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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	3	3	0	0

Accession and Pathway Details

Accession Name	Accession No.	Accession Type	Pathway Link
MAPK_MKP1_ oscillation	9	Network	Shared_Object_MAPK_MKP1_oscillation, PKC, MAPK, PLA2, Ras
This model relates to figure 5 in Bhalla US, Iyengar R. Chaos (2001) 11(1):221-226. It includes the model used for figures 2-4 and also has MKP-1 induction by MAPK activity in the synapse. PP2A is set to 0.16 uM and MKP synthesis is varied from 5x to 40 x basal to get a range of interesting behaviours.

MAPK-tyr acting as a Molecule in MAPK_MKP1_oscillation Network

Name	Accession Name	Pathway Name	Initial Conc. (uM)	Volume (fL)	Buffered
MAPK-tyr	MAPK_MKP1_ oscillation Accession No. : 9	MAPK Pathway No. : 61	0	1000	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 MAPK_MKP1_oscillation Network

	Enzyme Molecule / Enzyme Activity	Accession Name	Pathway Name	Km (uM)	kcat (s^-1)	Ratio	Enzyme Type	Reagents
1	MAPKK* / MAPKKthr	MAPK_MKP1_ oscillation Accession No. : 9	MAPK Pathway No. : 61	0.0462963	0.15	4	explicit E-S complex	Substrate MAPK-tyr Product MAPK*
	Rate consts same as for MAPKKtyr.
2	MKP-1** / MKP1*-tyr-deph	MAPK_MKP1_ oscillation Accession No. : 9	MAPK Pathway No. : 61	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.
3	MKP-1 / MKP1-tyr-deph	MAPK_MKP1_ oscillation Accession No. : 9	Shared_Object_ MAPK_MKP1_ oscillation Pathway No. : 59	0.0666667	1	4	Classical Michaelis-Menten V = Etot.S.Kcat/Km+S	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

MAPK-tyr acting as a Product of an Enzyme in MAPK_MKP1_oscillation Network

	Enzyme Molecule / Enzyme Activity	Accession Name	Pathway Name	Km (uM)	kcat (s^-1)	Ratio	Enzyme Type	Reagents
1	MAPKK* / MAPKKtyr	MAPK_MKP1_ oscillation Accession No. : 9	MAPK Pathway No. : 61	0.0462963	0.15	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-1** / MKP1*-thr-deph	MAPK_MKP1_ oscillation Accession No. : 9	MAPK Pathway No. : 61	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
3	MKP-1 / MKP1-thr-deph	MAPK_MKP1_ oscillation Accession No. : 9	Shared_Object_ MAPK_MKP1_ oscillation Pathway No. : 59	0.0666667	1	4	Classical Michaelis-Menten V = Etot.S.Kcat/Km+S	Substrate MAPK* Product MAPK-tyr
	See MKP1-tyr-deph

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