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Accession Type:
Network
Ajay_Bhalla_
2004_PKM_Tuning
PKC
Shared_Object_
Ajay_Bhalla_
2004_PKM_tuning
PLA2
PLCbeta
Gq
MAPK
Ras
 Molecule
 Enzyme
 Reaction
EGFR
Sos
PLC_g
CaMKII
CaM
PP1
PP2B
PKA
AC
PKM

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Reaction List for pathway Ras (Pathway Number 318)

Kd is calculated only for second order reactions, like nA+nB <->nC or nA<->nC+nD, where n is number and A,B,C,D are molecules, where as for first order reactions Keq is calculated. Kd for higher order reactions is not considered.
  Name KfKbKdtauSubstrateProduct
1 bg-act-GEFkf
(uM^-1 s^-1)
1
(s^-1)
Kd(bf) = 0.1667(uM)-BetaGamma
inact-GEF
GEF-Gprot-bg
  SoS/GEF is present at 50 nM ie 3e4/cell. BetaGamma maxes out at 9e4. Assume we have 1/3 of the GEF active when the BetaGamma is 1.5e4. so 1e4 * kb = 2e4 * 1.5e4 * kf, so kf/kb = 3e-5. The rate of this equil should be reasonably fast, say 1/sec
2 CaM-bind-GEFkf
(uM^-1 s^-1)
1
(s^-1)
Kd(bf) = 0.005(uM)-inact-GEF
CaM-Ca4
CaM-GEF
  We have no numbers for this. It is probably between the two extremes represented by the CaMKII phosph states, and I have used guesses based on this. kf=1e-4 kb=1 The reaction is based on Farnsworth et al Nature 376 524-527 1995
3 dephosph-GAPkf
(s^-1)
0
(s^-1)
--GAP*
GAP
  Assume a reasonably good rate for dephosphorylating it, 1/sec
4 dephosph-GEFkf
(s^-1)
0
(s^-1)
--GEF*
inact-GEF
5 dephosph-inact-G
EF*
kf
(s^-1)
0
(s^-1)
--inact-GEF*
inact-GEF
6 Ras-intrinsic-GT
Pase
kf
(s^-1)
0
(s^-1)
--GTP-Ras
GDP-Ras
  This is extremely slow (1e-4), but it is significant as so little GAP actually gets complexed with it that the total GTP turnover rises only by 2-3 X (see Gibbs et al, JBC 265(33) 20437-20422) and Eccleston et al JBC 268(36) 27012-27019 kf = 1e-4


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