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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
MAPK-bistability -fig1c	35	Network	Shared_Object_MAPK-bistability-fig1c, Sos, PKC, MAPK, PLA2, Ras, PDGFR
Model for figure 1c in Bhalla US et al. Science (2002) 297(5583):1018-23. The demo for this figure is available here. This synaptic signaling model is without the MKP-1 feedback, so it is bistable and remains so over long periods.

MAPKK* acting as a Molecule in MAPK-bistability-fig1c Network

Name	Accession Name	Pathway Name	Initial Conc. (uM)	Volume (fL)	Buffered
MAPKK*	MAPK-bistability -fig1c Accession No. : 35	MAPK Pathway No. : 182	0	1000	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 MAPK-bistability-fig1c Network

	Enzyme Molecule / Enzyme Activity	Accession Name	Pathway Name	Km (uM)	kcat (s^-1)	Ratio	Enzyme Type	Reagents
1	MAPKK* / MAPKKtyr	MAPK-bistability -fig1c Accession No. : 35	MAPK Pathway No. : 182	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, ratio of 4 to get k2=0.6. k1=0.75/46.6nM=2.7e-5 In terms of Michaelis-Menten rates, Km = 0.046, Vmax = 0.15, ratio = 4.
2	MAPKK* / MAPKKthr	MAPK-bistability -fig1c Accession No. : 35	MAPK Pathway No. : 182	0.0462963	0.15	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 MAPK-bistability-fig1c Network

Enzyme Molecule / Enzyme Activity	Accession Name	Pathway Name	Km (uM)	kcat (s^-1)	Ratio	Enzyme Type	Reagents
PPhosphatase2A / MAPKK-deph	MAPK-bistability -fig1c Accession No. : 35	Shared_Object_ MAPK-bistability -fig1c Pathway No. : 179	15.6566	6	4.16667	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 MAPK-bistability-fig1c Network

	Enzyme Molecule / Enzyme Activity	Accession Name	Pathway Name	Km (uM)	kcat (s^-1)	Ratio	Enzyme Type	Reagents
1	RGR / RGR.2	MAPK-bistability -fig1c Accession No. : 35	MAPK Pathway No. : 182	0.159091	0.105	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 = 5.5e-6, k2 = .42, k3 = 0.105
2	Raf-GTP-Ras / Raf-GTP-Ras.2	MAPK-bistability -fig1c Accession No. : 35	MAPK Pathway No. : 182	0.159091	0.105	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.

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