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Molecule Parameter List for MAPKK*

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

MAPKK* 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	1	2	0	0

Accession and Pathway Details

Accession Name	Accession No.	Accession Type	Pathway Link
Ajay_Bhalla_ 2007_PKM	80	Network	Shared_Object_Ajay_Bhalla_2007_PKM, PKC, MAPK, Ras, CaM, PKM
This is a non-bistable model of ERKII signaling that also incorporates PKM synthesis triggered by Ca influx. It is a simplified variant of the model of Ajay SM, Bhalla US. Eur J Neurosci. 2004 Nov;20(10):2671-80.

MAPKK* acting as a Molecule in Ajay_Bhalla_2007_PKM Network

Name	Accession Name	Pathway Name	Initial Conc. (uM)	Volume (fL)	Buffered
MAPKK*	Ajay_Bhalla_ 2007_PKM Accession No. : 80	MAPK Pathway No. : 371	0	1.5	No
MAPKK phosphorylates MAPK on both the tyr and thr residues, first tyr then thr. Refs: Seger et al JBC267:20 pp 14373 1992 The MAPKK itself is phosphorylated on ser as well as thr residues. Let us assume that the ser goes first, and that the sequential phosphorylation is needed. See Kyriakis et al Nature 358 417-421 1992

MAPKK* acting as an Enzyme in Ajay_Bhalla_2007_PKM Network

	Enzyme Molecule / Enzyme Activity	Accession Name	Pathway Name	Km (uM)	kcat (s^-1)	Ratio	Enzyme Type	Reagents
1	MAPKK* / MAPKKtyr	Ajay_Bhalla_ 2007_PKM Accession No. : 80	MAPK Pathway No. : 371	0.0462968	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	MAPKK* / MAPKKthr	Ajay_Bhalla_ 2007_PKM Accession No. : 80	MAPK Pathway No. : 371	0.0462968	0.3	4	explicit E-S complex	Substrate MAPK-tyr Product MAPK*
	Rate consts same as for MAPKKtyr.

MAPKK* acting as a Substrate for an Enzyme in Ajay_Bhalla_2007_PKM Network

Enzyme Molecule / Enzyme Activity	Accession Name	Pathway Name	Km (uM)	kcat (s^-1)	Ratio	Enzyme Type	Reagents
PPhosphatase2A / MAPKK-deph	Ajay_Bhalla_ 2007_PKM Accession No. : 80	Shared_Object_ Ajay_Bhalla_ 2007_PKM Pathway No. : 369	15.6566	6	4	explicit E-S complex	Substrate MAPKK* Product MAPKK-ser
See: Kyriakis et al Nature 358 pp 417-421 1992 Ahn et al Curr Op Cell Biol 4:992-999 1992 for this pathway. See parent PPhosphatase2A for parms.

MAPKK* acting as a Product of an Enzyme in Ajay_Bhalla_2007_PKM Network

	Enzyme Molecule / Enzyme Activity	Accession Name	Pathway Name	Km (uM)	kcat (s^-1)	Ratio	Enzyme Type	Reagents
1	Raf-GTP-Ras / Raf-GTP-Ras.2	Ajay_Bhalla_ 2007_PKM Accession No. : 80	MAPK Pathway No. : 371	0.159096	0.3	4	explicit E-S complex	Substrate MAPKK-ser Product MAPKK*
	Kinetics are the same as for the craf_1* activity, ie., k1=5.5e-6, k2=0.42, k3 = 0.105 These are basedo n Force et al PNAS USA 91 1270-1274, 1994., but k1 is scaled up 5x (ie., Km is scaled down 5x to the value used here and for craf_1* activity: Km = 0.1591).
2	Raf-GTP-Ras / Raf-GTP-Ras.2	Ajay_Bhalla_ 2007_PKM Accession No. : 80	MAPK Pathway No. : 371	0.159096	0.3	4	explicit E-S complex	Substrate MAPKK-ser Product MAPKK*
	Same kinetics as other c-raf activated forms. See Force et al PNAS 91 1270-1274 1994. k1 = 1.1e-6, k2 = .42, k3 = 1.05 raise k1 to 5.5e-6

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