NCBS Home page
Accession List
Pathway List
Search
Authorized Users
Help
News archives

Accession Type:
Pathway
RasGTPase
RasGTPase
 Molecule
 Reaction

Enter a Search String

Special character and space not allowed in the query term. Search string should be at least 2 characters long.
Search in: Search for Match By

Reaction List for pathway RasGTPase (Pathway Number 307)

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 GAP_
dissociation
kf
(s^-1)
1.2
(uM^-1 s^-1)
Kd(cb) = 0.0258(uM)-RasGDP_NF1
RasGDP
NF1
  Dissociation of NF1 from Ras.GDP NF1 is a mammalian GAP Kf = 46.5 /sec Kb = 1.2 /sec/uM Table 3, Phillips RA et al 2003 Biochemistry 42: 3956-3965
2 GTP_
hydrolysis[1]
kf
(s^-1)
0.22
(s^-1)
Keq = 0.0113(uM)0.051secRasGTP-NF1*
RasGDP-NF1_Pi
  First step in hydrolysis of GTP bound to Ras complexed with NF1 - a mammalian GAP Kf = 19.5 /sec Kb = 0.22 /sec Table 3, Phillips RA et al 2003 Biochemistry 42: 3956-3965
3 GTP_
hydrolysis[2]
kf
(s^-1)
0.0001
(uM^-1 s^-1)
Kd(cb) = 0(uM)-RasGDP-NF1_Pi
Pi
RasGDP_NF1
  Second step in hydrolysis of GTP bound to Ras is complexed with NF1 - a mammalian GAP Kf = 40 /sec Kb = 108 /M/sec = 1.08e-04 /uM/sec Phillips RA et al 2003 Biochemistry 42: 3956-3965
4 NF1_bindingkf
(uM^-1 s^-1)
6.36
(s^-1)
Kd(bf) = 5.3(uM)-RasGTP
NF1
RasGTP-NF1
  Binding of NF1 to Ras.GTP NF1 is a mammalian GAP Kd = 5.3 uM Table 3, Phillips RA et al 2003 Biochemistry 42: 3956-3965
5 Ras_activationkf
(s^-1)
5.5
(s^-1)
Keq = 0.0132(uM)0.002secRasGTP-NF1
RasGTP-NF1*
  Activation of Ras by GAP (i.e NF1) Kf = 418 /sec Kb = 5.5 /sec Table 3, Phillips RA et al 2003 Biochemistry 42: 3956-3965


Pathway Details   Molecule List  Enzyme List  Reaction List  


Database compilation and code copyright (C) 2022, Upinder S. Bhalla and NCBS/TIFR
This Copyright is applied to ensure that the contents of this database remain freely available. Please see FAQ for details.