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Molecule Parameter List for MAPK*

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* participated asMoleculeSum total ofEnzymeSubstrate of an enzymeProduct of an enzymeSubstrate in ReactionProduct in Reaction
No. of occurrences1042110

Accession and Pathway Details
Accession NameAccession No.Accession TypePathway Link
  • MAPK_MKP1_
    oscillation
  • 9Network
    Shared_Object_MAPK_MKP1_oscillation PKC MAPK 
    PLA2 Ras 
    This model relates to figure 5 in Bhalla US, Iyengar R. Chaos (2001) 11(1):221-226. It includes the model used for figures 2-4 and also has MKP-1 induction by MAPK activity in the synapse. PP2A is set to 0.16 uM and MKP synthesis is varied from 5x to 40 x basal to get a range of interesting behaviours.

    MAPK* acting as a Molecule in  
    MAPK_MKP1_oscillation Network
    NameAccession NamePathway NameInitial Conc.
    (uM)
    Volume
    (fL)
    Buffered
    MAPK*
  • MAPK_MKP1_
    oscillation

    Accession No. : 9
  • Shared_Object_
    MAPK_MKP1_
    oscillation

    Pathway No. : 59
  • 01000No
    This version is phosphorylated on both the tyr and thr residues and is active: refs The rate consts are very hard to nail down. Combine Sanghera et al JBC 265(1) :52-57 with Nemenoff et al JBC 93 pp 1960 to get k3=10/sec = k2 (from Nemenoff Vmax) and k1 = (k2 + k3)/Km = 1.3e-6 Or: k3 = 10, k2 = 40, k1 = 3.25e-6

    MAPK* acting as an Enzyme in  
    MAPK_MKP1_oscillation Network
     Enzyme Molecule /
    Enzyme Activity
    Accession NamePathway NameKm (uM)kcat (s^-1)RatioEnzyme TypeReagents
    1MAPK* /
    MAPK*-feedback
  • MAPK_MKP1_
    oscillation

    Accession No. : 9
  • Shared_Object_
    MAPK_MKP1_
    oscillation

    Pathway No. : 59
  • 25.641104explicit 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.
    2MAPK* /
    MAPK*
  • MAPK_MKP1_
    oscillation

    Accession No. : 9
  • Shared_Object_
    MAPK_MKP1_
    oscillation

    Pathway No. : 59
  • 25.641204explicit E-S complexSubstrate
    PLA2-cytosolic

    Product
    PLA2*
        Km = 25uM @ 50 uM ATP and 1mg/ml MBP (huge XS of substrate) Vmax = 4124 pmol/min/ml at a conc of 125 pmol/ml of enz, so: k3 = .5/sec (rate limiting) k1 = (k2 + k3)/Km = (.5 + 0)/(25*6e5) = 2e-8 (#/cell)^-1 #s from Sanghera et al JBC 265 pp 52 , 1990. From Nemenoff et al JBC 268(3):1960-1964 - using Sanghera's 1e-4 ratio of MAPK to protein, we get k3 = 7/sec from 1000 pmol/min/mg fig 5
    3MAPK* /
    MKP-1-phosph
  • MAPK_MKP1_
    oscillation

    Accession No. : 9
  • Shared_Object_
    MAPK_MKP1_
    oscillation

    Pathway No. : 59
  • 25.64114explicit E-S complexSubstrate
    MKP-1

    Product
    MKP-1-ser359*
        3 Feb 2000. See Brondello et al Science 286:2514 1999. Rates assumed standard MAPK rates based on Sanghera et al JBC 265(1):53-57 1990. 24 Apr 2K, based on 12 Feb 2K: scaled by 0.1 to 3.25e-7,4,1
    4MAPK* /
    MKP-1-phosph2
  • MAPK_MKP1_
    oscillation

    Accession No. : 9
  • Shared_Object_
    MAPK_MKP1_
    oscillation

    Pathway No. : 59
  • 25.64114explicit E-S complexSubstrate
    MKP-1-ser359*

    Product
    MKP-1**
        3 Feb 2000. See Brondello et al Science 286:2514 1999. Rates assumed standard MAPK rates based on Sanghera et al JBC 265(1):53-57 1990. 24 Apr 2K, based on 12 Feb 2K: Scaled x0.1 to 3.25e-7,4,1

    MAPK* acting as a Substrate for an Enzyme in  
    MAPK_MKP1_oscillation Network
     Enzyme Molecule /
    Enzyme Activity
    Accession NamePathway NameKm (uM)kcat (s^-1)RatioEnzyme TypeReagents
    1MKP-1**  /
    MKP1*-thr-deph
  • MAPK_MKP1_
    oscillation

    Accession No. : 9
  • MAPK
    Pathway No. : 61
    0.066666714Classical Michaelis-Menten
    V = Etot.S.Kcat/Km+S
    Substrate
    MAPK*

    Product
    MAPK-tyr
        3 Feb 2000. Same rates as MKP1
    2MKP-1  /
    MKP1-thr-deph
  • MAPK_MKP1_
    oscillation

    Accession No. : 9
  • Shared_Object_
    MAPK_MKP1_
    oscillation

    Pathway No. : 59
  • 0.066666714Classical Michaelis-Menten
    V = Etot.S.Kcat/Km+S
    Substrate
    MAPK*

    Product
    MAPK-tyr
        See MKP1-tyr-deph

    MAPK* acting as a Product of an Enzyme in  
    MAPK_MKP1_oscillation Network
    Enzyme Molecule /
    Enzyme Activity
    Accession NamePathway NameKm (uM)kcat (s^-1)RatioEnzyme TypeReagents
    MAPKK*  /
    MAPKKthr
  • MAPK_MKP1_
    oscillation

    Accession No. : 9
  • MAPK
    Pathway No. : 61
    0.04629630.154explicit E-S complexSubstrate
    MAPK-tyr

    Product
    MAPK*
    Rate consts same as for MAPKKtyr.

    MAPK* acting as a Substrate in a reaction in  
    MAPK_MKP1_oscillation 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
    translocation
  • MAPK_MKP1_
    oscillation

    Accession No. : 9
  • MAPK
    Pathway No. : 61
    0
    (s^-1)
    0.0001
    (s^-1)
    Keq = 5(uM)-Substrate
    MAPK*

    Product
    nuc_MAPK*
    5 Feb 2000. A nuclear translocation step. The rates are set up so that not too much MAPK gets siphoned off. 24 Apr 2000. Based on 12 Feb model. Rates slowed down x 0.02 to kf=2e-5 kb=1e-4



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