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Enzyme List for pathway MAPK (Pathway Number 61)

 Molecule Name/
Site Name 		Km (uM) kcat (1/s)Ratio
(k2/k3)		Enzyme TypeSubstrate Product
1 Enzyme Activity:
MAPKKthr

Enzyme Molecule:
MAPKK*		0.04630.154explicit E-S complexMAPK-tyr
MAPK*
  Rate consts same as for MAPKKtyr.
2 Enzyme Activity:
MAPKKtyr

Enzyme Molecule:
MAPKK*		0.04630.154explicit E-S complexMAPK
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
3 Enzyme Activity:
MKP-1-synthesis

Enzyme Molecule:
nuc_MAPK*		27.36320.000110explicit E-S complexMKP-1-gene
MKP-1
  5 Feb 2000 This is a crude model of activation of MKP1 production by MAPK. Time-course poorly constrained: 10 min to > 100 min. Rates are further constrained by the known degradation rates of MKP-1, also in this model. Peak MKP-1 is about 10 times basal (from Brondello et al Science 286:2514 1999). Max MAPK ~.25 uM, degradation 45 min. So this enz has to provide 22nM MKP every 45 min.
4 Enzyme Activity:
MKP1*-thr-deph

Enzyme Molecule:
MKP-1**		0.066714Classical Michaelis-Menten
V = Etot.S.Kcat/Km+S		MAPK*
MAPK-tyr
  3 Feb 2000. Same rates as MKP1
5 Enzyme Activity:
MKP1*-tyr-deph

Enzyme Molecule:
MKP-1**		0.066714Classical Michaelis-Menten
V = Etot.S.Kcat/Km+S		MAPK-tyr
MAPK
  3 Feb 2000. Same rates as MKP-1.
6 Enzyme Activity:
Raf-GTP-Ras*.1

Enzyme Molecule:
Raf-GTP-Ras*		0.15910.1054explicit E-S complexMAPKK
MAPKK-ser
  Kinetics are the same as for the craf-1* activity, ie., k1=1.1e-6, k2=.42, k3 =0.105 These are based on Force et al PNAS USA 91 1270-1274 1994. These parms cannot reach the observed 4X stim of MAPK. So lets increase the affinity, ie, raise k1 10X to 1.1e-5 Lets take it back down to where it was. Back up to 5X: 5.5e-6
7 Enzyme Activity:
Raf-GTP-Ras*.2

Enzyme Molecule:
Raf-GTP-Ras*		0.15910.1054explicit E-S complexMAPKK-ser
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
8 Enzyme Activity:
RGR.1

Enzyme Molecule:
RGR		0.15910.1054explicit E-S complexMAPKK
MAPKK-ser
  Kinetics are the same as for the craf-1* activity, ie., k1=1.1e-6, k2=.42, k3 =0.105 These are based on Force et al PNAS USA 91 1270-1274 1994. These parms cannot reach the observed 4X stim of MAPK. So lets increase the affinity, ie, raise k1 10X to 1.1e-5 Lets take it back down to where it was. Back up to 5X: 5.5e-6
9 Enzyme Activity:
RGR.2

Enzyme Molecule:
RGR		0.15910.1054explicit E-S complexMAPKK-ser
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
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