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Molecule Parameter List for MKP-1

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
MKP-1 participated asMoleculeSum total ofEnzymeSubstrate of an enzymeProduct of an enzymeSubstrate in ReactionProduct in Reaction
No. of occurrences25050002424

Accession and Pathway Details
Accession NameAccession No.Accession TypePathway Link
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    		• 81NetworkShared_Object_Ajay_bhalla_2007_ReacDiff1_1e-12,  
    PKC,  MAPK,  Ras,  CaM,  PKM,  chain,  kinetics,  PKC,  MAPK,  Ras,  CaM,  PKM,  kinetics[1],  
    PKC,  MAPK,  Ras,  CaM,  PKM,  kinetics[2],  PKC,  MAPK,  Ras,  CaM,  PKM,  kinetics[3],  
    PKC,  MAPK,  MAPK,  Ras,  CaM,  PKM,  kinetics[4],  PKC,  MAPK,  Ras,  CaM,  PKM,  
    kinetics[5],  PKC,  MAPK,  Ras,  kinetics[6],  CaM,  PKM,  PKC,  MAPK,  Ras,  
    CaM,  PKM,  kinetics[7],  PKC,  Ras,  CaM,  PKM,  kinetics[8],  PKC,  MAPK,  
    Ras,  CaM,  PKM,  kinetics[9],  PKC,  MAPK,  Ras,  CaM,  PKM,  kinetics[10],  
    PKC,  MAPK,  Ras,  CaM,  PKM,  kinetics[11],  PKC,  MAPK,  Ras,  CaM,  PKM,  kinetics[12],  
    PKC,  MAPK,  Ras,  CaM,  PKM,  kinetics[13],  PKC,  MAPK,  Ras,  CaM,  PKM,  kinetics[14],  
    PKC,  MAPK,  Ras,  CaM,  PKM,  kinetics[15],  PKC,  MAPK,  Ras,  CaM,  PKM,  kinetics[16],  
    PKC,  MAPK,  Ras,  CaM,  PKM,  kinetics[17],  PKC,  MAPK,  Ras,  CaM,  PKM,  kinetics[18],  
    PKC,  MAPK,  Ras,  CaM,  PKM,  kinetics[19],  PKC,  MAPK,  Ras,  CaM,  PKM,  kinetics[20],  
    PKC,  MAPK,  Ras,  CaM,  PKM,  kinetics[21],  PKC,  MAPK,  Ras,  CaM,  PKM,  kinetics[22],  
    PKC,  MAPK,  Ras,  CaM,  PKM,  kinetics[23],  PKC,  MAPK,  Ras,  CaM,  PKM 
    This is a 25-compartment reaction-diffusion version of the Ajay_Bhalla_2007_PKM model. The original single-compartment model is repeated 25 times. In addition, a subset (27 out of 42) molecules can diffuse between compartments. Diffusion is implemented as a reaction between corresponding molecules in neighboring compartments. For D = 1e-12 m^2/sec (i.e., 1 micron^2/sec ) the kf and kb of this reaction for these 10 micron compartments are both 0.01/sec. For D = 1e-13 m^2/sec (i.e., 0.1 micron^2/sec ) the kf and kb are 0.001/sec.
    The stimulus file pkm_mapk22_diff_1e-12_Fig4A which was used for the model to replicate Figure 4A from the paper.
    This stimulus file pkm_mapk22_diff_1e-12_Fig4G which was used for the model to replicate Figure 4G from the paper

    MKP-1 acting as a Molecule in      Ajay_bhalla_2007_ReacDiff1_1e-12 Network
    NameAccession NamePathway NameInitial Conc.
    (uM)    		Volume
    (fL)    		Buffered
    MKP-1
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
  • Shared_Object_
    Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Pathway No. : 375
    		• 0.021.5No
    MKP-1 dephosphoryates and inactivates MAPK in vivo: Sun et al Cell 75 487-493 1993. Levels of MKP-1 are regulated, and rise in 1 hour. Kinetics from Charles et al PNAS 90:5292-5296 1993. They refer to Charles et al Oncogene 7 187-190 who show that half-life of MKP1/3CH134 is 40 min. 80% deph of MAPK in 20 min Sep 17 1997: CoInit now 0.4x to 0.0032. See parm searches from jun96 on.
    MKP-1
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
    		• kinetics
    Pathway No. : 382    		0.021.5No
    MKP-1 dephosphoryates and inactivates MAPK in vivo: Sun et al Cell 75 487-493 1993. Levels of MKP-1 are regulated, and rise in 1 hour. Kinetics from Charles et al PNAS 90:5292-5296 1993. They refer to Charles et al Oncogene 7 187-190 who show that half-life of MKP1/3CH134 is 40 min. 80% deph of MAPK in 20 min Sep 17 1997: CoInit now 0.4x to 0.0032. See parm searches from jun96 on.
    MKP-1
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
    		• kinetics[1]
    Pathway No. : 388    		0.021.5No
    MKP-1 dephosphoryates and inactivates MAPK in vivo: Sun et al Cell 75 487-493 1993. Levels of MKP-1 are regulated, and rise in 1 hour. Kinetics from Charles et al PNAS 90:5292-5296 1993. They refer to Charles et al Oncogene 7 187-190 who show that half-life of MKP1/3CH134 is 40 min. 80% deph of MAPK in 20 min Sep 17 1997: CoInit now 0.4x to 0.0032. See parm searches from jun96 on.
    MKP-1
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
    		• kinetics[2]
    Pathway No. : 394    		0.021.5No
    MKP-1 dephosphoryates and inactivates MAPK in vivo: Sun et al Cell 75 487-493 1993. Levels of MKP-1 are regulated, and rise in 1 hour. Kinetics from Charles et al PNAS 90:5292-5296 1993. They refer to Charles et al Oncogene 7 187-190 who show that half-life of MKP1/3CH134 is 40 min. 80% deph of MAPK in 20 min Sep 17 1997: CoInit now 0.4x to 0.0032. See parm searches from jun96 on.
    MKP-1
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
    		• kinetics[3]
    Pathway No. : 400    		0.021.5No
    MKP-1 dephosphoryates and inactivates MAPK in vivo: Sun et al Cell 75 487-493 1993. Levels of MKP-1 are regulated, and rise in 1 hour. Kinetics from Charles et al PNAS 90:5292-5296 1993. They refer to Charles et al Oncogene 7 187-190 who show that half-life of MKP1/3CH134 is 40 min. 80% deph of MAPK in 20 min Sep 17 1997: CoInit now 0.4x to 0.0032. See parm searches from jun96 on.
    MKP-1
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
    		• kinetics[4]
    Pathway No. : 407    		0.021.5No
    MKP-1 dephosphoryates and inactivates MAPK in vivo: Sun et al Cell 75 487-493 1993. Levels of MKP-1 are regulated, and rise in 1 hour. Kinetics from Charles et al PNAS 90:5292-5296 1993. They refer to Charles et al Oncogene 7 187-190 who show that half-life of MKP1/3CH134 is 40 min. 80% deph of MAPK in 20 min Sep 17 1997: CoInit now 0.4x to 0.0032. See parm searches from jun96 on.
    MKP-1
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
    		• kinetics[5]
    Pathway No. : 413    		0.021.5No
    MKP-1 dephosphoryates and inactivates MAPK in vivo: Sun et al Cell 75 487-493 1993. Levels of MKP-1 are regulated, and rise in 1 hour. Kinetics from Charles et al PNAS 90:5292-5296 1993. They refer to Charles et al Oncogene 7 187-190 who show that half-life of MKP1/3CH134 is 40 min. 80% deph of MAPK in 20 min Sep 17 1997: CoInit now 0.4x to 0.0032. See parm searches from jun96 on.
    MKP-1
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
    		• kinetics[6]
    Pathway No. : 417    		0.021.5No
    MKP-1 dephosphoryates and inactivates MAPK in vivo: Sun et al Cell 75 487-493 1993. Levels of MKP-1 are regulated, and rise in 1 hour. Kinetics from Charles et al PNAS 90:5292-5296 1993. They refer to Charles et al Oncogene 7 187-190 who show that half-life of MKP1/3CH134 is 40 min. 80% deph of MAPK in 20 min Sep 17 1997: CoInit now 0.4x to 0.0032. See parm searches from jun96 on.
    MKP-1
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
    		• kinetics[7]
    Pathway No. : 425    		0.021.5No
    MKP-1 dephosphoryates and inactivates MAPK in vivo: Sun et al Cell 75 487-493 1993. Levels of MKP-1 are regulated, and rise in 1 hour. Kinetics from Charles et al PNAS 90:5292-5296 1993. They refer to Charles et al Oncogene 7 187-190 who show that half-life of MKP1/3CH134 is 40 min. 80% deph of MAPK in 20 min Sep 17 1997: CoInit now 0.4x to 0.0032. See parm searches from jun96 on.
    MKP-1
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
    		• kinetics[8]
    Pathway No. : 430    		0.021.5No
    MKP-1 dephosphoryates and inactivates MAPK in vivo: Sun et al Cell 75 487-493 1993. Levels of MKP-1 are regulated, and rise in 1 hour. Kinetics from Charles et al PNAS 90:5292-5296 1993. They refer to Charles et al Oncogene 7 187-190 who show that half-life of MKP1/3CH134 is 40 min. 80% deph of MAPK in 20 min Sep 17 1997: CoInit now 0.4x to 0.0032. See parm searches from jun96 on.
    MKP-1
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
    		• kinetics[9]
    Pathway No. : 436    		0.021.5No
    MKP-1 dephosphoryates and inactivates MAPK in vivo: Sun et al Cell 75 487-493 1993. Levels of MKP-1 are regulated, and rise in 1 hour. Kinetics from Charles et al PNAS 90:5292-5296 1993. They refer to Charles et al Oncogene 7 187-190 who show that half-life of MKP1/3CH134 is 40 min. 80% deph of MAPK in 20 min Sep 17 1997: CoInit now 0.4x to 0.0032. See parm searches from jun96 on.
    MKP-1
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
    		• kinetics[10]
    Pathway No. : 442    		0.021.5No
    MKP-1 dephosphoryates and inactivates MAPK in vivo: Sun et al Cell 75 487-493 1993. Levels of MKP-1 are regulated, and rise in 1 hour. Kinetics from Charles et al PNAS 90:5292-5296 1993. They refer to Charles et al Oncogene 7 187-190 who show that half-life of MKP1/3CH134 is 40 min. 80% deph of MAPK in 20 min Sep 17 1997: CoInit now 0.4x to 0.0032. See parm searches from jun96 on.
    MKP-1
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
    		• kinetics[11]
    Pathway No. : 448    		0.021.5No
    MKP-1 dephosphoryates and inactivates MAPK in vivo: Sun et al Cell 75 487-493 1993. Levels of MKP-1 are regulated, and rise in 1 hour. Kinetics from Charles et al PNAS 90:5292-5296 1993. They refer to Charles et al Oncogene 7 187-190 who show that half-life of MKP1/3CH134 is 40 min. 80% deph of MAPK in 20 min Sep 17 1997: CoInit now 0.4x to 0.0032. See parm searches from jun96 on.
    MKP-1
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
    		• kinetics[12]
    Pathway No. : 454    		0.021.5No
    MKP-1 dephosphoryates and inactivates MAPK in vivo: Sun et al Cell 75 487-493 1993. Levels of MKP-1 are regulated, and rise in 1 hour. Kinetics from Charles et al PNAS 90:5292-5296 1993. They refer to Charles et al Oncogene 7 187-190 who show that half-life of MKP1/3CH134 is 40 min. 80% deph of MAPK in 20 min Sep 17 1997: CoInit now 0.4x to 0.0032. See parm searches from jun96 on.
    MKP-1
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
    		• kinetics[13]
    Pathway No. : 460    		0.021.5No
    MKP-1 dephosphoryates and inactivates MAPK in vivo: Sun et al Cell 75 487-493 1993. Levels of MKP-1 are regulated, and rise in 1 hour. Kinetics from Charles et al PNAS 90:5292-5296 1993. They refer to Charles et al Oncogene 7 187-190 who show that half-life of MKP1/3CH134 is 40 min. 80% deph of MAPK in 20 min Sep 17 1997: CoInit now 0.4x to 0.0032. See parm searches from jun96 on.
    MKP-1
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
    		• kinetics[14]
    Pathway No. : 466    		0.021.5No
    MKP-1 dephosphoryates and inactivates MAPK in vivo: Sun et al Cell 75 487-493 1993. Levels of MKP-1 are regulated, and rise in 1 hour. Kinetics from Charles et al PNAS 90:5292-5296 1993. They refer to Charles et al Oncogene 7 187-190 who show that half-life of MKP1/3CH134 is 40 min. 80% deph of MAPK in 20 min Sep 17 1997: CoInit now 0.4x to 0.0032. See parm searches from jun96 on.
    MKP-1
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
    		• kinetics[15]
    Pathway No. : 472    		0.021.5No
    MKP-1 dephosphoryates and inactivates MAPK in vivo: Sun et al Cell 75 487-493 1993. Levels of MKP-1 are regulated, and rise in 1 hour. Kinetics from Charles et al PNAS 90:5292-5296 1993. They refer to Charles et al Oncogene 7 187-190 who show that half-life of MKP1/3CH134 is 40 min. 80% deph of MAPK in 20 min Sep 17 1997: CoInit now 0.4x to 0.0032. See parm searches from jun96 on.
    MKP-1
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
    		• kinetics[16]
    Pathway No. : 478    		0.021.5No
    MKP-1 dephosphoryates and inactivates MAPK in vivo: Sun et al Cell 75 487-493 1993. Levels of MKP-1 are regulated, and rise in 1 hour. Kinetics from Charles et al PNAS 90:5292-5296 1993. They refer to Charles et al Oncogene 7 187-190 who show that half-life of MKP1/3CH134 is 40 min. 80% deph of MAPK in 20 min Sep 17 1997: CoInit now 0.4x to 0.0032. See parm searches from jun96 on.
    MKP-1
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
    		• kinetics[17]
    Pathway No. : 484    		0.021.5No
    MKP-1 dephosphoryates and inactivates MAPK in vivo: Sun et al Cell 75 487-493 1993. Levels of MKP-1 are regulated, and rise in 1 hour. Kinetics from Charles et al PNAS 90:5292-5296 1993. They refer to Charles et al Oncogene 7 187-190 who show that half-life of MKP1/3CH134 is 40 min. 80% deph of MAPK in 20 min Sep 17 1997: CoInit now 0.4x to 0.0032. See parm searches from jun96 on.
    MKP-1
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
    		• kinetics[18]
    Pathway No. : 490    		0.021.5No
    MKP-1 dephosphoryates and inactivates MAPK in vivo: Sun et al Cell 75 487-493 1993. Levels of MKP-1 are regulated, and rise in 1 hour. Kinetics from Charles et al PNAS 90:5292-5296 1993. They refer to Charles et al Oncogene 7 187-190 who show that half-life of MKP1/3CH134 is 40 min. 80% deph of MAPK in 20 min Sep 17 1997: CoInit now 0.4x to 0.0032. See parm searches from jun96 on.
    MKP-1
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
    		• kinetics[19]
    Pathway No. : 496    		0.021.5No
    MKP-1 dephosphoryates and inactivates MAPK in vivo: Sun et al Cell 75 487-493 1993. Levels of MKP-1 are regulated, and rise in 1 hour. Kinetics from Charles et al PNAS 90:5292-5296 1993. They refer to Charles et al Oncogene 7 187-190 who show that half-life of MKP1/3CH134 is 40 min. 80% deph of MAPK in 20 min Sep 17 1997: CoInit now 0.4x to 0.0032. See parm searches from jun96 on.
    MKP-1
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
    		• kinetics[20]
    Pathway No. : 502    		0.021.5No
    MKP-1 dephosphoryates and inactivates MAPK in vivo: Sun et al Cell 75 487-493 1993. Levels of MKP-1 are regulated, and rise in 1 hour. Kinetics from Charles et al PNAS 90:5292-5296 1993. They refer to Charles et al Oncogene 7 187-190 who show that half-life of MKP1/3CH134 is 40 min. 80% deph of MAPK in 20 min Sep 17 1997: CoInit now 0.4x to 0.0032. See parm searches from jun96 on.
    MKP-1
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
    		• kinetics[21]
    Pathway No. : 508    		0.021.5No
    MKP-1 dephosphoryates and inactivates MAPK in vivo: Sun et al Cell 75 487-493 1993. Levels of MKP-1 are regulated, and rise in 1 hour. Kinetics from Charles et al PNAS 90:5292-5296 1993. They refer to Charles et al Oncogene 7 187-190 who show that half-life of MKP1/3CH134 is 40 min. 80% deph of MAPK in 20 min Sep 17 1997: CoInit now 0.4x to 0.0032. See parm searches from jun96 on.
    MKP-1
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
    		• kinetics[22]
    Pathway No. : 514    		0.021.5No
    MKP-1 dephosphoryates and inactivates MAPK in vivo: Sun et al Cell 75 487-493 1993. Levels of MKP-1 are regulated, and rise in 1 hour. Kinetics from Charles et al PNAS 90:5292-5296 1993. They refer to Charles et al Oncogene 7 187-190 who show that half-life of MKP1/3CH134 is 40 min. 80% deph of MAPK in 20 min Sep 17 1997: CoInit now 0.4x to 0.0032. See parm searches from jun96 on.
    MKP-1
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
    		• kinetics[23]
    Pathway No. : 520    		0.021.5No
    MKP-1 dephosphoryates and inactivates MAPK in vivo: Sun et al Cell 75 487-493 1993. Levels of MKP-1 are regulated, and rise in 1 hour. Kinetics from Charles et al PNAS 90:5292-5296 1993. They refer to Charles et al Oncogene 7 187-190 who show that half-life of MKP1/3CH134 is 40 min. 80% deph of MAPK in 20 min Sep 17 1997: CoInit now 0.4x to 0.0032. See parm searches from jun96 on.

    MKP-1 acting as an Enzyme in      Ajay_bhalla_2007_ReacDiff1_1e-12 Network
     Enzyme Molecule /
    Enzyme Activity    		Accession NamePathway NameKm (uM)kcat (s^-1)RatioEnzyme TypeReagents
    1MKP-1 /
    MKP1-tyr-deph
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
  • Shared_Object_
    Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Pathway No. : 375
    		• 7.0000344explicit E-S complexSubstrate
    MAPK-tyr

    Product
    MAPK
        The original kinetics have been modified to obey the k2 = 4 * k3 rule, while keeping kcat and Km fixed. As noted in the NOTES, the only constraining data point is the time course of MAPK dephosphorylation, which this model satisfies. It would be nice to have more accurate estimates of rate consts and MKP-1 levels from the literature. Effective Km : 67 nM kcat = 1.43 umol/min/mg
    2MKP-1 /
    MKP1-thr-deph
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
  • Shared_Object_
    Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Pathway No. : 375
    		• 7.0000344explicit E-S complexSubstrate
    MAPK*

    Product
    MAPK-tyr
        See MKP1-tyr-deph
    3MKP-1 /
    MKP1-tyr-deph
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
    		• kinetics
    Pathway No. : 382    		7.0000344explicit E-S complexSubstrate
    MAPK-tyr

    Product
    MAPK
        The original kinetics have been modified to obey the k2 = 4 * k3 rule, while keeping kcat and Km fixed. As noted in the NOTES, the only constraining data point is the time course of MAPK dephosphorylation, which this model satisfies. It would be nice to have more accurate estimates of rate consts and MKP-1 levels from the literature. Effective Km : 67 nM kcat = 1.43 umol/min/mg
    4MKP-1 /
    MKP1-thr-deph
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
    		• kinetics
    Pathway No. : 382    		7.0000344explicit E-S complexSubstrate
    MAPK*

    Product
    MAPK-tyr
        See MKP1-tyr-deph
    5MKP-1 /
    MKP1-tyr-deph
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
    		• kinetics[1]
    Pathway No. : 388    		7.0000344explicit E-S complexSubstrate
    MAPK-tyr

    Product
    MAPK
        The original kinetics have been modified to obey the k2 = 4 * k3 rule, while keeping kcat and Km fixed. As noted in the NOTES, the only constraining data point is the time course of MAPK dephosphorylation, which this model satisfies. It would be nice to have more accurate estimates of rate consts and MKP-1 levels from the literature. Effective Km : 67 nM kcat = 1.43 umol/min/mg
    6MKP-1 /
    MKP1-thr-deph
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
    		• kinetics[1]
    Pathway No. : 388    		7.0000344explicit E-S complexSubstrate
    MAPK*

    Product
    MAPK-tyr
        See MKP1-tyr-deph
    7MKP-1 /
    MKP1-tyr-deph
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
    		• kinetics[2]
    Pathway No. : 394    		7.0000344explicit E-S complexSubstrate
    MAPK-tyr

    Product
    MAPK
        The original kinetics have been modified to obey the k2 = 4 * k3 rule, while keeping kcat and Km fixed. As noted in the NOTES, the only constraining data point is the time course of MAPK dephosphorylation, which this model satisfies. It would be nice to have more accurate estimates of rate consts and MKP-1 levels from the literature. Effective Km : 67 nM kcat = 1.43 umol/min/mg
    8MKP-1 /
    MKP1-thr-deph
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
    		• kinetics[2]
    Pathway No. : 394    		7.0000344explicit E-S complexSubstrate
    MAPK*

    Product
    MAPK-tyr
        See MKP1-tyr-deph
    9MKP-1 /
    MKP1-tyr-deph
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
    		• kinetics[3]
    Pathway No. : 400    		7.0000344explicit E-S complexSubstrate
    MAPK-tyr

    Product
    MAPK
        The original kinetics have been modified to obey the k2 = 4 * k3 rule, while keeping kcat and Km fixed. As noted in the NOTES, the only constraining data point is the time course of MAPK dephosphorylation, which this model satisfies. It would be nice to have more accurate estimates of rate consts and MKP-1 levels from the literature. Effective Km : 67 nM kcat = 1.43 umol/min/mg
    10MKP-1 /
    MKP1-thr-deph
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
    		• kinetics[3]
    Pathway No. : 400    		7.0000344explicit E-S complexSubstrate
    MAPK*

    Product
    MAPK-tyr
        See MKP1-tyr-deph
    11MKP-1 /
    MKP1-tyr-deph
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
    		• kinetics[4]
    Pathway No. : 407    		7.0000344explicit E-S complexSubstrate
    MAPK-tyr

    Product
    MAPK
        The original kinetics have been modified to obey the k2 = 4 * k3 rule, while keeping kcat and Km fixed. As noted in the NOTES, the only constraining data point is the time course of MAPK dephosphorylation, which this model satisfies. It would be nice to have more accurate estimates of rate consts and MKP-1 levels from the literature. Effective Km : 67 nM kcat = 1.43 umol/min/mg
    12MKP-1 /
    MKP1-thr-deph
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
    		• kinetics[4]
    Pathway No. : 407    		7.0000344explicit E-S complexSubstrate
    MAPK*

    Product
    MAPK-tyr
        See MKP1-tyr-deph
    13MKP-1 /
    MKP1-tyr-deph
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
    		• kinetics[5]
    Pathway No. : 413    		7.0000344explicit E-S complexSubstrate
    MAPK-tyr

    Product
    MAPK
        The original kinetics have been modified to obey the k2 = 4 * k3 rule, while keeping kcat and Km fixed. As noted in the NOTES, the only constraining data point is the time course of MAPK dephosphorylation, which this model satisfies. It would be nice to have more accurate estimates of rate consts and MKP-1 levels from the literature. Effective Km : 67 nM kcat = 1.43 umol/min/mg
    14MKP-1 /
    MKP1-thr-deph
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
    		• kinetics[5]
    Pathway No. : 413    		7.0000344explicit E-S complexSubstrate
    MAPK*

    Product
    MAPK-tyr
        See MKP1-tyr-deph
    15MKP-1 /
    MKP1-tyr-deph
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
    		• kinetics[6]
    Pathway No. : 417    		7.0000344explicit E-S complexSubstrate
    MAPK-tyr

    Product
    MAPK
        The original kinetics have been modified to obey the k2 = 4 * k3 rule, while keeping kcat and Km fixed. As noted in the NOTES, the only constraining data point is the time course of MAPK dephosphorylation, which this model satisfies. It would be nice to have more accurate estimates of rate consts and MKP-1 levels from the literature. Effective Km : 67 nM kcat = 1.43 umol/min/mg
    16MKP-1 /
    MKP1-thr-deph
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
    		• kinetics[6]
    Pathway No. : 417    		7.0000344explicit E-S complexSubstrate
    MAPK*

    Product
    MAPK-tyr
        See MKP1-tyr-deph
    17MKP-1 /
    MKP1-tyr-deph
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
    		• kinetics[7]
    Pathway No. : 425    		7.0000344explicit E-S complexSubstrate
    MAPK-tyr

    Product
    MAPK
        The original kinetics have been modified to obey the k2 = 4 * k3 rule, while keeping kcat and Km fixed. As noted in the NOTES, the only constraining data point is the time course of MAPK dephosphorylation, which this model satisfies. It would be nice to have more accurate estimates of rate consts and MKP-1 levels from the literature. Effective Km : 67 nM kcat = 1.43 umol/min/mg
    18MKP-1 /
    MKP1-thr-deph
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
    		• kinetics[7]
    Pathway No. : 425    		7.0000344explicit E-S complexSubstrate
    MAPK*

    Product
    MAPK-tyr
        See MKP1-tyr-deph
    19MKP-1 /
    MKP1-tyr-deph
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
    		• kinetics[8]
    Pathway No. : 430    		7.0000344explicit E-S complexSubstrate
    MAPK-tyr

    Product
    MAPK
        The original kinetics have been modified to obey the k2 = 4 * k3 rule, while keeping kcat and Km fixed. As noted in the NOTES, the only constraining data point is the time course of MAPK dephosphorylation, which this model satisfies. It would be nice to have more accurate estimates of rate consts and MKP-1 levels from the literature. Effective Km : 67 nM kcat = 1.43 umol/min/mg
    20MKP-1 /
    MKP1-thr-deph
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
    		• kinetics[8]
    Pathway No. : 430    		7.0000344explicit E-S complexSubstrate
    MAPK*

    Product
    MAPK-tyr
        See MKP1-tyr-deph
    21MKP-1 /
    MKP1-tyr-deph
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
    		• kinetics[9]
    Pathway No. : 436    		7.0000344explicit E-S complexSubstrate
    MAPK-tyr

    Product
    MAPK
        The original kinetics have been modified to obey the k2 = 4 * k3 rule, while keeping kcat and Km fixed. As noted in the NOTES, the only constraining data point is the time course of MAPK dephosphorylation, which this model satisfies. It would be nice to have more accurate estimates of rate consts and MKP-1 levels from the literature. Effective Km : 67 nM kcat = 1.43 umol/min/mg
    22MKP-1 /
    MKP1-thr-deph
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
    		• kinetics[9]
    Pathway No. : 436    		7.0000344explicit E-S complexSubstrate
    MAPK*

    Product
    MAPK-tyr
        See MKP1-tyr-deph
    23MKP-1 /
    MKP1-tyr-deph
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
    		• kinetics[10]
    Pathway No. : 442    		7.0000344explicit E-S complexSubstrate
    MAPK-tyr

    Product
    MAPK
        The original kinetics have been modified to obey the k2 = 4 * k3 rule, while keeping kcat and Km fixed. As noted in the NOTES, the only constraining data point is the time course of MAPK dephosphorylation, which this model satisfies. It would be nice to have more accurate estimates of rate consts and MKP-1 levels from the literature. Effective Km : 67 nM kcat = 1.43 umol/min/mg
    24MKP-1 /
    MKP1-thr-deph
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
    		• kinetics[10]
    Pathway No. : 442    		7.0000344explicit E-S complexSubstrate
    MAPK*

    Product
    MAPK-tyr
        See MKP1-tyr-deph
    25MKP-1 /
    MKP1-tyr-deph
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
    		• kinetics[11]
    Pathway No. : 448    		7.0000344explicit E-S complexSubstrate
    MAPK-tyr

    Product
    MAPK
        The original kinetics have been modified to obey the k2 = 4 * k3 rule, while keeping kcat and Km fixed. As noted in the NOTES, the only constraining data point is the time course of MAPK dephosphorylation, which this model satisfies. It would be nice to have more accurate estimates of rate consts and MKP-1 levels from the literature. Effective Km : 67 nM kcat = 1.43 umol/min/mg
    26MKP-1 /
    MKP1-thr-deph
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
    		• kinetics[11]
    Pathway No. : 448    		7.0000344explicit E-S complexSubstrate
    MAPK*

    Product
    MAPK-tyr
        See MKP1-tyr-deph
    27MKP-1 /
    MKP1-tyr-deph
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
    		• kinetics[12]
    Pathway No. : 454    		7.0000344explicit E-S complexSubstrate
    MAPK-tyr

    Product
    MAPK
        The original kinetics have been modified to obey the k2 = 4 * k3 rule, while keeping kcat and Km fixed. As noted in the NOTES, the only constraining data point is the time course of MAPK dephosphorylation, which this model satisfies. It would be nice to have more accurate estimates of rate consts and MKP-1 levels from the literature. Effective Km : 67 nM kcat = 1.43 umol/min/mg
    28MKP-1 /
    MKP1-thr-deph
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
    		• kinetics[12]
    Pathway No. : 454    		7.0000344explicit E-S complexSubstrate
    MAPK*

    Product
    MAPK-tyr
        See MKP1-tyr-deph
    29MKP-1 /
    MKP1-tyr-deph
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
    		• kinetics[13]
    Pathway No. : 460    		7.0000344explicit E-S complexSubstrate
    MAPK-tyr

    Product
    MAPK
        The original kinetics have been modified to obey the k2 = 4 * k3 rule, while keeping kcat and Km fixed. As noted in the NOTES, the only constraining data point is the time course of MAPK dephosphorylation, which this model satisfies. It would be nice to have more accurate estimates of rate consts and MKP-1 levels from the literature. Effective Km : 67 nM kcat = 1.43 umol/min/mg
    30MKP-1 /
    MKP1-thr-deph
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
    		• kinetics[13]
    Pathway No. : 460    		7.0000344explicit E-S complexSubstrate
    MAPK*

    Product
    MAPK-tyr
        See MKP1-tyr-deph
    31MKP-1 /
    MKP1-tyr-deph
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
    		• kinetics[14]
    Pathway No. : 466    		7.0000344explicit E-S complexSubstrate
    MAPK-tyr

    Product
    MAPK
        The original kinetics have been modified to obey the k2 = 4 * k3 rule, while keeping kcat and Km fixed. As noted in the NOTES, the only constraining data point is the time course of MAPK dephosphorylation, which this model satisfies. It would be nice to have more accurate estimates of rate consts and MKP-1 levels from the literature. Effective Km : 67 nM kcat = 1.43 umol/min/mg
    32MKP-1 /
    MKP1-thr-deph
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
    		• kinetics[14]
    Pathway No. : 466    		7.0000344explicit E-S complexSubstrate
    MAPK*

    Product
    MAPK-tyr
        See MKP1-tyr-deph
    33MKP-1 /
    MKP1-tyr-deph
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
    		• kinetics[15]
    Pathway No. : 472    		7.0000344explicit E-S complexSubstrate
    MAPK-tyr

    Product
    MAPK
        The original kinetics have been modified to obey the k2 = 4 * k3 rule, while keeping kcat and Km fixed. As noted in the NOTES, the only constraining data point is the time course of MAPK dephosphorylation, which this model satisfies. It would be nice to have more accurate estimates of rate consts and MKP-1 levels from the literature. Effective Km : 67 nM kcat = 1.43 umol/min/mg
    34MKP-1 /
    MKP1-thr-deph
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
    		• kinetics[15]
    Pathway No. : 472    		7.0000344explicit E-S complexSubstrate
    MAPK*

    Product
    MAPK-tyr
        See MKP1-tyr-deph
    35MKP-1 /
    MKP1-tyr-deph
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
    		• kinetics[16]
    Pathway No. : 478    		7.0000344explicit E-S complexSubstrate
    MAPK-tyr

    Product
    MAPK
        The original kinetics have been modified to obey the k2 = 4 * k3 rule, while keeping kcat and Km fixed. As noted in the NOTES, the only constraining data point is the time course of MAPK dephosphorylation, which this model satisfies. It would be nice to have more accurate estimates of rate consts and MKP-1 levels from the literature. Effective Km : 67 nM kcat = 1.43 umol/min/mg
    36MKP-1 /
    MKP1-thr-deph
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
    		• kinetics[16]
    Pathway No. : 478    		7.0000344explicit E-S complexSubstrate
    MAPK*

    Product
    MAPK-tyr
        See MKP1-tyr-deph
    37MKP-1 /
    MKP1-tyr-deph
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
    		• kinetics[17]
    Pathway No. : 484    		7.0000344explicit E-S complexSubstrate
    MAPK-tyr

    Product
    MAPK
        The original kinetics have been modified to obey the k2 = 4 * k3 rule, while keeping kcat and Km fixed. As noted in the NOTES, the only constraining data point is the time course of MAPK dephosphorylation, which this model satisfies. It would be nice to have more accurate estimates of rate consts and MKP-1 levels from the literature. Effective Km : 67 nM kcat = 1.43 umol/min/mg
    38MKP-1 /
    MKP1-thr-deph
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
    		• kinetics[17]
    Pathway No. : 484    		7.0000344explicit E-S complexSubstrate
    MAPK*

    Product
    MAPK-tyr
        See MKP1-tyr-deph
    39MKP-1 /
    MKP1-tyr-deph
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
    		• kinetics[18]
    Pathway No. : 490    		7.0000344explicit E-S complexSubstrate
    MAPK-tyr

    Product
    MAPK
        The original kinetics have been modified to obey the k2 = 4 * k3 rule, while keeping kcat and Km fixed. As noted in the NOTES, the only constraining data point is the time course of MAPK dephosphorylation, which this model satisfies. It would be nice to have more accurate estimates of rate consts and MKP-1 levels from the literature. Effective Km : 67 nM kcat = 1.43 umol/min/mg
    40MKP-1 /
    MKP1-thr-deph
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
    		• kinetics[18]
    Pathway No. : 490    		7.0000344explicit E-S complexSubstrate
    MAPK*

    Product
    MAPK-tyr
        See MKP1-tyr-deph
    41MKP-1 /
    MKP1-tyr-deph
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
    		• kinetics[19]
    Pathway No. : 496    		7.0000344explicit E-S complexSubstrate
    MAPK-tyr

    Product
    MAPK
        The original kinetics have been modified to obey the k2 = 4 * k3 rule, while keeping kcat and Km fixed. As noted in the NOTES, the only constraining data point is the time course of MAPK dephosphorylation, which this model satisfies. It would be nice to have more accurate estimates of rate consts and MKP-1 levels from the literature. Effective Km : 67 nM kcat = 1.43 umol/min/mg
    42MKP-1 /
    MKP1-thr-deph
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
    		• kinetics[19]
    Pathway No. : 496    		7.0000344explicit E-S complexSubstrate
    MAPK*

    Product
    MAPK-tyr
        See MKP1-tyr-deph
    43MKP-1 /
    MKP1-tyr-deph
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
    		• kinetics[20]
    Pathway No. : 502    		7.0000344explicit E-S complexSubstrate
    MAPK-tyr

    Product
    MAPK
        The original kinetics have been modified to obey the k2 = 4 * k3 rule, while keeping kcat and Km fixed. As noted in the NOTES, the only constraining data point is the time course of MAPK dephosphorylation, which this model satisfies. It would be nice to have more accurate estimates of rate consts and MKP-1 levels from the literature. Effective Km : 67 nM kcat = 1.43 umol/min/mg
    44MKP-1 /
    MKP1-thr-deph
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
    		• kinetics[20]
    Pathway No. : 502    		7.0000344explicit E-S complexSubstrate
    MAPK*

    Product
    MAPK-tyr
        See MKP1-tyr-deph
    45MKP-1 /
    MKP1-tyr-deph
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
    		• kinetics[21]
    Pathway No. : 508    		7.0000344explicit E-S complexSubstrate
    MAPK-tyr

    Product
    MAPK
        The original kinetics have been modified to obey the k2 = 4 * k3 rule, while keeping kcat and Km fixed. As noted in the NOTES, the only constraining data point is the time course of MAPK dephosphorylation, which this model satisfies. It would be nice to have more accurate estimates of rate consts and MKP-1 levels from the literature. Effective Km : 67 nM kcat = 1.43 umol/min/mg
    46MKP-1 /
    MKP1-thr-deph
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
    		• kinetics[21]
    Pathway No. : 508    		7.0000344explicit E-S complexSubstrate
    MAPK*

    Product
    MAPK-tyr
        See MKP1-tyr-deph
    47MKP-1 /
    MKP1-tyr-deph
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
    		• kinetics[22]
    Pathway No. : 514    		7.0000344explicit E-S complexSubstrate
    MAPK-tyr

    Product
    MAPK
        The original kinetics have been modified to obey the k2 = 4 * k3 rule, while keeping kcat and Km fixed. As noted in the NOTES, the only constraining data point is the time course of MAPK dephosphorylation, which this model satisfies. It would be nice to have more accurate estimates of rate consts and MKP-1 levels from the literature. Effective Km : 67 nM kcat = 1.43 umol/min/mg
    48MKP-1 /
    MKP1-thr-deph
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
    		• kinetics[22]
    Pathway No. : 514    		7.0000344explicit E-S complexSubstrate
    MAPK*

    Product
    MAPK-tyr
        See MKP1-tyr-deph
    49MKP-1 /
    MKP1-tyr-deph
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
    		• kinetics[23]
    Pathway No. : 520    		7.0000344explicit E-S complexSubstrate
    MAPK-tyr

    Product
    MAPK
        The original kinetics have been modified to obey the k2 = 4 * k3 rule, while keeping kcat and Km fixed. As noted in the NOTES, the only constraining data point is the time course of MAPK dephosphorylation, which this model satisfies. It would be nice to have more accurate estimates of rate consts and MKP-1 levels from the literature. Effective Km : 67 nM kcat = 1.43 umol/min/mg
    50MKP-1 /
    MKP1-thr-deph
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
    		• kinetics[23]
    Pathway No. : 520    		7.0000344explicit E-S complexSubstrate
    MAPK*

    Product
    MAPK-tyr
        See MKP1-tyr-deph

    MKP-1 acting as a Substrate in a reaction in      Ajay_bhalla_2007_ReacDiff1_1e-12 Network
    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 reaction are not consider.
     NameAccession NamePathway NameKfKbKdtauReagents
    1diff
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
  • Shared_Object_
    Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Pathway No. : 375
    		• 0.01
    (s^-1)    		0.01
    (s^-1)    		Keq = 1(uM)50secSubstrate
    MKP-1

    Product
    MKP-1
    2diff
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
  • Shared_Object_
    Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Pathway No. : 375
    		• 0.01
    (s^-1)    		0.01
    (s^-1)    		Keq = 1(uM)50secSubstrate
    MKP-1

    Product
    MKP-1
    3diff
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
  • Shared_Object_
    Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Pathway No. : 375
    		• 0.01
    (s^-1)    		0.01
    (s^-1)    		Keq = 1(uM)50secSubstrate
    MKP-1

    Product
    MKP-1
    4diff
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
  • Shared_Object_
    Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Pathway No. : 375
    		• 0.01
    (s^-1)    		0.01
    (s^-1)    		Keq = 1(uM)50secSubstrate
    MKP-1

    Product
    MKP-1
    5diff
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
  • Shared_Object_
    Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Pathway No. : 375
    		• 0.01
    (s^-1)    		0.01
    (s^-1)    		Keq = 1(uM)50secSubstrate
    MKP-1

    Product
    MKP-1
    6diff
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
  • Shared_Object_
    Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Pathway No. : 375
    		• 0.01
    (s^-1)    		0.01
    (s^-1)    		Keq = 1(uM)50secSubstrate
    MKP-1

    Product
    MKP-1
    7diff
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
  • Shared_Object_
    Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Pathway No. : 375
    		• 0.01
    (s^-1)    		0.01
    (s^-1)    		Keq = 1(uM)50secSubstrate
    MKP-1

    Product
    MKP-1
    8diff
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
  • Shared_Object_
    Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Pathway No. : 375
    		• 0.01
    (s^-1)    		0.01
    (s^-1)    		Keq = 1(uM)50secSubstrate
    MKP-1

    Product
    MKP-1
    9diff
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
  • Shared_Object_
    Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Pathway No. : 375
    		• 0.01
    (s^-1)    		0.01
    (s^-1)    		Keq = 1(uM)50secSubstrate
    MKP-1

    Product
    MKP-1
    10diff
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
  • Shared_Object_
    Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Pathway No. : 375
    		• 0.01
    (s^-1)    		0.01
    (s^-1)    		Keq = 1(uM)50secSubstrate
    MKP-1

    Product
    MKP-1
    11diff
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
  • Shared_Object_
    Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Pathway No. : 375
    		• 0.01
    (s^-1)    		0.01
    (s^-1)    		Keq = 1(uM)50secSubstrate
    MKP-1

    Product
    MKP-1
    12diff
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
  • Shared_Object_
    Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Pathway No. : 375
    		• 0.01
    (s^-1)    		0.01
    (s^-1)    		Keq = 1(uM)50secSubstrate
    MKP-1

    Product
    MKP-1
    13diff
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
  • Shared_Object_
    Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Pathway No. : 375
    		• 0.01
    (s^-1)    		0.01
    (s^-1)    		Keq = 1(uM)50secSubstrate
    MKP-1

    Product
    MKP-1
    14diff
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
  • Shared_Object_
    Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Pathway No. : 375
    		• 0.01
    (s^-1)    		0.01
    (s^-1)    		Keq = 1(uM)50secSubstrate
    MKP-1

    Product
    MKP-1
    15diff
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
  • Shared_Object_
    Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Pathway No. : 375
    		• 0.01
    (s^-1)    		0.01
    (s^-1)    		Keq = 1(uM)50secSubstrate
    MKP-1

    Product
    MKP-1
    16diff
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
  • Shared_Object_
    Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Pathway No. : 375
    		• 0.01
    (s^-1)    		0.01
    (s^-1)    		Keq = 1(uM)50secSubstrate
    MKP-1

    Product
    MKP-1
    17diff
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
  • Shared_Object_
    Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Pathway No. : 375
    		• 0.01
    (s^-1)    		0.01
    (s^-1)    		Keq = 1(uM)50secSubstrate
    MKP-1

    Product
    MKP-1
    18diff
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
  • Shared_Object_
    Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Pathway No. : 375
    		• 0.01
    (s^-1)    		0.01
    (s^-1)    		Keq = 1(uM)50secSubstrate
    MKP-1

    Product
    MKP-1
    19diff
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
  • Shared_Object_
    Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Pathway No. : 375
    		• 0.01
    (s^-1)    		0.01
    (s^-1)    		Keq = 1(uM)50secSubstrate
    MKP-1

    Product
    MKP-1
    20diff
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
  • Shared_Object_
    Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Pathway No. : 375
    		• 0.01
    (s^-1)    		0.01
    (s^-1)    		Keq = 1(uM)50secSubstrate
    MKP-1

    Product
    MKP-1
    21diff
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
  • Shared_Object_
    Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Pathway No. : 375
    		• 0.01
    (s^-1)    		0.01
    (s^-1)    		Keq = 1(uM)50secSubstrate
    MKP-1

    Product
    MKP-1
    22diff
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
  • Shared_Object_
    Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Pathway No. : 375
    		• 0.01
    (s^-1)    		0.01
    (s^-1)    		Keq = 1(uM)50secSubstrate
    MKP-1

    Product
    MKP-1
    23diff
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
  • Shared_Object_
    Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Pathway No. : 375
    		• 0.01
    (s^-1)    		0.01
    (s^-1)    		Keq = 1(uM)50secSubstrate
    MKP-1

    Product
    MKP-1
    24diff
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
  • Shared_Object_
    Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Pathway No. : 375
    		• 0.01
    (s^-1)    		0.01
    (s^-1)    		Keq = 1(uM)50secSubstrate
    MKP-1

    Product
    MKP-1

    MKP-1 acting as a Product in a reaction in      Ajay_bhalla_2007_ReacDiff1_1e-12 Network
    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 reaction are not consider.
     NameAccession NamePathway NameKfKbKdtauReagents
    1diff
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
  • Shared_Object_
    Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Pathway No. : 375
    		• 0.01
    (s^-1)    		0.01
    (s^-1)    		Keq = 1(uM)50secSubstrate
    MKP-1

    Product
    MKP-1
    2diff
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
  • Shared_Object_
    Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Pathway No. : 375
    		• 0.01
    (s^-1)    		0.01
    (s^-1)    		Keq = 1(uM)50secSubstrate
    MKP-1

    Product
    MKP-1
    3diff
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
  • Shared_Object_
    Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Pathway No. : 375
    		• 0.01
    (s^-1)    		0.01
    (s^-1)    		Keq = 1(uM)50secSubstrate
    MKP-1

    Product
    MKP-1
    4diff
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
  • Shared_Object_
    Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Pathway No. : 375
    		• 0.01
    (s^-1)    		0.01
    (s^-1)    		Keq = 1(uM)50secSubstrate
    MKP-1

    Product
    MKP-1
    5diff
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
  • Shared_Object_
    Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Pathway No. : 375
    		• 0.01
    (s^-1)    		0.01
    (s^-1)    		Keq = 1(uM)50secSubstrate
    MKP-1

    Product
    MKP-1
    6diff
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
  • Shared_Object_
    Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Pathway No. : 375
    		• 0.01
    (s^-1)    		0.01
    (s^-1)    		Keq = 1(uM)50secSubstrate
    MKP-1

    Product
    MKP-1
    7diff
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
  • Shared_Object_
    Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Pathway No. : 375
    		• 0.01
    (s^-1)    		0.01
    (s^-1)    		Keq = 1(uM)50secSubstrate
    MKP-1

    Product
    MKP-1
    8diff
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
  • Shared_Object_
    Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Pathway No. : 375
    		• 0.01
    (s^-1)    		0.01
    (s^-1)    		Keq = 1(uM)50secSubstrate
    MKP-1

    Product
    MKP-1
    9diff
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
  • Shared_Object_
    Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Pathway No. : 375
    		• 0.01
    (s^-1)    		0.01
    (s^-1)    		Keq = 1(uM)50secSubstrate
    MKP-1

    Product
    MKP-1
    10diff
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
  • Shared_Object_
    Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Pathway No. : 375
    		• 0.01
    (s^-1)    		0.01
    (s^-1)    		Keq = 1(uM)50secSubstrate
    MKP-1

    Product
    MKP-1
    11diff
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
  • Shared_Object_
    Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Pathway No. : 375
    		• 0.01
    (s^-1)    		0.01
    (s^-1)    		Keq = 1(uM)50secSubstrate
    MKP-1

    Product
    MKP-1
    12diff
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
  • Shared_Object_
    Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Pathway No. : 375
    		• 0.01
    (s^-1)    		0.01
    (s^-1)    		Keq = 1(uM)50secSubstrate
    MKP-1

    Product
    MKP-1
    13diff
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
  • Shared_Object_
    Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Pathway No. : 375
    		• 0.01
    (s^-1)    		0.01
    (s^-1)    		Keq = 1(uM)50secSubstrate
    MKP-1

    Product
    MKP-1
    14diff
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
  • Shared_Object_
    Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Pathway No. : 375
    		• 0.01
    (s^-1)    		0.01
    (s^-1)    		Keq = 1(uM)50secSubstrate
    MKP-1

    Product
    MKP-1
    15diff
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
  • Shared_Object_
    Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Pathway No. : 375
    		• 0.01
    (s^-1)    		0.01
    (s^-1)    		Keq = 1(uM)50secSubstrate
    MKP-1

    Product
    MKP-1
    16diff
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
  • Shared_Object_
    Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Pathway No. : 375
    		• 0.01
    (s^-1)    		0.01
    (s^-1)    		Keq = 1(uM)50secSubstrate
    MKP-1

    Product
    MKP-1
    17diff
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
  • Shared_Object_
    Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Pathway No. : 375
    		• 0.01
    (s^-1)    		0.01
    (s^-1)    		Keq = 1(uM)50secSubstrate
    MKP-1

    Product
    MKP-1
    18diff
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
  • Shared_Object_
    Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Pathway No. : 375
    		• 0.01
    (s^-1)    		0.01
    (s^-1)    		Keq = 1(uM)50secSubstrate
    MKP-1

    Product
    MKP-1
    19diff
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
  • Shared_Object_
    Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Pathway No. : 375
    		• 0.01
    (s^-1)    		0.01
    (s^-1)    		Keq = 1(uM)50secSubstrate
    MKP-1

    Product
    MKP-1
    20diff
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
  • Shared_Object_
    Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Pathway No. : 375
    		• 0.01
    (s^-1)    		0.01
    (s^-1)    		Keq = 1(uM)50secSubstrate
    MKP-1

    Product
    MKP-1
    21diff
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
  • Shared_Object_
    Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Pathway No. : 375
    		• 0.01
    (s^-1)    		0.01
    (s^-1)    		Keq = 1(uM)50secSubstrate
    MKP-1

    Product
    MKP-1
    22diff
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
  • Shared_Object_
    Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Pathway No. : 375
    		• 0.01
    (s^-1)    		0.01
    (s^-1)    		Keq = 1(uM)50secSubstrate
    MKP-1

    Product
    MKP-1
    23diff
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
  • Shared_Object_
    Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Pathway No. : 375
    		• 0.01
    (s^-1)    		0.01
    (s^-1)    		Keq = 1(uM)50secSubstrate
    MKP-1

    Product
    MKP-1
    24diff
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Accession No. : 81
  • Shared_Object_
    Ajay_bhalla_
    2007_ReacDiff1_
    1e-12
    Pathway No. : 375
    		• 0.01
    (s^-1)    		0.01
    (s^-1)    		Keq = 1(uM)50secSubstrate
    MKP-1

    Product
    MKP-1


    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.