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Name Notes Model

Molecule Parameter List for MAPK_dash_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_dash_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
Differential syn thesis of mRNA	95	Network	kinetics,  compartment_1,  compartment_2
The model consists of three major pathways: Calcium-calmodulin dependent protein kinase IV (CaMKIV), Mitogen-activated protein kinase (MAPK) and Protein Phosphatase 1 (PP1). Each of these converged on CREB activation. We also modeled further interactions with Transducer of regulated CREB activity 1 (TORC1) and the protein kinase A (PKA) pathway.

MAPK_dash_tyr acting as a Molecule in  Differential synthesis of mRNA Network

Name	Accession Name	Pathway Name	Initial Conc. (uM)	Volume (fL)	Buffered
MAPK_dash_tyr	Differential syn thesis of mRNA Accession No. : 95	kinetics Pathway No. : 1115	0	1000	No
Haystead et al FEBS Lett. 306(1) pp 17-22 show that phosphorylation is strictly sequential, first tyr185 then thr183.

MAPK_dash_tyr acting as a Substrate for an Enzyme in  Differential synthesis of mRNA Network

	Enzyme Molecule / Enzyme Activity	Accession Name	Pathway Name	Km (uM)	kcat (s^-1)	Ratio	Enzyme Type	Reagents
1	MAPKK_star  / MAPKKthr	Differential syn thesis of mRNA Accession No. : 95	kinetics Pathway No. : 1115	0.0463	0.3	4	explicit E-S complex	Substrate MAPK_dash_tyr Product MAPK_star
	Rate consts same as for MAPKKtyr.
2	MKP_dash_1  / MKP1_dash_tyr_ dash_deph	Differential syn thesis of mRNA Accession No. : 95	kinetics Pathway No. : 1115	0.1333	4	4	explicit E-S complex	Substrate MAPK_dash_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

MAPK_dash_tyr acting as a Product of an Enzyme in  Differential synthesis of mRNA Network

	Enzyme Molecule / Enzyme Activity	Accession Name	Pathway Name	Km (uM)	kcat (s^-1)	Ratio	Enzyme Type	Reagents
1	MAPKK_star  / MAPKKtyr	Differential syn thesis of mRNA Accession No. : 95	kinetics Pathway No. : 1115	0.0463	0.3	4	explicit E-S complex	Substrate MAPK Product MAPK_dash_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_dash_1  / MKP1_dash_thr_ dash_deph	Differential syn thesis of mRNA Accession No. : 95	kinetics Pathway No. : 1115	0.1333	4	4	explicit E-S complex	Substrate MAPK_star Product MAPK_dash_tyr
	See MKP1-tyr-deph