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Molecule Parameter List for craf-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
craf-1* participated asMoleculeSum total ofEnzymeSubstrate of an enzymeProduct of an enzymeSubstrate in ReactionProduct in Reaction
No. of occurrences25005050250

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

    craf-1* acting as a Molecule in  
    Ajay_bhalla_2007_ReacDiff1_1e-12 Network
    NameAccession NamePathway NameInitial Conc.
    (uM)
    Volume
    (fL)
    Buffered
    craf-1*
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • MAPK
    Pathway No. : 377
    01.5No
    craf-1*
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • MAPK
    Pathway No. : 384
    01.5No
    craf-1*
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • MAPK
    Pathway No. : 390
    01.5No
    craf-1*
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • MAPK
    Pathway No. : 396
    01.5No
    craf-1*
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • MAPK
    Pathway No. : 403
    01.5No
    craf-1*
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • MAPK
    Pathway No. : 409
    01.5No
    craf-1*
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • MAPK
    Pathway No. : 415
    01.5No
    craf-1*
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • MAPK
    Pathway No. : 421
    01.5No
    craf-1*
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • MAPK
    Pathway No. : 402
    01.5No
    craf-1*
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • MAPK
    Pathway No. : 432
    01.5No
    craf-1*
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • MAPK
    Pathway No. : 438
    01.5No
    craf-1*
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • MAPK
    Pathway No. : 444
    01.5No
    craf-1*
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • MAPK
    Pathway No. : 450
    01.5No
    craf-1*
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • MAPK
    Pathway No. : 456
    01.5No
    craf-1*
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • MAPK
    Pathway No. : 462
    01.5No
    craf-1*
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • MAPK
    Pathway No. : 468
    01.5No
    craf-1*
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • MAPK
    Pathway No. : 474
    01.5No
    craf-1*
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • MAPK
    Pathway No. : 480
    01.5No
    craf-1*
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • MAPK
    Pathway No. : 486
    01.5No
    craf-1*
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • MAPK
    Pathway No. : 492
    01.5No
    craf-1*
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • MAPK
    Pathway No. : 498
    01.5No
    craf-1*
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • MAPK
    Pathway No. : 504
    01.5No
    craf-1*
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • MAPK
    Pathway No. : 510
    01.5No
    craf-1*
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • MAPK
    Pathway No. : 516
    01.5No
    craf-1*
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • MAPK
    Pathway No. : 522
    01.5No

    craf-1* acting as a Substrate for an Enzyme in  
    Ajay_bhalla_2007_ReacDiff1_1e-12 Network
     Enzyme Molecule /
    Enzyme Activity
    Accession NamePathway NameKm (uM)kcat (s^-1)RatioEnzyme TypeReagents
    1MAPK*  /
    MAPK*-feedback
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • Shared_Object_
    Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Pathway No. : 375
  • 25.6405104explicit E-S complexSubstrate
    craf-1*

    Product
    craf-1**
        Ueki et al JBC 269(22):15756-15761 show the presence of this step, but not the rate consts, which are derived from Sanghera et al JBC 265(1):52-57, 1990, see the deriv in the MAPK* notes.
    2PPhosphatase2A  /
    craf-deph
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • Shared_Object_
    Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Pathway No. : 375
  • 15.656764explicit E-S complexSubstrate
    craf-1*

    Product
    craf-1
        See parent PPhosphatase2A for parms
    3MAPK*  /
    MAPK*-feedback
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics
    Pathway No. : 382
    25.6405104explicit E-S complexSubstrate
    craf-1*

    Product
    craf-1**
        Ueki et al JBC 269(22):15756-15761 show the presence of this step, but not the rate consts, which are derived from Sanghera et al JBC 265(1):52-57, 1990, see the deriv in the MAPK* notes.
    4PPhosphatase2A  /
    craf-deph
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics
    Pathway No. : 382
    15.656764explicit E-S complexSubstrate
    craf-1*

    Product
    craf-1
        See parent PPhosphatase2A for parms
    5MAPK*  /
    MAPK*-feedback
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[1]
    Pathway No. : 388
    25.6405104explicit E-S complexSubstrate
    craf-1*

    Product
    craf-1**
        Ueki et al JBC 269(22):15756-15761 show the presence of this step, but not the rate consts, which are derived from Sanghera et al JBC 265(1):52-57, 1990, see the deriv in the MAPK* notes.
    6PPhosphatase2A  /
    craf-deph
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[1]
    Pathway No. : 388
    15.656764explicit E-S complexSubstrate
    craf-1*

    Product
    craf-1
        See parent PPhosphatase2A for parms
    7MAPK*  /
    MAPK*-feedback
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[2]
    Pathway No. : 394
    25.6405104explicit E-S complexSubstrate
    craf-1*

    Product
    craf-1**
        Ueki et al JBC 269(22):15756-15761 show the presence of this step, but not the rate consts, which are derived from Sanghera et al JBC 265(1):52-57, 1990, see the deriv in the MAPK* notes.
    8PPhosphatase2A  /
    craf-deph
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[2]
    Pathway No. : 394
    15.656764explicit E-S complexSubstrate
    craf-1*

    Product
    craf-1
        See parent PPhosphatase2A for parms
    9MAPK*  /
    MAPK*-feedback
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[3]
    Pathway No. : 400
    25.6405104explicit E-S complexSubstrate
    craf-1*

    Product
    craf-1**
        Ueki et al JBC 269(22):15756-15761 show the presence of this step, but not the rate consts, which are derived from Sanghera et al JBC 265(1):52-57, 1990, see the deriv in the MAPK* notes.
    10PPhosphatase2A  /
    craf-deph
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[3]
    Pathway No. : 400
    15.656764explicit E-S complexSubstrate
    craf-1*

    Product
    craf-1
        See parent PPhosphatase2A for parms
    11MAPK*  /
    MAPK*-feedback
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[4]
    Pathway No. : 407
    25.6405104explicit E-S complexSubstrate
    craf-1*

    Product
    craf-1**
        Ueki et al JBC 269(22):15756-15761 show the presence of this step, but not the rate consts, which are derived from Sanghera et al JBC 265(1):52-57, 1990, see the deriv in the MAPK* notes.
    12PPhosphatase2A  /
    craf-deph
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[4]
    Pathway No. : 407
    15.656764explicit E-S complexSubstrate
    craf-1*

    Product
    craf-1
        See parent PPhosphatase2A for parms
    13MAPK*  /
    MAPK*-feedback
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[5]
    Pathway No. : 413
    25.6405104explicit E-S complexSubstrate
    craf-1*

    Product
    craf-1**
        Ueki et al JBC 269(22):15756-15761 show the presence of this step, but not the rate consts, which are derived from Sanghera et al JBC 265(1):52-57, 1990, see the deriv in the MAPK* notes.
    14PPhosphatase2A  /
    craf-deph
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[5]
    Pathway No. : 413
    15.656764explicit E-S complexSubstrate
    craf-1*

    Product
    craf-1
        See parent PPhosphatase2A for parms
    15MAPK*  /
    MAPK*-feedback
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[6]
    Pathway No. : 417
    25.6405104explicit E-S complexSubstrate
    craf-1*

    Product
    craf-1**
        Ueki et al JBC 269(22):15756-15761 show the presence of this step, but not the rate consts, which are derived from Sanghera et al JBC 265(1):52-57, 1990, see the deriv in the MAPK* notes.
    16PPhosphatase2A  /
    craf-deph
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[6]
    Pathway No. : 417
    15.656764explicit E-S complexSubstrate
    craf-1*

    Product
    craf-1
        See parent PPhosphatase2A for parms
    17MAPK*  /
    MAPK*-feedback
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[7]
    Pathway No. : 425
    25.6405104explicit E-S complexSubstrate
    craf-1*

    Product
    craf-1**
        Ueki et al JBC 269(22):15756-15761 show the presence of this step, but not the rate consts, which are derived from Sanghera et al JBC 265(1):52-57, 1990, see the deriv in the MAPK* notes.
    18PPhosphatase2A  /
    craf-deph
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[7]
    Pathway No. : 425
    15.656764explicit E-S complexSubstrate
    craf-1*

    Product
    craf-1
        See parent PPhosphatase2A for parms
    19MAPK*  /
    MAPK*-feedback
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[8]
    Pathway No. : 430
    25.6405104explicit E-S complexSubstrate
    craf-1*

    Product
    craf-1**
        Ueki et al JBC 269(22):15756-15761 show the presence of this step, but not the rate consts, which are derived from Sanghera et al JBC 265(1):52-57, 1990, see the deriv in the MAPK* notes.
    20PPhosphatase2A  /
    craf-deph
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[8]
    Pathway No. : 430
    15.656764explicit E-S complexSubstrate
    craf-1*

    Product
    craf-1
        See parent PPhosphatase2A for parms
    21MAPK*  /
    MAPK*-feedback
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[9]
    Pathway No. : 436
    25.6405104explicit E-S complexSubstrate
    craf-1*

    Product
    craf-1**
        Ueki et al JBC 269(22):15756-15761 show the presence of this step, but not the rate consts, which are derived from Sanghera et al JBC 265(1):52-57, 1990, see the deriv in the MAPK* notes.
    22PPhosphatase2A  /
    craf-deph
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[9]
    Pathway No. : 436
    15.656764explicit E-S complexSubstrate
    craf-1*

    Product
    craf-1
        See parent PPhosphatase2A for parms
    23MAPK*  /
    MAPK*-feedback
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[10]
    Pathway No. : 442
    25.6405104explicit E-S complexSubstrate
    craf-1*

    Product
    craf-1**
        Ueki et al JBC 269(22):15756-15761 show the presence of this step, but not the rate consts, which are derived from Sanghera et al JBC 265(1):52-57, 1990, see the deriv in the MAPK* notes.
    24PPhosphatase2A  /
    craf-deph
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[10]
    Pathway No. : 442
    15.656764explicit E-S complexSubstrate
    craf-1*

    Product
    craf-1
        See parent PPhosphatase2A for parms
    25MAPK*  /
    MAPK*-feedback
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[11]
    Pathway No. : 448
    25.6405104explicit E-S complexSubstrate
    craf-1*

    Product
    craf-1**
        Ueki et al JBC 269(22):15756-15761 show the presence of this step, but not the rate consts, which are derived from Sanghera et al JBC 265(1):52-57, 1990, see the deriv in the MAPK* notes.
    26PPhosphatase2A  /
    craf-deph
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[11]
    Pathway No. : 448
    15.656764explicit E-S complexSubstrate
    craf-1*

    Product
    craf-1
        See parent PPhosphatase2A for parms
    27MAPK*  /
    MAPK*-feedback
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[12]
    Pathway No. : 454
    25.6405104explicit E-S complexSubstrate
    craf-1*

    Product
    craf-1**
        Ueki et al JBC 269(22):15756-15761 show the presence of this step, but not the rate consts, which are derived from Sanghera et al JBC 265(1):52-57, 1990, see the deriv in the MAPK* notes.
    28PPhosphatase2A  /
    craf-deph
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[12]
    Pathway No. : 454
    15.656764explicit E-S complexSubstrate
    craf-1*

    Product
    craf-1
        See parent PPhosphatase2A for parms
    29MAPK*  /
    MAPK*-feedback
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[13]
    Pathway No. : 460
    25.6405104explicit E-S complexSubstrate
    craf-1*

    Product
    craf-1**
        Ueki et al JBC 269(22):15756-15761 show the presence of this step, but not the rate consts, which are derived from Sanghera et al JBC 265(1):52-57, 1990, see the deriv in the MAPK* notes.
    30PPhosphatase2A  /
    craf-deph
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[13]
    Pathway No. : 460
    15.656764explicit E-S complexSubstrate
    craf-1*

    Product
    craf-1
        See parent PPhosphatase2A for parms
    31MAPK*  /
    MAPK*-feedback
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[14]
    Pathway No. : 466
    25.6405104explicit E-S complexSubstrate
    craf-1*

    Product
    craf-1**
        Ueki et al JBC 269(22):15756-15761 show the presence of this step, but not the rate consts, which are derived from Sanghera et al JBC 265(1):52-57, 1990, see the deriv in the MAPK* notes.
    32PPhosphatase2A  /
    craf-deph
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[14]
    Pathway No. : 466
    15.656764explicit E-S complexSubstrate
    craf-1*

    Product
    craf-1
        See parent PPhosphatase2A for parms
    33MAPK*  /
    MAPK*-feedback
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[15]
    Pathway No. : 472
    25.6405104explicit E-S complexSubstrate
    craf-1*

    Product
    craf-1**
        Ueki et al JBC 269(22):15756-15761 show the presence of this step, but not the rate consts, which are derived from Sanghera et al JBC 265(1):52-57, 1990, see the deriv in the MAPK* notes.
    34PPhosphatase2A  /
    craf-deph
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[15]
    Pathway No. : 472
    15.656764explicit E-S complexSubstrate
    craf-1*

    Product
    craf-1
        See parent PPhosphatase2A for parms
    35MAPK*  /
    MAPK*-feedback
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[16]
    Pathway No. : 478
    25.6405104explicit E-S complexSubstrate
    craf-1*

    Product
    craf-1**
        Ueki et al JBC 269(22):15756-15761 show the presence of this step, but not the rate consts, which are derived from Sanghera et al JBC 265(1):52-57, 1990, see the deriv in the MAPK* notes.
    36PPhosphatase2A  /
    craf-deph
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[16]
    Pathway No. : 478
    15.656764explicit E-S complexSubstrate
    craf-1*

    Product
    craf-1
        See parent PPhosphatase2A for parms
    37MAPK*  /
    MAPK*-feedback
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[17]
    Pathway No. : 484
    25.6405104explicit E-S complexSubstrate
    craf-1*

    Product
    craf-1**
        Ueki et al JBC 269(22):15756-15761 show the presence of this step, but not the rate consts, which are derived from Sanghera et al JBC 265(1):52-57, 1990, see the deriv in the MAPK* notes.
    38PPhosphatase2A  /
    craf-deph
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[17]
    Pathway No. : 484
    15.656764explicit E-S complexSubstrate
    craf-1*

    Product
    craf-1
        See parent PPhosphatase2A for parms
    39MAPK*  /
    MAPK*-feedback
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[18]
    Pathway No. : 490
    25.6405104explicit E-S complexSubstrate
    craf-1*

    Product
    craf-1**
        Ueki et al JBC 269(22):15756-15761 show the presence of this step, but not the rate consts, which are derived from Sanghera et al JBC 265(1):52-57, 1990, see the deriv in the MAPK* notes.
    40PPhosphatase2A  /
    craf-deph
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[18]
    Pathway No. : 490
    15.656764explicit E-S complexSubstrate
    craf-1*

    Product
    craf-1
        See parent PPhosphatase2A for parms
    41MAPK*  /
    MAPK*-feedback
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[19]
    Pathway No. : 496
    25.6405104explicit E-S complexSubstrate
    craf-1*

    Product
    craf-1**
        Ueki et al JBC 269(22):15756-15761 show the presence of this step, but not the rate consts, which are derived from Sanghera et al JBC 265(1):52-57, 1990, see the deriv in the MAPK* notes.
    42PPhosphatase2A  /
    craf-deph
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[19]
    Pathway No. : 496
    15.656764explicit E-S complexSubstrate
    craf-1*

    Product
    craf-1
        See parent PPhosphatase2A for parms
    43MAPK*  /
    MAPK*-feedback
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[20]
    Pathway No. : 502
    25.6405104explicit E-S complexSubstrate
    craf-1*

    Product
    craf-1**
        Ueki et al JBC 269(22):15756-15761 show the presence of this step, but not the rate consts, which are derived from Sanghera et al JBC 265(1):52-57, 1990, see the deriv in the MAPK* notes.
    44PPhosphatase2A  /
    craf-deph
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[20]
    Pathway No. : 502
    15.656764explicit E-S complexSubstrate
    craf-1*

    Product
    craf-1
        See parent PPhosphatase2A for parms
    45MAPK*  /
    MAPK*-feedback
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[21]
    Pathway No. : 508
    25.6405104explicit E-S complexSubstrate
    craf-1*

    Product
    craf-1**
        Ueki et al JBC 269(22):15756-15761 show the presence of this step, but not the rate consts, which are derived from Sanghera et al JBC 265(1):52-57, 1990, see the deriv in the MAPK* notes.
    46PPhosphatase2A  /
    craf-deph
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[21]
    Pathway No. : 508
    15.656764explicit E-S complexSubstrate
    craf-1*

    Product
    craf-1
        See parent PPhosphatase2A for parms
    47MAPK*  /
    MAPK*-feedback
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[22]
    Pathway No. : 514
    25.6405104explicit E-S complexSubstrate
    craf-1*

    Product
    craf-1**
        Ueki et al JBC 269(22):15756-15761 show the presence of this step, but not the rate consts, which are derived from Sanghera et al JBC 265(1):52-57, 1990, see the deriv in the MAPK* notes.
    48PPhosphatase2A  /
    craf-deph
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[22]
    Pathway No. : 514
    15.656764explicit E-S complexSubstrate
    craf-1*

    Product
    craf-1
        See parent PPhosphatase2A for parms
    49MAPK*  /
    MAPK*-feedback
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[23]
    Pathway No. : 520
    25.6405104explicit E-S complexSubstrate
    craf-1*

    Product
    craf-1**
        Ueki et al JBC 269(22):15756-15761 show the presence of this step, but not the rate consts, which are derived from Sanghera et al JBC 265(1):52-57, 1990, see the deriv in the MAPK* notes.
    50PPhosphatase2A  /
    craf-deph
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[23]
    Pathway No. : 520
    15.656764explicit E-S complexSubstrate
    craf-1*

    Product
    craf-1
        See parent PPhosphatase2A for parms

    craf-1* acting as a Product of an Enzyme in  
    Ajay_bhalla_2007_ReacDiff1_1e-12 Network
     Enzyme Molecule /
    Enzyme Activity
    Accession NamePathway NameKm (uM)kcat (s^-1)RatioEnzyme TypeReagents
    1PKC-active  /
    PKC-act-raf
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • Shared_Object_
    Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Pathway No. : 375
  • 20.000544explicit E-S complexSubstrate
    craf-1

    Product
    craf-1*
        Rate consts from Chen et al Biochem 32, 1032 (1993) k3 = k2 = 4 k1 = 9e-5 recalculated gives 1.666e-5, which is not very different. Looks like k3 is rate-limiting in this case: there is a huge amount of craf locked up in the enz complex. Let us assume a 10x higher Km, ie, lower affinity. k1 drops by 10x. Also changed k2 to 4x k3. Lowerd k1 to 1e-6 to balance 10X DAG sensitivity of PKC
    2PPhosphatase2A  /
    craf**-deph
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • Shared_Object_
    Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Pathway No. : 375
  • 15.656764explicit E-S complexSubstrate
    craf-1**

    Product
    craf-1*
        Ueki et al JBC 269(22) pp 15756-15761 1994 show hyperphosphorylation of craf, so this is there to dephosphorylate it. Identity of phosphatase is not known to me, but it may be PP2A like the rest, so I have made it so.
    3PKC-active  /
    PKC-act-raf
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics
    Pathway No. : 382
    20.000544explicit E-S complexSubstrate
    craf-1

    Product
    craf-1*
        Rate consts from Chen et al Biochem 32, 1032 (1993) k3 = k2 = 4 k1 = 9e-5 recalculated gives 1.666e-5, which is not very different. Looks like k3 is rate-limiting in this case: there is a huge amount of craf locked up in the enz complex. Let us assume a 10x higher Km, ie, lower affinity. k1 drops by 10x. Also changed k2 to 4x k3. Lowerd k1 to 1e-6 to balance 10X DAG sensitivity of PKC
    4PPhosphatase2A  /
    craf**-deph
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics
    Pathway No. : 382
    15.656764explicit E-S complexSubstrate
    craf-1**

    Product
    craf-1*
        Ueki et al JBC 269(22) pp 15756-15761 1994 show hyperphosphorylation of craf, so this is there to dephosphorylate it. Identity of phosphatase is not known to me, but it may be PP2A like the rest, so I have made it so.
    5PKC-active  /
    PKC-act-raf
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[1]
    Pathway No. : 388
    20.000544explicit E-S complexSubstrate
    craf-1

    Product
    craf-1*
        Rate consts from Chen et al Biochem 32, 1032 (1993) k3 = k2 = 4 k1 = 9e-5 recalculated gives 1.666e-5, which is not very different. Looks like k3 is rate-limiting in this case: there is a huge amount of craf locked up in the enz complex. Let us assume a 10x higher Km, ie, lower affinity. k1 drops by 10x. Also changed k2 to 4x k3. Lowerd k1 to 1e-6 to balance 10X DAG sensitivity of PKC
    6PPhosphatase2A  /
    craf**-deph
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[1]
    Pathway No. : 388
    15.656764explicit E-S complexSubstrate
    craf-1**

    Product
    craf-1*
        Ueki et al JBC 269(22) pp 15756-15761 1994 show hyperphosphorylation of craf, so this is there to dephosphorylate it. Identity of phosphatase is not known to me, but it may be PP2A like the rest, so I have made it so.
    7PKC-active  /
    PKC-act-raf
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[2]
    Pathway No. : 394
    20.000544explicit E-S complexSubstrate
    craf-1

    Product
    craf-1*
        Rate consts from Chen et al Biochem 32, 1032 (1993) k3 = k2 = 4 k1 = 9e-5 recalculated gives 1.666e-5, which is not very different. Looks like k3 is rate-limiting in this case: there is a huge amount of craf locked up in the enz complex. Let us assume a 10x higher Km, ie, lower affinity. k1 drops by 10x. Also changed k2 to 4x k3. Lowerd k1 to 1e-6 to balance 10X DAG sensitivity of PKC
    8PPhosphatase2A  /
    craf**-deph
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[2]
    Pathway No. : 394
    15.656764explicit E-S complexSubstrate
    craf-1**

    Product
    craf-1*
        Ueki et al JBC 269(22) pp 15756-15761 1994 show hyperphosphorylation of craf, so this is there to dephosphorylate it. Identity of phosphatase is not known to me, but it may be PP2A like the rest, so I have made it so.
    9PKC-active  /
    PKC-act-raf
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[3]
    Pathway No. : 400
    20.000544explicit E-S complexSubstrate
    craf-1

    Product
    craf-1*
        Rate consts from Chen et al Biochem 32, 1032 (1993) k3 = k2 = 4 k1 = 9e-5 recalculated gives 1.666e-5, which is not very different. Looks like k3 is rate-limiting in this case: there is a huge amount of craf locked up in the enz complex. Let us assume a 10x higher Km, ie, lower affinity. k1 drops by 10x. Also changed k2 to 4x k3. Lowerd k1 to 1e-6 to balance 10X DAG sensitivity of PKC
    10PPhosphatase2A  /
    craf**-deph
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[3]
    Pathway No. : 400
    15.656764explicit E-S complexSubstrate
    craf-1**

    Product
    craf-1*
        Ueki et al JBC 269(22) pp 15756-15761 1994 show hyperphosphorylation of craf, so this is there to dephosphorylate it. Identity of phosphatase is not known to me, but it may be PP2A like the rest, so I have made it so.
    11PKC-active  /
    PKC-act-raf
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[4]
    Pathway No. : 407
    20.000544explicit E-S complexSubstrate
    craf-1

    Product
    craf-1*
        Rate consts from Chen et al Biochem 32, 1032 (1993) k3 = k2 = 4 k1 = 9e-5 recalculated gives 1.666e-5, which is not very different. Looks like k3 is rate-limiting in this case: there is a huge amount of craf locked up in the enz complex. Let us assume a 10x higher Km, ie, lower affinity. k1 drops by 10x. Also changed k2 to 4x k3. Lowerd k1 to 1e-6 to balance 10X DAG sensitivity of PKC
    12PPhosphatase2A  /
    craf**-deph
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[4]
    Pathway No. : 407
    15.656764explicit E-S complexSubstrate
    craf-1**

    Product
    craf-1*
        Ueki et al JBC 269(22) pp 15756-15761 1994 show hyperphosphorylation of craf, so this is there to dephosphorylate it. Identity of phosphatase is not known to me, but it may be PP2A like the rest, so I have made it so.
    13PKC-active  /
    PKC-act-raf
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[5]
    Pathway No. : 413
    20.000544explicit E-S complexSubstrate
    craf-1

    Product
    craf-1*
        Rate consts from Chen et al Biochem 32, 1032 (1993) k3 = k2 = 4 k1 = 9e-5 recalculated gives 1.666e-5, which is not very different. Looks like k3 is rate-limiting in this case: there is a huge amount of craf locked up in the enz complex. Let us assume a 10x higher Km, ie, lower affinity. k1 drops by 10x. Also changed k2 to 4x k3. Lowerd k1 to 1e-6 to balance 10X DAG sensitivity of PKC
    14PPhosphatase2A  /
    craf**-deph
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[5]
    Pathway No. : 413
    15.656764explicit E-S complexSubstrate
    craf-1**

    Product
    craf-1*
        Ueki et al JBC 269(22) pp 15756-15761 1994 show hyperphosphorylation of craf, so this is there to dephosphorylate it. Identity of phosphatase is not known to me, but it may be PP2A like the rest, so I have made it so.
    15PKC-active  /
    PKC-act-raf
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[6]
    Pathway No. : 417
    20.000544explicit E-S complexSubstrate
    craf-1

    Product
    craf-1*
        Rate consts from Chen et al Biochem 32, 1032 (1993) k3 = k2 = 4 k1 = 9e-5 recalculated gives 1.666e-5, which is not very different. Looks like k3 is rate-limiting in this case: there is a huge amount of craf locked up in the enz complex. Let us assume a 10x higher Km, ie, lower affinity. k1 drops by 10x. Also changed k2 to 4x k3. Lowerd k1 to 1e-6 to balance 10X DAG sensitivity of PKC
    16PPhosphatase2A  /
    craf**-deph
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[6]
    Pathway No. : 417
    15.656764explicit E-S complexSubstrate
    craf-1**

    Product
    craf-1*
        Ueki et al JBC 269(22) pp 15756-15761 1994 show hyperphosphorylation of craf, so this is there to dephosphorylate it. Identity of phosphatase is not known to me, but it may be PP2A like the rest, so I have made it so.
    17PKC-active  /
    PKC-act-raf
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[7]
    Pathway No. : 425
    20.000544explicit E-S complexSubstrate
    craf-1

    Product
    craf-1*
        Rate consts from Chen et al Biochem 32, 1032 (1993) k3 = k2 = 4 k1 = 9e-5 recalculated gives 1.666e-5, which is not very different. Looks like k3 is rate-limiting in this case: there is a huge amount of craf locked up in the enz complex. Let us assume a 10x higher Km, ie, lower affinity. k1 drops by 10x. Also changed k2 to 4x k3. Lowerd k1 to 1e-6 to balance 10X DAG sensitivity of PKC
    18PPhosphatase2A  /
    craf**-deph
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[7]
    Pathway No. : 425
    15.656764explicit E-S complexSubstrate
    craf-1**

    Product
    craf-1*
        Ueki et al JBC 269(22) pp 15756-15761 1994 show hyperphosphorylation of craf, so this is there to dephosphorylate it. Identity of phosphatase is not known to me, but it may be PP2A like the rest, so I have made it so.
    19PKC-active  /
    PKC-act-raf
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[8]
    Pathway No. : 430
    20.000544explicit E-S complexSubstrate
    craf-1

    Product
    craf-1*
        Rate consts from Chen et al Biochem 32, 1032 (1993) k3 = k2 = 4 k1 = 9e-5 recalculated gives 1.666e-5, which is not very different. Looks like k3 is rate-limiting in this case: there is a huge amount of craf locked up in the enz complex. Let us assume a 10x higher Km, ie, lower affinity. k1 drops by 10x. Also changed k2 to 4x k3. Lowerd k1 to 1e-6 to balance 10X DAG sensitivity of PKC
    20PPhosphatase2A  /
    craf**-deph
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[8]
    Pathway No. : 430
    15.656764explicit E-S complexSubstrate
    craf-1**

    Product
    craf-1*
        Ueki et al JBC 269(22) pp 15756-15761 1994 show hyperphosphorylation of craf, so this is there to dephosphorylate it. Identity of phosphatase is not known to me, but it may be PP2A like the rest, so I have made it so.
    21PKC-active  /
    PKC-act-raf
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[9]
    Pathway No. : 436
    20.000544explicit E-S complexSubstrate
    craf-1

    Product
    craf-1*
        Rate consts from Chen et al Biochem 32, 1032 (1993) k3 = k2 = 4 k1 = 9e-5 recalculated gives 1.666e-5, which is not very different. Looks like k3 is rate-limiting in this case: there is a huge amount of craf locked up in the enz complex. Let us assume a 10x higher Km, ie, lower affinity. k1 drops by 10x. Also changed k2 to 4x k3. Lowerd k1 to 1e-6 to balance 10X DAG sensitivity of PKC
    22PPhosphatase2A  /
    craf**-deph
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[9]
    Pathway No. : 436
    15.656764explicit E-S complexSubstrate
    craf-1**

    Product
    craf-1*
        Ueki et al JBC 269(22) pp 15756-15761 1994 show hyperphosphorylation of craf, so this is there to dephosphorylate it. Identity of phosphatase is not known to me, but it may be PP2A like the rest, so I have made it so.
    23PKC-active  /
    PKC-act-raf
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[10]
    Pathway No. : 442
    20.000544explicit E-S complexSubstrate
    craf-1

    Product
    craf-1*
        Rate consts from Chen et al Biochem 32, 1032 (1993) k3 = k2 = 4 k1 = 9e-5 recalculated gives 1.666e-5, which is not very different. Looks like k3 is rate-limiting in this case: there is a huge amount of craf locked up in the enz complex. Let us assume a 10x higher Km, ie, lower affinity. k1 drops by 10x. Also changed k2 to 4x k3. Lowerd k1 to 1e-6 to balance 10X DAG sensitivity of PKC
    24PPhosphatase2A  /
    craf**-deph
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[10]
    Pathway No. : 442
    15.656764explicit E-S complexSubstrate
    craf-1**

    Product
    craf-1*
        Ueki et al JBC 269(22) pp 15756-15761 1994 show hyperphosphorylation of craf, so this is there to dephosphorylate it. Identity of phosphatase is not known to me, but it may be PP2A like the rest, so I have made it so.
    25PKC-active  /
    PKC-act-raf
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[11]
    Pathway No. : 448
    20.000544explicit E-S complexSubstrate
    craf-1

    Product
    craf-1*
        Rate consts from Chen et al Biochem 32, 1032 (1993) k3 = k2 = 4 k1 = 9e-5 recalculated gives 1.666e-5, which is not very different. Looks like k3 is rate-limiting in this case: there is a huge amount of craf locked up in the enz complex. Let us assume a 10x higher Km, ie, lower affinity. k1 drops by 10x. Also changed k2 to 4x k3. Lowerd k1 to 1e-6 to balance 10X DAG sensitivity of PKC
    26PPhosphatase2A  /
    craf**-deph
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[11]
    Pathway No. : 448
    15.656764explicit E-S complexSubstrate
    craf-1**

    Product
    craf-1*
        Ueki et al JBC 269(22) pp 15756-15761 1994 show hyperphosphorylation of craf, so this is there to dephosphorylate it. Identity of phosphatase is not known to me, but it may be PP2A like the rest, so I have made it so.
    27PKC-active  /
    PKC-act-raf
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[12]
    Pathway No. : 454
    20.000544explicit E-S complexSubstrate
    craf-1

    Product
    craf-1*
        Rate consts from Chen et al Biochem 32, 1032 (1993) k3 = k2 = 4 k1 = 9e-5 recalculated gives 1.666e-5, which is not very different. Looks like k3 is rate-limiting in this case: there is a huge amount of craf locked up in the enz complex. Let us assume a 10x higher Km, ie, lower affinity. k1 drops by 10x. Also changed k2 to 4x k3. Lowerd k1 to 1e-6 to balance 10X DAG sensitivity of PKC
    28PPhosphatase2A  /
    craf**-deph
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[12]
    Pathway No. : 454
    15.656764explicit E-S complexSubstrate
    craf-1**

    Product
    craf-1*
        Ueki et al JBC 269(22) pp 15756-15761 1994 show hyperphosphorylation of craf, so this is there to dephosphorylate it. Identity of phosphatase is not known to me, but it may be PP2A like the rest, so I have made it so.
    29PKC-active  /
    PKC-act-raf
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[13]
    Pathway No. : 460
    20.000544explicit E-S complexSubstrate
    craf-1

    Product
    craf-1*
        Rate consts from Chen et al Biochem 32, 1032 (1993) k3 = k2 = 4 k1 = 9e-5 recalculated gives 1.666e-5, which is not very different. Looks like k3 is rate-limiting in this case: there is a huge amount of craf locked up in the enz complex. Let us assume a 10x higher Km, ie, lower affinity. k1 drops by 10x. Also changed k2 to 4x k3. Lowerd k1 to 1e-6 to balance 10X DAG sensitivity of PKC
    30PPhosphatase2A  /
    craf**-deph
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[13]
    Pathway No. : 460
    15.656764explicit E-S complexSubstrate
    craf-1**

    Product
    craf-1*
        Ueki et al JBC 269(22) pp 15756-15761 1994 show hyperphosphorylation of craf, so this is there to dephosphorylate it. Identity of phosphatase is not known to me, but it may be PP2A like the rest, so I have made it so.
    31PKC-active  /
    PKC-act-raf
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[14]
    Pathway No. : 466
    20.000544explicit E-S complexSubstrate
    craf-1

    Product
    craf-1*
        Rate consts from Chen et al Biochem 32, 1032 (1993) k3 = k2 = 4 k1 = 9e-5 recalculated gives 1.666e-5, which is not very different. Looks like k3 is rate-limiting in this case: there is a huge amount of craf locked up in the enz complex. Let us assume a 10x higher Km, ie, lower affinity. k1 drops by 10x. Also changed k2 to 4x k3. Lowerd k1 to 1e-6 to balance 10X DAG sensitivity of PKC
    32PPhosphatase2A  /
    craf**-deph
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[14]
    Pathway No. : 466
    15.656764explicit E-S complexSubstrate
    craf-1**

    Product
    craf-1*
        Ueki et al JBC 269(22) pp 15756-15761 1994 show hyperphosphorylation of craf, so this is there to dephosphorylate it. Identity of phosphatase is not known to me, but it may be PP2A like the rest, so I have made it so.
    33PKC-active  /
    PKC-act-raf
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[15]
    Pathway No. : 472
    20.000544explicit E-S complexSubstrate
    craf-1

    Product
    craf-1*
        Rate consts from Chen et al Biochem 32, 1032 (1993) k3 = k2 = 4 k1 = 9e-5 recalculated gives 1.666e-5, which is not very different. Looks like k3 is rate-limiting in this case: there is a huge amount of craf locked up in the enz complex. Let us assume a 10x higher Km, ie, lower affinity. k1 drops by 10x. Also changed k2 to 4x k3. Lowerd k1 to 1e-6 to balance 10X DAG sensitivity of PKC
    34PPhosphatase2A  /
    craf**-deph
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[15]
    Pathway No. : 472
    15.656764explicit E-S complexSubstrate
    craf-1**

    Product
    craf-1*
        Ueki et al JBC 269(22) pp 15756-15761 1994 show hyperphosphorylation of craf, so this is there to dephosphorylate it. Identity of phosphatase is not known to me, but it may be PP2A like the rest, so I have made it so.
    35PKC-active  /
    PKC-act-raf
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[16]
    Pathway No. : 478
    20.000544explicit E-S complexSubstrate
    craf-1

    Product
    craf-1*
        Rate consts from Chen et al Biochem 32, 1032 (1993) k3 = k2 = 4 k1 = 9e-5 recalculated gives 1.666e-5, which is not very different. Looks like k3 is rate-limiting in this case: there is a huge amount of craf locked up in the enz complex. Let us assume a 10x higher Km, ie, lower affinity. k1 drops by 10x. Also changed k2 to 4x k3. Lowerd k1 to 1e-6 to balance 10X DAG sensitivity of PKC
    36PPhosphatase2A  /
    craf**-deph
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[16]
    Pathway No. : 478
    15.656764explicit E-S complexSubstrate
    craf-1**

    Product
    craf-1*
        Ueki et al JBC 269(22) pp 15756-15761 1994 show hyperphosphorylation of craf, so this is there to dephosphorylate it. Identity of phosphatase is not known to me, but it may be PP2A like the rest, so I have made it so.
    37PKC-active  /
    PKC-act-raf
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[17]
    Pathway No. : 484
    20.000544explicit E-S complexSubstrate
    craf-1

    Product
    craf-1*
        Rate consts from Chen et al Biochem 32, 1032 (1993) k3 = k2 = 4 k1 = 9e-5 recalculated gives 1.666e-5, which is not very different. Looks like k3 is rate-limiting in this case: there is a huge amount of craf locked up in the enz complex. Let us assume a 10x higher Km, ie, lower affinity. k1 drops by 10x. Also changed k2 to 4x k3. Lowerd k1 to 1e-6 to balance 10X DAG sensitivity of PKC
    38PPhosphatase2A  /
    craf**-deph
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[17]
    Pathway No. : 484
    15.656764explicit E-S complexSubstrate
    craf-1**

    Product
    craf-1*
        Ueki et al JBC 269(22) pp 15756-15761 1994 show hyperphosphorylation of craf, so this is there to dephosphorylate it. Identity of phosphatase is not known to me, but it may be PP2A like the rest, so I have made it so.
    39PKC-active  /
    PKC-act-raf
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[18]
    Pathway No. : 490
    20.000544explicit E-S complexSubstrate
    craf-1

    Product
    craf-1*
        Rate consts from Chen et al Biochem 32, 1032 (1993) k3 = k2 = 4 k1 = 9e-5 recalculated gives 1.666e-5, which is not very different. Looks like k3 is rate-limiting in this case: there is a huge amount of craf locked up in the enz complex. Let us assume a 10x higher Km, ie, lower affinity. k1 drops by 10x. Also changed k2 to 4x k3. Lowerd k1 to 1e-6 to balance 10X DAG sensitivity of PKC
    40PPhosphatase2A  /
    craf**-deph
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[18]
    Pathway No. : 490
    15.656764explicit E-S complexSubstrate
    craf-1**

    Product
    craf-1*
        Ueki et al JBC 269(22) pp 15756-15761 1994 show hyperphosphorylation of craf, so this is there to dephosphorylate it. Identity of phosphatase is not known to me, but it may be PP2A like the rest, so I have made it so.
    41PKC-active  /
    PKC-act-raf
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[19]
    Pathway No. : 496
    20.000544explicit E-S complexSubstrate
    craf-1

    Product
    craf-1*
        Rate consts from Chen et al Biochem 32, 1032 (1993) k3 = k2 = 4 k1 = 9e-5 recalculated gives 1.666e-5, which is not very different. Looks like k3 is rate-limiting in this case: there is a huge amount of craf locked up in the enz complex. Let us assume a 10x higher Km, ie, lower affinity. k1 drops by 10x. Also changed k2 to 4x k3. Lowerd k1 to 1e-6 to balance 10X DAG sensitivity of PKC
    42PPhosphatase2A  /
    craf**-deph
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[19]
    Pathway No. : 496
    15.656764explicit E-S complexSubstrate
    craf-1**

    Product
    craf-1*
        Ueki et al JBC 269(22) pp 15756-15761 1994 show hyperphosphorylation of craf, so this is there to dephosphorylate it. Identity of phosphatase is not known to me, but it may be PP2A like the rest, so I have made it so.
    43PKC-active  /
    PKC-act-raf
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[20]
    Pathway No. : 502
    20.000544explicit E-S complexSubstrate
    craf-1

    Product
    craf-1*
        Rate consts from Chen et al Biochem 32, 1032 (1993) k3 = k2 = 4 k1 = 9e-5 recalculated gives 1.666e-5, which is not very different. Looks like k3 is rate-limiting in this case: there is a huge amount of craf locked up in the enz complex. Let us assume a 10x higher Km, ie, lower affinity. k1 drops by 10x. Also changed k2 to 4x k3. Lowerd k1 to 1e-6 to balance 10X DAG sensitivity of PKC
    44PPhosphatase2A  /
    craf**-deph
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[20]
    Pathway No. : 502
    15.656764explicit E-S complexSubstrate
    craf-1**

    Product
    craf-1*
        Ueki et al JBC 269(22) pp 15756-15761 1994 show hyperphosphorylation of craf, so this is there to dephosphorylate it. Identity of phosphatase is not known to me, but it may be PP2A like the rest, so I have made it so.
    45PKC-active  /
    PKC-act-raf
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[21]
    Pathway No. : 508
    20.000544explicit E-S complexSubstrate
    craf-1

    Product
    craf-1*
        Rate consts from Chen et al Biochem 32, 1032 (1993) k3 = k2 = 4 k1 = 9e-5 recalculated gives 1.666e-5, which is not very different. Looks like k3 is rate-limiting in this case: there is a huge amount of craf locked up in the enz complex. Let us assume a 10x higher Km, ie, lower affinity. k1 drops by 10x. Also changed k2 to 4x k3. Lowerd k1 to 1e-6 to balance 10X DAG sensitivity of PKC
    46PPhosphatase2A  /
    craf**-deph
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[21]
    Pathway No. : 508
    15.656764explicit E-S complexSubstrate
    craf-1**

    Product
    craf-1*
        Ueki et al JBC 269(22) pp 15756-15761 1994 show hyperphosphorylation of craf, so this is there to dephosphorylate it. Identity of phosphatase is not known to me, but it may be PP2A like the rest, so I have made it so.
    47PKC-active  /
    PKC-act-raf
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[22]
    Pathway No. : 514
    20.000544explicit E-S complexSubstrate
    craf-1

    Product
    craf-1*
        Rate consts from Chen et al Biochem 32, 1032 (1993) k3 = k2 = 4 k1 = 9e-5 recalculated gives 1.666e-5, which is not very different. Looks like k3 is rate-limiting in this case: there is a huge amount of craf locked up in the enz complex. Let us assume a 10x higher Km, ie, lower affinity. k1 drops by 10x. Also changed k2 to 4x k3. Lowerd k1 to 1e-6 to balance 10X DAG sensitivity of PKC
    48PPhosphatase2A  /
    craf**-deph
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[22]
    Pathway No. : 514
    15.656764explicit E-S complexSubstrate
    craf-1**

    Product
    craf-1*
        Ueki et al JBC 269(22) pp 15756-15761 1994 show hyperphosphorylation of craf, so this is there to dephosphorylate it. Identity of phosphatase is not known to me, but it may be PP2A like the rest, so I have made it so.
    49PKC-active  /
    PKC-act-raf
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[23]
    Pathway No. : 520
    20.000544explicit E-S complexSubstrate
    craf-1

    Product
    craf-1*
        Rate consts from Chen et al Biochem 32, 1032 (1993) k3 = k2 = 4 k1 = 9e-5 recalculated gives 1.666e-5, which is not very different. Looks like k3 is rate-limiting in this case: there is a huge amount of craf locked up in the enz complex. Let us assume a 10x higher Km, ie, lower affinity. k1 drops by 10x. Also changed k2 to 4x k3. Lowerd k1 to 1e-6 to balance 10X DAG sensitivity of PKC
    50PPhosphatase2A  /
    craf**-deph
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[23]
    Pathway No. : 520
    15.656764explicit E-S complexSubstrate
    craf-1**

    Product
    craf-1*
        Ueki et al JBC 269(22) pp 15756-15761 1994 show hyperphosphorylation of craf, so this is there to dephosphorylate it. Identity of phosphatase is not known to me, but it may be PP2A like the rest, so I have made it so.

    craf-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
    1Ras-act-craf
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • Shared_Object_
    Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Pathway No. : 375
  • 9.9998
    (uM^-1 s^-1)
    0.5
    (s^-1)
    Kd(bf) = 0.05(uM)-Substrate
    GTP-Ras
    craf-1*

    Product
    Raf*-GTP-Ras
      Assume the binding is fast and limited only by the amount of Ras* available. So kf=kb/[craf-1] If kb is 1/sec, then kf = 1/0.2 uM = 1/(0.2 * 6e5) = 8.3e-6 Later: Raise it by 10 X to 4e-5 From Hallberg et al JBC 269:6 3913-3916 1994, 3% of cellular Raf is complexed with Ras. So we raise kb 4x to 4 This step needed to memb-anchor and activate Raf: Leevers et al Nature 369 411-414 May 16, 2003 Changed Ras and Raf to synaptic levels, an increase of about 2x for each. To maintain the percentage of complexed Raf, reduced the kf by 2.4 fold to 10.
    2Ras-act-craf
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics
    Pathway No. : 382
    9.9998
    (uM^-1 s^-1)
    0.5
    (s^-1)
    Kd(bf) = 0.05(uM)-Substrate
    GTP-Ras
    craf-1*

    Product
    Raf*-GTP-Ras
      Assume the binding is fast and limited only by the amount of Ras* available. So kf=kb/[craf-1] If kb is 1/sec, then kf = 1/0.2 uM = 1/(0.2 * 6e5) = 8.3e-6 Later: Raise it by 10 X to 4e-5 From Hallberg et al JBC 269:6 3913-3916 1994, 3% of cellular Raf is complexed with Ras. So we raise kb 4x to 4 This step needed to memb-anchor and activate Raf: Leevers et al Nature 369 411-414 May 16, 2003 Changed Ras and Raf to synaptic levels, an increase of about 2x for each. To maintain the percentage of complexed Raf, reduced the kf by 2.4 fold to 10.
    3Ras-act-craf
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[1]
    Pathway No. : 388
    9.9998
    (uM^-1 s^-1)
    0.5
    (s^-1)
    Kd(bf) = 0.05(uM)-Substrate
    GTP-Ras
    craf-1*

    Product
    Raf*-GTP-Ras
      Assume the binding is fast and limited only by the amount of Ras* available. So kf=kb/[craf-1] If kb is 1/sec, then kf = 1/0.2 uM = 1/(0.2 * 6e5) = 8.3e-6 Later: Raise it by 10 X to 4e-5 From Hallberg et al JBC 269:6 3913-3916 1994, 3% of cellular Raf is complexed with Ras. So we raise kb 4x to 4 This step needed to memb-anchor and activate Raf: Leevers et al Nature 369 411-414 May 16, 2003 Changed Ras and Raf to synaptic levels, an increase of about 2x for each. To maintain the percentage of complexed Raf, reduced the kf by 2.4 fold to 10.
    4Ras-act-craf
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[2]
    Pathway No. : 394
    9.9998
    (uM^-1 s^-1)
    0.5
    (s^-1)
    Kd(bf) = 0.05(uM)-Substrate
    GTP-Ras
    craf-1*

    Product
    Raf*-GTP-Ras
      Assume the binding is fast and limited only by the amount of Ras* available. So kf=kb/[craf-1] If kb is 1/sec, then kf = 1/0.2 uM = 1/(0.2 * 6e5) = 8.3e-6 Later: Raise it by 10 X to 4e-5 From Hallberg et al JBC 269:6 3913-3916 1994, 3% of cellular Raf is complexed with Ras. So we raise kb 4x to 4 This step needed to memb-anchor and activate Raf: Leevers et al Nature 369 411-414 May 16, 2003 Changed Ras and Raf to synaptic levels, an increase of about 2x for each. To maintain the percentage of complexed Raf, reduced the kf by 2.4 fold to 10.
    5Ras-act-craf
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[3]
    Pathway No. : 400
    9.9998
    (uM^-1 s^-1)
    0.5
    (s^-1)
    Kd(bf) = 0.05(uM)-Substrate
    GTP-Ras
    craf-1*

    Product
    Raf*-GTP-Ras
      Assume the binding is fast and limited only by the amount of Ras* available. So kf=kb/[craf-1] If kb is 1/sec, then kf = 1/0.2 uM = 1/(0.2 * 6e5) = 8.3e-6 Later: Raise it by 10 X to 4e-5 From Hallberg et al JBC 269:6 3913-3916 1994, 3% of cellular Raf is complexed with Ras. So we raise kb 4x to 4 This step needed to memb-anchor and activate Raf: Leevers et al Nature 369 411-414 May 16, 2003 Changed Ras and Raf to synaptic levels, an increase of about 2x for each. To maintain the percentage of complexed Raf, reduced the kf by 2.4 fold to 10.
    6Ras-act-craf
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[4]
    Pathway No. : 407
    9.9998
    (uM^-1 s^-1)
    0.5
    (s^-1)
    Kd(bf) = 0.05(uM)-Substrate
    GTP-Ras
    craf-1*

    Product
    Raf*-GTP-Ras
      Assume the binding is fast and limited only by the amount of Ras* available. So kf=kb/[craf-1] If kb is 1/sec, then kf = 1/0.2 uM = 1/(0.2 * 6e5) = 8.3e-6 Later: Raise it by 10 X to 4e-5 From Hallberg et al JBC 269:6 3913-3916 1994, 3% of cellular Raf is complexed with Ras. So we raise kb 4x to 4 This step needed to memb-anchor and activate Raf: Leevers et al Nature 369 411-414 May 16, 2003 Changed Ras and Raf to synaptic levels, an increase of about 2x for each. To maintain the percentage of complexed Raf, reduced the kf by 2.4 fold to 10.
    7Ras-act-craf
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[5]
    Pathway No. : 413
    9.9998
    (uM^-1 s^-1)
    0.5
    (s^-1)
    Kd(bf) = 0.05(uM)-Substrate
    GTP-Ras
    craf-1*

    Product
    Raf*-GTP-Ras
      Assume the binding is fast and limited only by the amount of Ras* available. So kf=kb/[craf-1] If kb is 1/sec, then kf = 1/0.2 uM = 1/(0.2 * 6e5) = 8.3e-6 Later: Raise it by 10 X to 4e-5 From Hallberg et al JBC 269:6 3913-3916 1994, 3% of cellular Raf is complexed with Ras. So we raise kb 4x to 4 This step needed to memb-anchor and activate Raf: Leevers et al Nature 369 411-414 May 16, 2003 Changed Ras and Raf to synaptic levels, an increase of about 2x for each. To maintain the percentage of complexed Raf, reduced the kf by 2.4 fold to 10.
    8Ras-act-craf
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[6]
    Pathway No. : 417
    9.9998
    (uM^-1 s^-1)
    0.5
    (s^-1)
    Kd(bf) = 0.05(uM)-Substrate
    GTP-Ras
    craf-1*

    Product
    Raf*-GTP-Ras
      Assume the binding is fast and limited only by the amount of Ras* available. So kf=kb/[craf-1] If kb is 1/sec, then kf = 1/0.2 uM = 1/(0.2 * 6e5) = 8.3e-6 Later: Raise it by 10 X to 4e-5 From Hallberg et al JBC 269:6 3913-3916 1994, 3% of cellular Raf is complexed with Ras. So we raise kb 4x to 4 This step needed to memb-anchor and activate Raf: Leevers et al Nature 369 411-414 May 16, 2003 Changed Ras and Raf to synaptic levels, an increase of about 2x for each. To maintain the percentage of complexed Raf, reduced the kf by 2.4 fold to 10.
    9Ras-act-craf
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[7]
    Pathway No. : 425
    9.9998
    (uM^-1 s^-1)
    0.5
    (s^-1)
    Kd(bf) = 0.05(uM)-Substrate
    GTP-Ras
    craf-1*

    Product
    Raf*-GTP-Ras
      Assume the binding is fast and limited only by the amount of Ras* available. So kf=kb/[craf-1] If kb is 1/sec, then kf = 1/0.2 uM = 1/(0.2 * 6e5) = 8.3e-6 Later: Raise it by 10 X to 4e-5 From Hallberg et al JBC 269:6 3913-3916 1994, 3% of cellular Raf is complexed with Ras. So we raise kb 4x to 4 This step needed to memb-anchor and activate Raf: Leevers et al Nature 369 411-414 May 16, 2003 Changed Ras and Raf to synaptic levels, an increase of about 2x for each. To maintain the percentage of complexed Raf, reduced the kf by 2.4 fold to 10.
    10Ras-act-craf
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[8]
    Pathway No. : 430
    9.9998
    (uM^-1 s^-1)
    0.5
    (s^-1)
    Kd(bf) = 0.05(uM)-Substrate
    GTP-Ras
    craf-1*

    Product
    Raf*-GTP-Ras
      Assume the binding is fast and limited only by the amount of Ras* available. So kf=kb/[craf-1] If kb is 1/sec, then kf = 1/0.2 uM = 1/(0.2 * 6e5) = 8.3e-6 Later: Raise it by 10 X to 4e-5 From Hallberg et al JBC 269:6 3913-3916 1994, 3% of cellular Raf is complexed with Ras. So we raise kb 4x to 4 This step needed to memb-anchor and activate Raf: Leevers et al Nature 369 411-414 May 16, 2003 Changed Ras and Raf to synaptic levels, an increase of about 2x for each. To maintain the percentage of complexed Raf, reduced the kf by 2.4 fold to 10.
    11Ras-act-craf
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[9]
    Pathway No. : 436
    9.9998
    (uM^-1 s^-1)
    0.5
    (s^-1)
    Kd(bf) = 0.05(uM)-Substrate
    GTP-Ras
    craf-1*

    Product
    Raf*-GTP-Ras
      Assume the binding is fast and limited only by the amount of Ras* available. So kf=kb/[craf-1] If kb is 1/sec, then kf = 1/0.2 uM = 1/(0.2 * 6e5) = 8.3e-6 Later: Raise it by 10 X to 4e-5 From Hallberg et al JBC 269:6 3913-3916 1994, 3% of cellular Raf is complexed with Ras. So we raise kb 4x to 4 This step needed to memb-anchor and activate Raf: Leevers et al Nature 369 411-414 May 16, 2003 Changed Ras and Raf to synaptic levels, an increase of about 2x for each. To maintain the percentage of complexed Raf, reduced the kf by 2.4 fold to 10.
    12Ras-act-craf
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[10]
    Pathway No. : 442
    9.9998
    (uM^-1 s^-1)
    0.5
    (s^-1)
    Kd(bf) = 0.05(uM)-Substrate
    GTP-Ras
    craf-1*

    Product
    Raf*-GTP-Ras
      Assume the binding is fast and limited only by the amount of Ras* available. So kf=kb/[craf-1] If kb is 1/sec, then kf = 1/0.2 uM = 1/(0.2 * 6e5) = 8.3e-6 Later: Raise it by 10 X to 4e-5 From Hallberg et al JBC 269:6 3913-3916 1994, 3% of cellular Raf is complexed with Ras. So we raise kb 4x to 4 This step needed to memb-anchor and activate Raf: Leevers et al Nature 369 411-414 May 16, 2003 Changed Ras and Raf to synaptic levels, an increase of about 2x for each. To maintain the percentage of complexed Raf, reduced the kf by 2.4 fold to 10.
    13Ras-act-craf
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[11]
    Pathway No. : 448
    9.9998
    (uM^-1 s^-1)
    0.5
    (s^-1)
    Kd(bf) = 0.05(uM)-Substrate
    GTP-Ras
    craf-1*

    Product
    Raf*-GTP-Ras
      Assume the binding is fast and limited only by the amount of Ras* available. So kf=kb/[craf-1] If kb is 1/sec, then kf = 1/0.2 uM = 1/(0.2 * 6e5) = 8.3e-6 Later: Raise it by 10 X to 4e-5 From Hallberg et al JBC 269:6 3913-3916 1994, 3% of cellular Raf is complexed with Ras. So we raise kb 4x to 4 This step needed to memb-anchor and activate Raf: Leevers et al Nature 369 411-414 May 16, 2003 Changed Ras and Raf to synaptic levels, an increase of about 2x for each. To maintain the percentage of complexed Raf, reduced the kf by 2.4 fold to 10.
    14Ras-act-craf
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[12]
    Pathway No. : 454
    9.9998
    (uM^-1 s^-1)
    0.5
    (s^-1)
    Kd(bf) = 0.05(uM)-Substrate
    GTP-Ras
    craf-1*

    Product
    Raf*-GTP-Ras
      Assume the binding is fast and limited only by the amount of Ras* available. So kf=kb/[craf-1] If kb is 1/sec, then kf = 1/0.2 uM = 1/(0.2 * 6e5) = 8.3e-6 Later: Raise it by 10 X to 4e-5 From Hallberg et al JBC 269:6 3913-3916 1994, 3% of cellular Raf is complexed with Ras. So we raise kb 4x to 4 This step needed to memb-anchor and activate Raf: Leevers et al Nature 369 411-414 May 16, 2003 Changed Ras and Raf to synaptic levels, an increase of about 2x for each. To maintain the percentage of complexed Raf, reduced the kf by 2.4 fold to 10.
    15Ras-act-craf
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[13]
    Pathway No. : 460
    9.9998
    (uM^-1 s^-1)
    0.5
    (s^-1)
    Kd(bf) = 0.05(uM)-Substrate
    GTP-Ras
    craf-1*

    Product
    Raf*-GTP-Ras
      Assume the binding is fast and limited only by the amount of Ras* available. So kf=kb/[craf-1] If kb is 1/sec, then kf = 1/0.2 uM = 1/(0.2 * 6e5) = 8.3e-6 Later: Raise it by 10 X to 4e-5 From Hallberg et al JBC 269:6 3913-3916 1994, 3% of cellular Raf is complexed with Ras. So we raise kb 4x to 4 This step needed to memb-anchor and activate Raf: Leevers et al Nature 369 411-414 May 16, 2003 Changed Ras and Raf to synaptic levels, an increase of about 2x for each. To maintain the percentage of complexed Raf, reduced the kf by 2.4 fold to 10.
    16Ras-act-craf
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[14]
    Pathway No. : 466
    9.9998
    (uM^-1 s^-1)
    0.5
    (s^-1)
    Kd(bf) = 0.05(uM)-Substrate
    GTP-Ras
    craf-1*

    Product
    Raf*-GTP-Ras
      Assume the binding is fast and limited only by the amount of Ras* available. So kf=kb/[craf-1] If kb is 1/sec, then kf = 1/0.2 uM = 1/(0.2 * 6e5) = 8.3e-6 Later: Raise it by 10 X to 4e-5 From Hallberg et al JBC 269:6 3913-3916 1994, 3% of cellular Raf is complexed with Ras. So we raise kb 4x to 4 This step needed to memb-anchor and activate Raf: Leevers et al Nature 369 411-414 May 16, 2003 Changed Ras and Raf to synaptic levels, an increase of about 2x for each. To maintain the percentage of complexed Raf, reduced the kf by 2.4 fold to 10.
    17Ras-act-craf
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[15]
    Pathway No. : 472
    9.9998
    (uM^-1 s^-1)
    0.5
    (s^-1)
    Kd(bf) = 0.05(uM)-Substrate
    GTP-Ras
    craf-1*

    Product
    Raf*-GTP-Ras
      Assume the binding is fast and limited only by the amount of Ras* available. So kf=kb/[craf-1] If kb is 1/sec, then kf = 1/0.2 uM = 1/(0.2 * 6e5) = 8.3e-6 Later: Raise it by 10 X to 4e-5 From Hallberg et al JBC 269:6 3913-3916 1994, 3% of cellular Raf is complexed with Ras. So we raise kb 4x to 4 This step needed to memb-anchor and activate Raf: Leevers et al Nature 369 411-414 May 16, 2003 Changed Ras and Raf to synaptic levels, an increase of about 2x for each. To maintain the percentage of complexed Raf, reduced the kf by 2.4 fold to 10.
    18Ras-act-craf
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[16]
    Pathway No. : 478
    9.9998
    (uM^-1 s^-1)
    0.5
    (s^-1)
    Kd(bf) = 0.05(uM)-Substrate
    GTP-Ras
    craf-1*

    Product
    Raf*-GTP-Ras
      Assume the binding is fast and limited only by the amount of Ras* available. So kf=kb/[craf-1] If kb is 1/sec, then kf = 1/0.2 uM = 1/(0.2 * 6e5) = 8.3e-6 Later: Raise it by 10 X to 4e-5 From Hallberg et al JBC 269:6 3913-3916 1994, 3% of cellular Raf is complexed with Ras. So we raise kb 4x to 4 This step needed to memb-anchor and activate Raf: Leevers et al Nature 369 411-414 May 16, 2003 Changed Ras and Raf to synaptic levels, an increase of about 2x for each. To maintain the percentage of complexed Raf, reduced the kf by 2.4 fold to 10.
    19Ras-act-craf
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[17]
    Pathway No. : 484
    9.9998
    (uM^-1 s^-1)
    0.5
    (s^-1)
    Kd(bf) = 0.05(uM)-Substrate
    GTP-Ras
    craf-1*

    Product
    Raf*-GTP-Ras
      Assume the binding is fast and limited only by the amount of Ras* available. So kf=kb/[craf-1] If kb is 1/sec, then kf = 1/0.2 uM = 1/(0.2 * 6e5) = 8.3e-6 Later: Raise it by 10 X to 4e-5 From Hallberg et al JBC 269:6 3913-3916 1994, 3% of cellular Raf is complexed with Ras. So we raise kb 4x to 4 This step needed to memb-anchor and activate Raf: Leevers et al Nature 369 411-414 May 16, 2003 Changed Ras and Raf to synaptic levels, an increase of about 2x for each. To maintain the percentage of complexed Raf, reduced the kf by 2.4 fold to 10.
    20Ras-act-craf
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[18]
    Pathway No. : 490
    9.9998
    (uM^-1 s^-1)
    0.5
    (s^-1)
    Kd(bf) = 0.05(uM)-Substrate
    GTP-Ras
    craf-1*

    Product
    Raf*-GTP-Ras
      Assume the binding is fast and limited only by the amount of Ras* available. So kf=kb/[craf-1] If kb is 1/sec, then kf = 1/0.2 uM = 1/(0.2 * 6e5) = 8.3e-6 Later: Raise it by 10 X to 4e-5 From Hallberg et al JBC 269:6 3913-3916 1994, 3% of cellular Raf is complexed with Ras. So we raise kb 4x to 4 This step needed to memb-anchor and activate Raf: Leevers et al Nature 369 411-414 May 16, 2003 Changed Ras and Raf to synaptic levels, an increase of about 2x for each. To maintain the percentage of complexed Raf, reduced the kf by 2.4 fold to 10.
    21Ras-act-craf
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[19]
    Pathway No. : 496
    9.9998
    (uM^-1 s^-1)
    0.5
    (s^-1)
    Kd(bf) = 0.05(uM)-Substrate
    GTP-Ras
    craf-1*

    Product
    Raf*-GTP-Ras
      Assume the binding is fast and limited only by the amount of Ras* available. So kf=kb/[craf-1] If kb is 1/sec, then kf = 1/0.2 uM = 1/(0.2 * 6e5) = 8.3e-6 Later: Raise it by 10 X to 4e-5 From Hallberg et al JBC 269:6 3913-3916 1994, 3% of cellular Raf is complexed with Ras. So we raise kb 4x to 4 This step needed to memb-anchor and activate Raf: Leevers et al Nature 369 411-414 May 16, 2003 Changed Ras and Raf to synaptic levels, an increase of about 2x for each. To maintain the percentage of complexed Raf, reduced the kf by 2.4 fold to 10.
    22Ras-act-craf
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[20]
    Pathway No. : 502
    9.9998
    (uM^-1 s^-1)
    0.5
    (s^-1)
    Kd(bf) = 0.05(uM)-Substrate
    GTP-Ras
    craf-1*

    Product
    Raf*-GTP-Ras
      Assume the binding is fast and limited only by the amount of Ras* available. So kf=kb/[craf-1] If kb is 1/sec, then kf = 1/0.2 uM = 1/(0.2 * 6e5) = 8.3e-6 Later: Raise it by 10 X to 4e-5 From Hallberg et al JBC 269:6 3913-3916 1994, 3% of cellular Raf is complexed with Ras. So we raise kb 4x to 4 This step needed to memb-anchor and activate Raf: Leevers et al Nature 369 411-414 May 16, 2003 Changed Ras and Raf to synaptic levels, an increase of about 2x for each. To maintain the percentage of complexed Raf, reduced the kf by 2.4 fold to 10.
    23Ras-act-craf
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[21]
    Pathway No. : 508
    9.9998
    (uM^-1 s^-1)
    0.5
    (s^-1)
    Kd(bf) = 0.05(uM)-Substrate
    GTP-Ras
    craf-1*

    Product
    Raf*-GTP-Ras
      Assume the binding is fast and limited only by the amount of Ras* available. So kf=kb/[craf-1] If kb is 1/sec, then kf = 1/0.2 uM = 1/(0.2 * 6e5) = 8.3e-6 Later: Raise it by 10 X to 4e-5 From Hallberg et al JBC 269:6 3913-3916 1994, 3% of cellular Raf is complexed with Ras. So we raise kb 4x to 4 This step needed to memb-anchor and activate Raf: Leevers et al Nature 369 411-414 May 16, 2003 Changed Ras and Raf to synaptic levels, an increase of about 2x for each. To maintain the percentage of complexed Raf, reduced the kf by 2.4 fold to 10.
    24Ras-act-craf
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[22]
    Pathway No. : 514
    9.9998
    (uM^-1 s^-1)
    0.5
    (s^-1)
    Kd(bf) = 0.05(uM)-Substrate
    GTP-Ras
    craf-1*

    Product
    Raf*-GTP-Ras
      Assume the binding is fast and limited only by the amount of Ras* available. So kf=kb/[craf-1] If kb is 1/sec, then kf = 1/0.2 uM = 1/(0.2 * 6e5) = 8.3e-6 Later: Raise it by 10 X to 4e-5 From Hallberg et al JBC 269:6 3913-3916 1994, 3% of cellular Raf is complexed with Ras. So we raise kb 4x to 4 This step needed to memb-anchor and activate Raf: Leevers et al Nature 369 411-414 May 16, 2003 Changed Ras and Raf to synaptic levels, an increase of about 2x for each. To maintain the percentage of complexed Raf, reduced the kf by 2.4 fold to 10.
    25Ras-act-craf
  • Ajay_bhalla_
    2007_ReacDiff1_
    1e-12

    Accession No. : 81
  • kinetics[23]
    Pathway No. : 520
    9.9998
    (uM^-1 s^-1)
    0.5
    (s^-1)
    Kd(bf) = 0.05(uM)-Substrate
    GTP-Ras
    craf-1*

    Product
    Raf*-GTP-Ras
      Assume the binding is fast and limited only by the amount of Ras* available. So kf=kb/[craf-1] If kb is 1/sec, then kf = 1/0.2 uM = 1/(0.2 * 6e5) = 8.3e-6 Later: Raise it by 10 X to 4e-5 From Hallberg et al JBC 269:6 3913-3916 1994, 3% of cellular Raf is complexed with Ras. So we raise kb 4x to 4 This step needed to memb-anchor and activate Raf: Leevers et al Nature 369 411-414 May 16, 2003 Changed Ras and Raf to synaptic levels, an increase of about 2x for each. To maintain the percentage of complexed Raf, reduced the kf by 2.4 fold to 10.



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