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

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

Molecule Parameter List for MAPK-tyr

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
MAPK-tyr participated asMoleculeSum total ofEnzymeSubstrate of an enzymeProduct of an enzymeSubstrate in ReactionProduct in Reaction
No. of occurrences250050502424

Accession and Pathway Details
Accession NameAccession No.Accession TypePathway Link
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13
  • 82NetworkShared_Object_Ajay_Bhalla_2007_ReacDiff1_1e-13 
    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 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 MAPK 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-13_Fig4B which was used for the model to replicate Figure 4B from the paper.
    pkm_mapk22_diff_1e-13_Fig4H replicate Figure 4H.
    pkm_mapk22_diff_1e-13_Fig4I replicate Figure 4I.

    MAPK-tyr acting as a Molecule in  
    Ajay_Bhalla_2007_ReacDiff1_1e-13 Network
    NameAccession NamePathway NameInitial Conc.
    (uM)
    Volume
    (fL)
    Buffered
    MAPK-tyr
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • MAPK
    Pathway No. : 528
    01.5No
    Haystead et al FEBS Lett. 306(1) pp 17-22 show that phosphorylation is strictly sequential, first tyr185 then thr183.
    MAPK-tyr
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • MAPK
    Pathway No. : 535
    01.5No
    Haystead et al FEBS Lett. 306(1) pp 17-22 show that phosphorylation is strictly sequential, first tyr185 then thr183.
    MAPK-tyr
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • MAPK
    Pathway No. : 541
    01.5No
    Haystead et al FEBS Lett. 306(1) pp 17-22 show that phosphorylation is strictly sequential, first tyr185 then thr183.
    MAPK-tyr
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • MAPK
    Pathway No. : 547
    01.5No
    Haystead et al FEBS Lett. 306(1) pp 17-22 show that phosphorylation is strictly sequential, first tyr185 then thr183.
    MAPK-tyr
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • MAPK
    Pathway No. : 553
    01.5No
    Haystead et al FEBS Lett. 306(1) pp 17-22 show that phosphorylation is strictly sequential, first tyr185 then thr183.
    MAPK-tyr
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • MAPK
    Pathway No. : 559
    01.5No
    Haystead et al FEBS Lett. 306(1) pp 17-22 show that phosphorylation is strictly sequential, first tyr185 then thr183.
    MAPK-tyr
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • MAPK
    Pathway No. : 565
    01.5No
    Haystead et al FEBS Lett. 306(1) pp 17-22 show that phosphorylation is strictly sequential, first tyr185 then thr183.
    MAPK-tyr
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • MAPK
    Pathway No. : 571
    01.5No
    Haystead et al FEBS Lett. 306(1) pp 17-22 show that phosphorylation is strictly sequential, first tyr185 then thr183.
    MAPK-tyr
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • MAPK
    Pathway No. : 577
    01.5No
    Haystead et al FEBS Lett. 306(1) pp 17-22 show that phosphorylation is strictly sequential, first tyr185 then thr183.
    MAPK-tyr
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • MAPK
    Pathway No. : 583
    01.5No
    Haystead et al FEBS Lett. 306(1) pp 17-22 show that phosphorylation is strictly sequential, first tyr185 then thr183.
    MAPK-tyr
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • MAPK
    Pathway No. : 589
    01.5No
    Haystead et al FEBS Lett. 306(1) pp 17-22 show that phosphorylation is strictly sequential, first tyr185 then thr183.
    MAPK-tyr
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • MAPK
    Pathway No. : 595
    01.5No
    Haystead et al FEBS Lett. 306(1) pp 17-22 show that phosphorylation is strictly sequential, first tyr185 then thr183.
    MAPK-tyr
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • MAPK
    Pathway No. : 601
    01.5No
    Haystead et al FEBS Lett. 306(1) pp 17-22 show that phosphorylation is strictly sequential, first tyr185 then thr183.
    MAPK-tyr
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • MAPK
    Pathway No. : 607
    01.5No
    Haystead et al FEBS Lett. 306(1) pp 17-22 show that phosphorylation is strictly sequential, first tyr185 then thr183.
    MAPK-tyr
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • MAPK
    Pathway No. : 613
    01.5No
    Haystead et al FEBS Lett. 306(1) pp 17-22 show that phosphorylation is strictly sequential, first tyr185 then thr183.
    MAPK-tyr
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • MAPK
    Pathway No. : 619
    01.5No
    Haystead et al FEBS Lett. 306(1) pp 17-22 show that phosphorylation is strictly sequential, first tyr185 then thr183.
    MAPK-tyr
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • MAPK
    Pathway No. : 625
    01.5No
    Haystead et al FEBS Lett. 306(1) pp 17-22 show that phosphorylation is strictly sequential, first tyr185 then thr183.
    MAPK-tyr
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • MAPK
    Pathway No. : 631
    01.5No
    Haystead et al FEBS Lett. 306(1) pp 17-22 show that phosphorylation is strictly sequential, first tyr185 then thr183.
    MAPK-tyr
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • MAPK
    Pathway No. : 637
    01.5No
    Haystead et al FEBS Lett. 306(1) pp 17-22 show that phosphorylation is strictly sequential, first tyr185 then thr183.
    MAPK-tyr
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • MAPK
    Pathway No. : 643
    01.5No
    Haystead et al FEBS Lett. 306(1) pp 17-22 show that phosphorylation is strictly sequential, first tyr185 then thr183.
    MAPK-tyr
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • MAPK
    Pathway No. : 649
    01.5No
    Haystead et al FEBS Lett. 306(1) pp 17-22 show that phosphorylation is strictly sequential, first tyr185 then thr183.
    MAPK-tyr
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • MAPK
    Pathway No. : 655
    01.5No
    Haystead et al FEBS Lett. 306(1) pp 17-22 show that phosphorylation is strictly sequential, first tyr185 then thr183.
    MAPK-tyr
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • MAPK
    Pathway No. : 661
    01.5No
    Haystead et al FEBS Lett. 306(1) pp 17-22 show that phosphorylation is strictly sequential, first tyr185 then thr183.
    MAPK-tyr
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • MAPK
    Pathway No. : 667
    01.5No
    Haystead et al FEBS Lett. 306(1) pp 17-22 show that phosphorylation is strictly sequential, first tyr185 then thr183.
    MAPK-tyr
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • MAPK
    Pathway No. : 673
    01.5No
    Haystead et al FEBS Lett. 306(1) pp 17-22 show that phosphorylation is strictly sequential, first tyr185 then thr183.

    MAPK-tyr acting as a Substrate for an Enzyme in  
    Ajay_Bhalla_2007_ReacDiff1_1e-13 Network
     Enzyme Molecule /
    Enzyme Activity
    Accession NamePathway NameKm (uM)kcat (s^-1)RatioEnzyme TypeReagents
    1MAPKK*  /
    MAPKKthr
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • MAPK
    Pathway No. : 528
    0.04629640.34explicit E-S complexSubstrate
    MAPK-tyr

    Product
    MAPK*
        Rate consts same as for MAPKKtyr.
    2MKP-1  /
    MKP1-tyr-deph
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • Shared_Object_
    Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Pathway No. : 526
  • 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
    3MAPKK*  /
    MAPKKthr
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • MAPK
    Pathway No. : 535
    0.04629640.34explicit E-S complexSubstrate
    MAPK-tyr

    Product
    MAPK*
        Rate consts same as for MAPKKtyr.
    4MKP-1  /
    MKP1-tyr-deph
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • kinetics
    Pathway No. : 533
    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
    5MAPKK*  /
    MAPKKthr
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • MAPK
    Pathway No. : 541
    0.04629640.34explicit E-S complexSubstrate
    MAPK-tyr

    Product
    MAPK*
        Rate consts same as for MAPKKtyr.
    6MKP-1  /
    MKP1-tyr-deph
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • kinetics[1]
    Pathway No. : 539
    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
    7MAPKK*  /
    MAPKKthr
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • MAPK
    Pathway No. : 547
    0.04629640.34explicit E-S complexSubstrate
    MAPK-tyr

    Product
    MAPK*
        Rate consts same as for MAPKKtyr.
    8MKP-1  /
    MKP1-tyr-deph
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • kinetics[2]
    Pathway No. : 545
    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
    9MAPKK*  /
    MAPKKthr
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • MAPK
    Pathway No. : 553
    0.04629640.34explicit E-S complexSubstrate
    MAPK-tyr

    Product
    MAPK*
        Rate consts same as for MAPKKtyr.
    10MKP-1  /
    MKP1-tyr-deph
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • kinetics[3]
    Pathway No. : 551
    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
    11MAPKK*  /
    MAPKKthr
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • MAPK
    Pathway No. : 559
    0.04629640.34explicit E-S complexSubstrate
    MAPK-tyr

    Product
    MAPK*
        Rate consts same as for MAPKKtyr.
    12MKP-1  /
    MKP1-tyr-deph
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • kinetics[4]
    Pathway No. : 557
    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
    13MAPKK*  /
    MAPKKthr
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • MAPK
    Pathway No. : 565
    0.04629640.34explicit E-S complexSubstrate
    MAPK-tyr

    Product
    MAPK*
        Rate consts same as for MAPKKtyr.
    14MKP-1  /
    MKP1-tyr-deph
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • kinetics[5]
    Pathway No. : 563
    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
    15MAPKK*  /
    MAPKKthr
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • MAPK
    Pathway No. : 571
    0.04629640.34explicit E-S complexSubstrate
    MAPK-tyr

    Product
    MAPK*
        Rate consts same as for MAPKKtyr.
    16MKP-1  /
    MKP1-tyr-deph
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • kinetics[6]
    Pathway No. : 567
    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
    17MAPKK*  /
    MAPKKthr
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • MAPK
    Pathway No. : 577
    0.04629640.34explicit E-S complexSubstrate
    MAPK-tyr

    Product
    MAPK*
        Rate consts same as for MAPKKtyr.
    18MKP-1  /
    MKP1-tyr-deph
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • kinetics[7]
    Pathway No. : 575
    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
    19MAPKK*  /
    MAPKKthr
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • MAPK
    Pathway No. : 583
    0.04629640.34explicit E-S complexSubstrate
    MAPK-tyr

    Product
    MAPK*
        Rate consts same as for MAPKKtyr.
    20MKP-1  /
    MKP1-tyr-deph
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • kinetics[8]
    Pathway No. : 581
    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
    21MAPKK*  /
    MAPKKthr
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • MAPK
    Pathway No. : 589
    0.04629640.34explicit E-S complexSubstrate
    MAPK-tyr

    Product
    MAPK*
        Rate consts same as for MAPKKtyr.
    22MKP-1  /
    MKP1-tyr-deph
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • kinetics[9]
    Pathway No. : 587
    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
    23MAPKK*  /
    MAPKKthr
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • MAPK
    Pathway No. : 595
    0.04629640.34explicit E-S complexSubstrate
    MAPK-tyr

    Product
    MAPK*
        Rate consts same as for MAPKKtyr.
    24MKP-1  /
    MKP1-tyr-deph
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • kinetics[10]
    Pathway No. : 593
    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
    25MAPKK*  /
    MAPKKthr
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • MAPK
    Pathway No. : 601
    0.04629640.34explicit E-S complexSubstrate
    MAPK-tyr

    Product
    MAPK*
        Rate consts same as for MAPKKtyr.
    26MKP-1  /
    MKP1-tyr-deph
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • kinetics[11]
    Pathway No. : 599
    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
    27MAPKK*  /
    MAPKKthr
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • MAPK
    Pathway No. : 607
    0.04629640.34explicit E-S complexSubstrate
    MAPK-tyr

    Product
    MAPK*
        Rate consts same as for MAPKKtyr.
    28MKP-1  /
    MKP1-tyr-deph
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • kinetics[12]
    Pathway No. : 605
    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
    29MAPKK*  /
    MAPKKthr
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • MAPK
    Pathway No. : 613
    0.04629640.34explicit E-S complexSubstrate
    MAPK-tyr

    Product
    MAPK*
        Rate consts same as for MAPKKtyr.
    30MKP-1  /
    MKP1-tyr-deph
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • kinetics[13]
    Pathway No. : 611
    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
    31MAPKK*  /
    MAPKKthr
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • MAPK
    Pathway No. : 619
    0.04629640.34explicit E-S complexSubstrate
    MAPK-tyr

    Product
    MAPK*
        Rate consts same as for MAPKKtyr.
    32MKP-1  /
    MKP1-tyr-deph
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • kinetics[14]
    Pathway No. : 617
    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
    33MAPKK*  /
    MAPKKthr
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • MAPK
    Pathway No. : 625
    0.04629640.34explicit E-S complexSubstrate
    MAPK-tyr

    Product
    MAPK*
        Rate consts same as for MAPKKtyr.
    34MKP-1  /
    MKP1-tyr-deph
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • kinetics[15]
    Pathway No. : 623
    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
    35MAPKK*  /
    MAPKKthr
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • MAPK
    Pathway No. : 631
    0.04629640.34explicit E-S complexSubstrate
    MAPK-tyr

    Product
    MAPK*
        Rate consts same as for MAPKKtyr.
    36MKP-1  /
    MKP1-tyr-deph
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • kinetics[16]
    Pathway No. : 629
    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
    37MAPKK*  /
    MAPKKthr
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • MAPK
    Pathway No. : 637
    0.04629640.34explicit E-S complexSubstrate
    MAPK-tyr

    Product
    MAPK*
        Rate consts same as for MAPKKtyr.
    38MKP-1  /
    MKP1-tyr-deph
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • kinetics[17]
    Pathway No. : 635
    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
    39MAPKK*  /
    MAPKKthr
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • MAPK
    Pathway No. : 643
    0.04629640.34explicit E-S complexSubstrate
    MAPK-tyr

    Product
    MAPK*
        Rate consts same as for MAPKKtyr.
    40MKP-1  /
    MKP1-tyr-deph
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • kinetics[18]
    Pathway No. : 641
    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
    41MAPKK*  /
    MAPKKthr
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • MAPK
    Pathway No. : 649
    0.04629640.34explicit E-S complexSubstrate
    MAPK-tyr

    Product
    MAPK*
        Rate consts same as for MAPKKtyr.
    42MKP-1  /
    MKP1-tyr-deph
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • kinetics[19]
    Pathway No. : 647
    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
    43MAPKK*  /
    MAPKKthr
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • MAPK
    Pathway No. : 655
    0.04629640.34explicit E-S complexSubstrate
    MAPK-tyr

    Product
    MAPK*
        Rate consts same as for MAPKKtyr.
    44MKP-1  /
    MKP1-tyr-deph
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • kinetics[20]
    Pathway No. : 653
    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
    45MAPKK*  /
    MAPKKthr
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • MAPK
    Pathway No. : 661
    0.04629640.34explicit E-S complexSubstrate
    MAPK-tyr

    Product
    MAPK*
        Rate consts same as for MAPKKtyr.
    46MKP-1  /
    MKP1-tyr-deph
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • kinetics[21]
    Pathway No. : 659
    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
    47MAPKK*  /
    MAPKKthr
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • MAPK
    Pathway No. : 667
    0.04629640.34explicit E-S complexSubstrate
    MAPK-tyr

    Product
    MAPK*
        Rate consts same as for MAPKKtyr.
    48MKP-1  /
    MKP1-tyr-deph
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • kinetics[22]
    Pathway No. : 665
    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
    49MAPKK*  /
    MAPKKthr
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • MAPK
    Pathway No. : 673
    0.04629640.34explicit E-S complexSubstrate
    MAPK-tyr

    Product
    MAPK*
        Rate consts same as for MAPKKtyr.
    50MKP-1  /
    MKP1-tyr-deph
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • kinetics[23]
    Pathway No. : 671
    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

    MAPK-tyr acting as a Product of an Enzyme in  
    Ajay_Bhalla_2007_ReacDiff1_1e-13 Network
     Enzyme Molecule /
    Enzyme Activity
    Accession NamePathway NameKm (uM)kcat (s^-1)RatioEnzyme TypeReagents
    1MAPKK*  /
    MAPKKtyr
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • MAPK
    Pathway No. : 528
    0.04629640.34explicit E-S complexSubstrate
    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, scale to get k2=0.6. k1=0.75/46.6nM=2.7e-5
    2MKP-1  /
    MKP1-thr-deph
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • Shared_Object_
    Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Pathway No. : 526
  • 7.0000344explicit E-S complexSubstrate
    MAPK*

    Product
    MAPK-tyr
        See MKP1-tyr-deph
    3MAPKK*  /
    MAPKKtyr
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • MAPK
    Pathway No. : 535
    0.04629640.34explicit E-S complexSubstrate
    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, scale to get k2=0.6. k1=0.75/46.6nM=2.7e-5
    4MKP-1  /
    MKP1-thr-deph
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • kinetics
    Pathway No. : 533
    7.0000344explicit E-S complexSubstrate
    MAPK*

    Product
    MAPK-tyr
        See MKP1-tyr-deph
    5MAPKK*  /
    MAPKKtyr
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • MAPK
    Pathway No. : 541
    0.04629640.34explicit E-S complexSubstrate
    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, scale to get k2=0.6. k1=0.75/46.6nM=2.7e-5
    6MKP-1  /
    MKP1-thr-deph
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • kinetics[1]
    Pathway No. : 539
    7.0000344explicit E-S complexSubstrate
    MAPK*

    Product
    MAPK-tyr
        See MKP1-tyr-deph
    7MAPKK*  /
    MAPKKtyr
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • MAPK
    Pathway No. : 547
    0.04629640.34explicit E-S complexSubstrate
    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, scale to get k2=0.6. k1=0.75/46.6nM=2.7e-5
    8MKP-1  /
    MKP1-thr-deph
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • kinetics[2]
    Pathway No. : 545
    7.0000344explicit E-S complexSubstrate
    MAPK*

    Product
    MAPK-tyr
        See MKP1-tyr-deph
    9MAPKK*  /
    MAPKKtyr
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • MAPK
    Pathway No. : 553
    0.04629640.34explicit E-S complexSubstrate
    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, scale to get k2=0.6. k1=0.75/46.6nM=2.7e-5
    10MKP-1  /
    MKP1-thr-deph
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • kinetics[3]
    Pathway No. : 551
    7.0000344explicit E-S complexSubstrate
    MAPK*

    Product
    MAPK-tyr
        See MKP1-tyr-deph
    11MAPKK*  /
    MAPKKtyr
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • MAPK
    Pathway No. : 559
    0.04629640.34explicit E-S complexSubstrate
    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, scale to get k2=0.6. k1=0.75/46.6nM=2.7e-5
    12MKP-1  /
    MKP1-thr-deph
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • kinetics[4]
    Pathway No. : 557
    7.0000344explicit E-S complexSubstrate
    MAPK*

    Product
    MAPK-tyr
        See MKP1-tyr-deph
    13MAPKK*  /
    MAPKKtyr
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • MAPK
    Pathway No. : 565
    0.04629640.34explicit E-S complexSubstrate
    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, scale to get k2=0.6. k1=0.75/46.6nM=2.7e-5
    14MKP-1  /
    MKP1-thr-deph
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • kinetics[5]
    Pathway No. : 563
    7.0000344explicit E-S complexSubstrate
    MAPK*

    Product
    MAPK-tyr
        See MKP1-tyr-deph
    15MAPKK*  /
    MAPKKtyr
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • MAPK
    Pathway No. : 571
    0.04629640.34explicit E-S complexSubstrate
    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, scale to get k2=0.6. k1=0.75/46.6nM=2.7e-5
    16MKP-1  /
    MKP1-thr-deph
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • kinetics[6]
    Pathway No. : 567
    7.0000344explicit E-S complexSubstrate
    MAPK*

    Product
    MAPK-tyr
        See MKP1-tyr-deph
    17MAPKK*  /
    MAPKKtyr
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • MAPK
    Pathway No. : 577
    0.04629640.34explicit E-S complexSubstrate
    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, scale to get k2=0.6. k1=0.75/46.6nM=2.7e-5
    18MKP-1  /
    MKP1-thr-deph
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • kinetics[7]
    Pathway No. : 575
    7.0000344explicit E-S complexSubstrate
    MAPK*

    Product
    MAPK-tyr
        See MKP1-tyr-deph
    19MAPKK*  /
    MAPKKtyr
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • MAPK
    Pathway No. : 583
    0.04629640.34explicit E-S complexSubstrate
    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, scale to get k2=0.6. k1=0.75/46.6nM=2.7e-5
    20MKP-1  /
    MKP1-thr-deph
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • kinetics[8]
    Pathway No. : 581
    7.0000344explicit E-S complexSubstrate
    MAPK*

    Product
    MAPK-tyr
        See MKP1-tyr-deph
    21MAPKK*  /
    MAPKKtyr
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • MAPK
    Pathway No. : 589
    0.04629640.34explicit E-S complexSubstrate
    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, scale to get k2=0.6. k1=0.75/46.6nM=2.7e-5
    22MKP-1  /
    MKP1-thr-deph
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • kinetics[9]
    Pathway No. : 587
    7.0000344explicit E-S complexSubstrate
    MAPK*

    Product
    MAPK-tyr
        See MKP1-tyr-deph
    23MAPKK*  /
    MAPKKtyr
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • MAPK
    Pathway No. : 595
    0.04629640.34explicit E-S complexSubstrate
    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, scale to get k2=0.6. k1=0.75/46.6nM=2.7e-5
    24MKP-1  /
    MKP1-thr-deph
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • kinetics[10]
    Pathway No. : 593
    7.0000344explicit E-S complexSubstrate
    MAPK*

    Product
    MAPK-tyr
        See MKP1-tyr-deph
    25MAPKK*  /
    MAPKKtyr
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • MAPK
    Pathway No. : 601
    0.04629640.34explicit E-S complexSubstrate
    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, scale to get k2=0.6. k1=0.75/46.6nM=2.7e-5
    26MKP-1  /
    MKP1-thr-deph
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • kinetics[11]
    Pathway No. : 599
    7.0000344explicit E-S complexSubstrate
    MAPK*

    Product
    MAPK-tyr
        See MKP1-tyr-deph
    27MAPKK*  /
    MAPKKtyr
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • MAPK
    Pathway No. : 607
    0.04629640.34explicit E-S complexSubstrate
    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, scale to get k2=0.6. k1=0.75/46.6nM=2.7e-5
    28MKP-1  /
    MKP1-thr-deph
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • kinetics[12]
    Pathway No. : 605
    7.0000344explicit E-S complexSubstrate
    MAPK*

    Product
    MAPK-tyr
        See MKP1-tyr-deph
    29MAPKK*  /
    MAPKKtyr
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • MAPK
    Pathway No. : 613
    0.04629640.34explicit E-S complexSubstrate
    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, scale to get k2=0.6. k1=0.75/46.6nM=2.7e-5
    30MKP-1  /
    MKP1-thr-deph
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • kinetics[13]
    Pathway No. : 611
    7.0000344explicit E-S complexSubstrate
    MAPK*

    Product
    MAPK-tyr
        See MKP1-tyr-deph
    31MAPKK*  /
    MAPKKtyr
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • MAPK
    Pathway No. : 619
    0.04629640.34explicit E-S complexSubstrate
    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, scale to get k2=0.6. k1=0.75/46.6nM=2.7e-5
    32MKP-1  /
    MKP1-thr-deph
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • kinetics[14]
    Pathway No. : 617
    7.0000344explicit E-S complexSubstrate
    MAPK*

    Product
    MAPK-tyr
        See MKP1-tyr-deph
    33MAPKK*  /
    MAPKKtyr
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • MAPK
    Pathway No. : 625
    0.04629640.34explicit E-S complexSubstrate
    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, scale to get k2=0.6. k1=0.75/46.6nM=2.7e-5
    34MKP-1  /
    MKP1-thr-deph
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • kinetics[15]
    Pathway No. : 623
    7.0000344explicit E-S complexSubstrate
    MAPK*

    Product
    MAPK-tyr
        See MKP1-tyr-deph
    35MAPKK*  /
    MAPKKtyr
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • MAPK
    Pathway No. : 631
    0.04629640.34explicit E-S complexSubstrate
    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, scale to get k2=0.6. k1=0.75/46.6nM=2.7e-5
    36MKP-1  /
    MKP1-thr-deph
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • kinetics[16]
    Pathway No. : 629
    7.0000344explicit E-S complexSubstrate
    MAPK*

    Product
    MAPK-tyr
        See MKP1-tyr-deph
    37MAPKK*  /
    MAPKKtyr
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • MAPK
    Pathway No. : 637
    0.04629640.34explicit E-S complexSubstrate
    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, scale to get k2=0.6. k1=0.75/46.6nM=2.7e-5
    38MKP-1  /
    MKP1-thr-deph
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • kinetics[17]
    Pathway No. : 635
    7.0000344explicit E-S complexSubstrate
    MAPK*

    Product
    MAPK-tyr
        See MKP1-tyr-deph
    39MAPKK*  /
    MAPKKtyr
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • MAPK
    Pathway No. : 643
    0.04629640.34explicit E-S complexSubstrate
    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, scale to get k2=0.6. k1=0.75/46.6nM=2.7e-5
    40MKP-1  /
    MKP1-thr-deph
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • kinetics[18]
    Pathway No. : 641
    7.0000344explicit E-S complexSubstrate
    MAPK*

    Product
    MAPK-tyr
        See MKP1-tyr-deph
    41MAPKK*  /
    MAPKKtyr
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • MAPK
    Pathway No. : 649
    0.04629640.34explicit E-S complexSubstrate
    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, scale to get k2=0.6. k1=0.75/46.6nM=2.7e-5
    42MKP-1  /
    MKP1-thr-deph
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • kinetics[19]
    Pathway No. : 647
    7.0000344explicit E-S complexSubstrate
    MAPK*

    Product
    MAPK-tyr
        See MKP1-tyr-deph
    43MAPKK*  /
    MAPKKtyr
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • MAPK
    Pathway No. : 655
    0.04629640.34explicit E-S complexSubstrate
    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, scale to get k2=0.6. k1=0.75/46.6nM=2.7e-5
    44MKP-1  /
    MKP1-thr-deph
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • kinetics[20]
    Pathway No. : 653
    7.0000344explicit E-S complexSubstrate
    MAPK*

    Product
    MAPK-tyr
        See MKP1-tyr-deph
    45MAPKK*  /
    MAPKKtyr
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • MAPK
    Pathway No. : 661
    0.04629640.34explicit E-S complexSubstrate
    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, scale to get k2=0.6. k1=0.75/46.6nM=2.7e-5
    46MKP-1  /
    MKP1-thr-deph
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • kinetics[21]
    Pathway No. : 659
    7.0000344explicit E-S complexSubstrate
    MAPK*

    Product
    MAPK-tyr
        See MKP1-tyr-deph
    47MAPKK*  /
    MAPKKtyr
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • MAPK
    Pathway No. : 667
    0.04629640.34explicit E-S complexSubstrate
    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, scale to get k2=0.6. k1=0.75/46.6nM=2.7e-5
    48MKP-1  /
    MKP1-thr-deph
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • kinetics[22]
    Pathway No. : 665
    7.0000344explicit E-S complexSubstrate
    MAPK*

    Product
    MAPK-tyr
        See MKP1-tyr-deph
    49MAPKK*  /
    MAPKKtyr
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • MAPK
    Pathway No. : 673
    0.04629640.34explicit E-S complexSubstrate
    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, scale to get k2=0.6. k1=0.75/46.6nM=2.7e-5
    50MKP-1  /
    MKP1-thr-deph
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • kinetics[23]
    Pathway No. : 671
    7.0000344explicit E-S complexSubstrate
    MAPK*

    Product
    MAPK-tyr
        See MKP1-tyr-deph

    MAPK-tyr acting as a Substrate in a reaction in  
    Ajay_Bhalla_2007_ReacDiff1_1e-13 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-13

    Accession No. : 82
  • Shared_Object_
    Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Pathway No. : 526
  • 0.001
    (s^-1)
    0.001
    (s^-1)
    Keq = 1(uM)500secSubstrate
    MAPK-tyr

    Product
    MAPK-tyr
    2diff
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • Shared_Object_
    Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Pathway No. : 526
  • 0.001
    (s^-1)
    0.001
    (s^-1)
    Keq = 1(uM)500secSubstrate
    MAPK-tyr

    Product
    MAPK-tyr
    3diff
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • Shared_Object_
    Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Pathway No. : 526
  • 0.001
    (s^-1)
    0.001
    (s^-1)
    Keq = 1(uM)500secSubstrate
    MAPK-tyr

    Product
    MAPK-tyr
    4diff
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • Shared_Object_
    Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Pathway No. : 526
  • 0.001
    (s^-1)
    0.001
    (s^-1)
    Keq = 1(uM)500secSubstrate
    MAPK-tyr

    Product
    MAPK-tyr
    5diff
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • Shared_Object_
    Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Pathway No. : 526
  • 0.001
    (s^-1)
    0.001
    (s^-1)
    Keq = 1(uM)500secSubstrate
    MAPK-tyr

    Product
    MAPK-tyr
    6diff
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • Shared_Object_
    Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Pathway No. : 526
  • 0.001
    (s^-1)
    0.001
    (s^-1)
    Keq = 1(uM)500secSubstrate
    MAPK-tyr

    Product
    MAPK-tyr
    7diff
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • Shared_Object_
    Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Pathway No. : 526
  • 0.001
    (s^-1)
    0.001
    (s^-1)
    Keq = 1(uM)500secSubstrate
    MAPK-tyr

    Product
    MAPK-tyr
    8diff
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • Shared_Object_
    Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Pathway No. : 526
  • 0.001
    (s^-1)
    0.001
    (s^-1)
    Keq = 1(uM)500secSubstrate
    MAPK-tyr

    Product
    MAPK-tyr
    9diff
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • Shared_Object_
    Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Pathway No. : 526
  • 0.001
    (s^-1)
    0.001
    (s^-1)
    Keq = 1(uM)500secSubstrate
    MAPK-tyr

    Product
    MAPK-tyr
    10diff
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • Shared_Object_
    Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Pathway No. : 526
  • 0.001
    (s^-1)
    0.001
    (s^-1)
    Keq = 1(uM)500secSubstrate
    MAPK-tyr

    Product
    MAPK-tyr
    11diff
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • Shared_Object_
    Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Pathway No. : 526
  • 0.001
    (s^-1)
    0.001
    (s^-1)
    Keq = 1(uM)500secSubstrate
    MAPK-tyr

    Product
    MAPK-tyr
    12diff
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • Shared_Object_
    Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Pathway No. : 526
  • 0.001
    (s^-1)
    0.001
    (s^-1)
    Keq = 1(uM)500secSubstrate
    MAPK-tyr

    Product
    MAPK-tyr
    13diff
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • Shared_Object_
    Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Pathway No. : 526
  • 0.001
    (s^-1)
    0.001
    (s^-1)
    Keq = 1(uM)500secSubstrate
    MAPK-tyr

    Product
    MAPK-tyr
    14diff
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • Shared_Object_
    Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Pathway No. : 526
  • 0.001
    (s^-1)
    0.001
    (s^-1)
    Keq = 1(uM)500secSubstrate
    MAPK-tyr

    Product
    MAPK-tyr
    15diff
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • Shared_Object_
    Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Pathway No. : 526
  • 0.001
    (s^-1)
    0.001
    (s^-1)
    Keq = 1(uM)500secSubstrate
    MAPK-tyr

    Product
    MAPK-tyr
    16diff
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • Shared_Object_
    Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Pathway No. : 526
  • 0.001
    (s^-1)
    0.001
    (s^-1)
    Keq = 1(uM)500secSubstrate
    MAPK-tyr

    Product
    MAPK-tyr
    17diff
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • Shared_Object_
    Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Pathway No. : 526
  • 0.001
    (s^-1)
    0.001
    (s^-1)
    Keq = 1(uM)500secSubstrate
    MAPK-tyr

    Product
    MAPK-tyr
    18diff
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • Shared_Object_
    Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Pathway No. : 526
  • 0.001
    (s^-1)
    0.001
    (s^-1)
    Keq = 1(uM)500secSubstrate
    MAPK-tyr

    Product
    MAPK-tyr
    19diff
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • Shared_Object_
    Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Pathway No. : 526
  • 0.001
    (s^-1)
    0.001
    (s^-1)
    Keq = 1(uM)500secSubstrate
    MAPK-tyr

    Product
    MAPK-tyr
    20diff
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • Shared_Object_
    Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Pathway No. : 526
  • 0.001
    (s^-1)
    0.001
    (s^-1)
    Keq = 1(uM)500secSubstrate
    MAPK-tyr

    Product
    MAPK-tyr
    21diff
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • Shared_Object_
    Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Pathway No. : 526
  • 0.001
    (s^-1)
    0.001
    (s^-1)
    Keq = 1(uM)500secSubstrate
    MAPK-tyr

    Product
    MAPK-tyr
    22diff
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • Shared_Object_
    Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Pathway No. : 526
  • 0.001
    (s^-1)
    0.001
    (s^-1)
    Keq = 1(uM)500secSubstrate
    MAPK-tyr

    Product
    MAPK-tyr
    23diff
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • Shared_Object_
    Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Pathway No. : 526
  • 0.001
    (s^-1)
    0.001
    (s^-1)
    Keq = 1(uM)500secSubstrate
    MAPK-tyr

    Product
    MAPK-tyr
    24diff
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • Shared_Object_
    Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Pathway No. : 526
  • 0.001
    (s^-1)
    0.001
    (s^-1)
    Keq = 1(uM)500secSubstrate
    MAPK-tyr

    Product
    MAPK-tyr

    MAPK-tyr acting as a Product in a reaction in  
    Ajay_Bhalla_2007_ReacDiff1_1e-13 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-13

    Accession No. : 82
  • Shared_Object_
    Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Pathway No. : 526
  • 0.001
    (s^-1)
    0.001
    (s^-1)
    Keq = 1(uM)500secSubstrate
    MAPK-tyr

    Product
    MAPK-tyr
    2diff
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • Shared_Object_
    Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Pathway No. : 526
  • 0.001
    (s^-1)
    0.001
    (s^-1)
    Keq = 1(uM)500secSubstrate
    MAPK-tyr

    Product
    MAPK-tyr
    3diff
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • Shared_Object_
    Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Pathway No. : 526
  • 0.001
    (s^-1)
    0.001
    (s^-1)
    Keq = 1(uM)500secSubstrate
    MAPK-tyr

    Product
    MAPK-tyr
    4diff
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • Shared_Object_
    Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Pathway No. : 526
  • 0.001
    (s^-1)
    0.001
    (s^-1)
    Keq = 1(uM)500secSubstrate
    MAPK-tyr

    Product
    MAPK-tyr
    5diff
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • Shared_Object_
    Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Pathway No. : 526
  • 0.001
    (s^-1)
    0.001
    (s^-1)
    Keq = 1(uM)500secSubstrate
    MAPK-tyr

    Product
    MAPK-tyr
    6diff
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • Shared_Object_
    Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Pathway No. : 526
  • 0.001
    (s^-1)
    0.001
    (s^-1)
    Keq = 1(uM)500secSubstrate
    MAPK-tyr

    Product
    MAPK-tyr
    7diff
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • Shared_Object_
    Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Pathway No. : 526
  • 0.001
    (s^-1)
    0.001
    (s^-1)
    Keq = 1(uM)500secSubstrate
    MAPK-tyr

    Product
    MAPK-tyr
    8diff
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • Shared_Object_
    Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Pathway No. : 526
  • 0.001
    (s^-1)
    0.001
    (s^-1)
    Keq = 1(uM)500secSubstrate
    MAPK-tyr

    Product
    MAPK-tyr
    9diff
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • Shared_Object_
    Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Pathway No. : 526
  • 0.001
    (s^-1)
    0.001
    (s^-1)
    Keq = 1(uM)500secSubstrate
    MAPK-tyr

    Product
    MAPK-tyr
    10diff
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • Shared_Object_
    Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Pathway No. : 526
  • 0.001
    (s^-1)
    0.001
    (s^-1)
    Keq = 1(uM)500secSubstrate
    MAPK-tyr

    Product
    MAPK-tyr
    11diff
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • Shared_Object_
    Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Pathway No. : 526
  • 0.001
    (s^-1)
    0.001
    (s^-1)
    Keq = 1(uM)500secSubstrate
    MAPK-tyr

    Product
    MAPK-tyr
    12diff
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • Shared_Object_
    Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Pathway No. : 526
  • 0.001
    (s^-1)
    0.001
    (s^-1)
    Keq = 1(uM)500secSubstrate
    MAPK-tyr

    Product
    MAPK-tyr
    13diff
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • Shared_Object_
    Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Pathway No. : 526
  • 0.001
    (s^-1)
    0.001
    (s^-1)
    Keq = 1(uM)500secSubstrate
    MAPK-tyr

    Product
    MAPK-tyr
    14diff
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • Shared_Object_
    Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Pathway No. : 526
  • 0.001
    (s^-1)
    0.001
    (s^-1)
    Keq = 1(uM)500secSubstrate
    MAPK-tyr

    Product
    MAPK-tyr
    15diff
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • Shared_Object_
    Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Pathway No. : 526
  • 0.001
    (s^-1)
    0.001
    (s^-1)
    Keq = 1(uM)500secSubstrate
    MAPK-tyr

    Product
    MAPK-tyr
    16diff
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • Shared_Object_
    Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Pathway No. : 526
  • 0.001
    (s^-1)
    0.001
    (s^-1)
    Keq = 1(uM)500secSubstrate
    MAPK-tyr

    Product
    MAPK-tyr
    17diff
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • Shared_Object_
    Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Pathway No. : 526
  • 0.001
    (s^-1)
    0.001
    (s^-1)
    Keq = 1(uM)500secSubstrate
    MAPK-tyr

    Product
    MAPK-tyr
    18diff
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • Shared_Object_
    Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Pathway No. : 526
  • 0.001
    (s^-1)
    0.001
    (s^-1)
    Keq = 1(uM)500secSubstrate
    MAPK-tyr

    Product
    MAPK-tyr
    19diff
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • Shared_Object_
    Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Pathway No. : 526
  • 0.001
    (s^-1)
    0.001
    (s^-1)
    Keq = 1(uM)500secSubstrate
    MAPK-tyr

    Product
    MAPK-tyr
    20diff
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • Shared_Object_
    Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Pathway No. : 526
  • 0.001
    (s^-1)
    0.001
    (s^-1)
    Keq = 1(uM)500secSubstrate
    MAPK-tyr

    Product
    MAPK-tyr
    21diff
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • Shared_Object_
    Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Pathway No. : 526
  • 0.001
    (s^-1)
    0.001
    (s^-1)
    Keq = 1(uM)500secSubstrate
    MAPK-tyr

    Product
    MAPK-tyr
    22diff
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • Shared_Object_
    Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Pathway No. : 526
  • 0.001
    (s^-1)
    0.001
    (s^-1)
    Keq = 1(uM)500secSubstrate
    MAPK-tyr

    Product
    MAPK-tyr
    23diff
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • Shared_Object_
    Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Pathway No. : 526
  • 0.001
    (s^-1)
    0.001
    (s^-1)
    Keq = 1(uM)500secSubstrate
    MAPK-tyr

    Product
    MAPK-tyr
    24diff
  • Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Accession No. : 82
  • Shared_Object_
    Ajay_Bhalla_
    2007_ReacDiff1_
    1e-13

    Pathway No. : 526
  • 0.001
    (s^-1)
    0.001
    (s^-1)
    Keq = 1(uM)500secSubstrate
    MAPK-tyr

    Product
    MAPK-tyr



    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.