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Molecule Parameter List for MAPK-tyr

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

MAPK-tyr 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	0	2	2	0	0

Accession and Pathway Details

Accession Name	Accession No.	Accession Type	Pathway Link
Ajay_Bhalla_ 2004_PKM_MKP3_ Tuning	77	Network	Shared_Object_Ajay_Bhalla_2004_PKM_MKP3_Tuning,  PKC,  PLA2,   PLCbeta,  Ras,  Gq,   MAPK,  EGFR,  Sos,   PLC_g,  CaMKII,  CaM,   PP1,  PP2B,  PKA,   AC,  MKP3,  PKM
This model is based on Ajay SM, Bhalla US. Eur J Neurosci. 2004 Nov;20(10):2671-80. This is the feedforward model with MPK3 from figure 8a.

MAPK-tyr acting as a Molecule in  Ajay_Bhalla_2004_PKM_MKP3_Tuning Network

Name	Accession Name	Pathway Name	Initial Conc. (uM)	Volume (fL)	Buffered
MAPK-tyr	Ajay_Bhalla_ 2004_PKM_MKP3_ Tuning Accession No. : 77	MAPK Pathway No. : 335	0	1.5	No
Haystead et al FEBS Lett. 306(1) pp 17-22 show that phosphorylation is strictly sequential, first tyr185 then thr183.

MAPK-tyr acting as a Substrate for an Enzyme in  Ajay_Bhalla_2004_PKM_MKP3_Tuning Network

	Enzyme Molecule / Enzyme Activity	Accession Name	Pathway Name	Km (uM)	kcat (s^-1)	Ratio	Enzyme Type	Reagents
1	MAPKK*  / MAPKKthr	Ajay_Bhalla_ 2004_PKM_MKP3_ Tuning Accession No. : 77	MAPK Pathway No. : 335	0.0462963	0.3	4	explicit E-S complex	Substrate MAPK-tyr Product MAPK*
	Rate consts same as for MAPKKtyr.
2	MKP-3  / MKP3-tyr-deph	Ajay_Bhalla_ 2004_PKM_MKP3_ Tuning Accession No. : 77	MKP3 Pathway No. : 345	10.0001	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 Km for MKP3 is set to 267 nM, twice as high as MKP1 version, to lessen substrate saturation.

MAPK-tyr acting as a Product of an Enzyme in  Ajay_Bhalla_2004_PKM_MKP3_Tuning Network

	Enzyme Molecule / Enzyme Activity	Accession Name	Pathway Name	Km (uM)	kcat (s^-1)	Ratio	Enzyme Type	Reagents
1	MAPKK*  / MAPKKtyr	Ajay_Bhalla_ 2004_PKM_MKP3_ Tuning Accession No. : 77	MAPK Pathway No. : 335	0.0462963	0.3	4	explicit E-S complex	Substrate MAPK Product MAPK-tyr
	The actual MAPKK is 2 forms from Seger et al JBC 267:20 14373(1992) Vmax = 150nmol/min/mg From Haystead et al FEBS 306(1):17-22 we get Km=46.6nM for at least one of the phosphs. Putting these together: k3=0.15/sec, scale to get k2=0.6. k1=0.75/46.6nM=2.7e-5
2	MKP-3  / MKP3-thr-deph	Ajay_Bhalla_ 2004_PKM_MKP3_ Tuning Accession No. : 77	MKP3 Pathway No. : 345	10.0001	4	4	explicit E-S complex	Substrate MAPK* Product MAPK-tyr
	See MKP1-tyr-deph Km is twice as high to avoid saturation.