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Molecule Parameter List for MAPK

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* 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	1	1	0	0

Accession and Pathway Details

Accession Name	Accession No.	Accession Type	Pathway Link
EGFR_MAPK	58	Network	Shared_Object_EGFR_MAPK, MAPK, Ras, EGFR, Sos
Model of MAPK activation by EGFR in the synapse. Demonstration programs using this model are available here. Primary citation:Bhalla US. Biophys J. (2004) 87(2):745-53.

MAPK acting as a Molecule in EGFR_MAPK Network

Name	Accession Name	Pathway Name	Initial Conc. (uM)	Volume (fL)	Buffered
MAPK	EGFR_MAPK Accession No. : 58	MAPK Pathway No. : 230	0.36	1000	No
conc is from Sanghera et al JBC 265 pp 52 (1990) A second calculation gives 3.1 uM, from same paper. They est MAPK is 1e-4x total protein, and protein is 15% of cell wt, so MAPK is 1.5e-5g/ml = 0.36uM. which is closer to our first estimate. Lets use this.

MAPK acting as a Substrate for an Enzyme in EGFR_MAPK Network

Enzyme Molecule / Enzyme Activity	Accession Name	Pathway Name	Km (uM)	kcat (s^-1)	Ratio	Enzyme Type	Reagents
MAPKK* / MAPKKtyr	EGFR_MAPK Accession No. : 58	MAPK Pathway No. : 230	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

MAPK acting as a Product of an Enzyme in EGFR_MAPK Network

Enzyme Molecule / Enzyme Activity	Accession Name	Pathway Name	Km (uM)	kcat (s^-1)	Ratio	Enzyme Type	Reagents
MKP-1 / MKP1-tyr-deph	EGFR_MAPK Accession No. : 58	Shared_Object_ EGFR_MAPK Pathway No. : 229	0.0666667	1	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

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