels are MKP-1 are highly variable, as it is induced depending on MAPK activity. This selected value is well below its induced peak, but sufficiently high so that MAPK will not go into a runaway activation state.

MKP-1 acting as an Enzyme in  Synaptic_Network Network

	Enzyme Molecule / Enzyme Activity	Accession Name	Pathway Name	Km (uM)	kcat (s^-1)	Ratio	Enzyme Type	Reagents
1	MKP-1 / MKP1-tyr-deph	Synaptic_ Network Accession No. : 16	Shared_Object_ Synaptic_ Network Pathway No. : 70	0.0666667	1	4	explicit E-S complex	Substrate MAPK-tyr Product MAPK
	The original kinetics from Bhalla and Iyengar Science 1999 have now been modified to obey the k2 = 4 * k3 rule, while keeping kcat and Km fixed. The main constraining data point is the time course of MAPK dephosphorylation, which this model satisfies. See Charles et al 1993 PNAS 90:5292-5296 and Charles et al Oncogene 7:187-190 Effective Km : 67 nM kcat = 1.43 umol/min/mg
2	MKP-1 / MKP1-thr-deph	Synaptic_ Network Accession No. : 16	Shared_Object_ Synaptic_ Network Pathway No. : 70	0.0666667	1	4	explicit E-S complex	Substrate MAPK* Product MAPK-tyr
	See MKP1-tyr-deph