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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 occurrences1002200

Accession and Pathway Details
Accession NameAccession No.Accession TypePathway Link
  • Synaptic_
    Network
  • 16Network
    Shared_Object_Synaptic_Network PKC PLA2 
    PLCbeta Gq MAPK 
    Ras EGFR Sos 
    PLC_g CaMKII CaM 
    PP1 PP2B PKA 
    AC CaRegulation 
    This model is an annotated version of the synaptic signaling network.
    The primary reference is Bhalla US and Iyengar R. Science (1999) 283(5400):381-7 but several of the model pathways have been updated.
    Bhalla US Biophys J. 2002 Aug;83(2):740-52
    Bhalla US J Comput Neurosci. 2002 Jul-Aug;13(1):49-62

    MAPK-tyr acting as a Molecule in  
    Synaptic_Network Network
    NameAccession NamePathway NameInitial Conc.
    (uM)
    Volume
    (fL)
    Buffered
    MAPK-tyr
  • Synaptic_
    Network

    Accession No. : 16
  • MAPK
    Pathway No. : 75
    01000No
    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  
    Synaptic_Network Network
     Enzyme Molecule /
    Enzyme Activity
    Accession NamePathway NameKm (uM)kcat (s^-1)RatioEnzyme TypeReagents
    1MAPKK*  /
    MAPKKthr
  • Synaptic_
    Network

    Accession No. : 16
  • MAPK
    Pathway No. : 75
    0.04629630.154explicit E-S complexSubstrate
    MAPK-tyr

    Product
    MAPK*
        Rate consts same as for MAPKKtyr.
    2MKP-1  /
    MKP1-tyr-deph
  • Synaptic_
    Network

    Accession No. : 16
  • Shared_Object_
    Synaptic_
    Network

    Pathway No. : 70
  • 0.066666714explicit E-S complexSubstrate
    MAPK-tyr

    Product
    MAPK
        The original kinetics from Bhalla and Iyengar Science 1999 have now been modified to obey the k2 = 4 * k3 rule, while keeping kcat and Km fixed. The main constraining data point is the time course of MAPK dephosphorylation, which this model satisfies. See Charles et al 1993 PNAS 90:5292-5296 and Charles et al Oncogene 7:187-190 Effective Km : 67 nM kcat = 1.43 umol/min/mg

    MAPK-tyr acting as a Product of an Enzyme in  
    Synaptic_Network Network
     Enzyme Molecule /
    Enzyme Activity
    Accession NamePathway NameKm (uM)kcat (s^-1)RatioEnzyme TypeReagents
    1MAPKK*  /
    MAPKKtyr
  • Synaptic_
    Network

    Accession No. : 16
  • MAPK
    Pathway No. : 75
    0.04629630.154explicit 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, ratio of 4 to get k2=0.6. k1=0.75/46.6nM=2.7e-5 In terms of Michaelis-Menten rates, Km = 0.046, Vmax = 0.15, ratio = 4.
    2MKP-1  /
    MKP1-thr-deph
  • Synaptic_
    Network

    Accession No. : 16
  • Shared_Object_
    Synaptic_
    Network

    Pathway No. : 70
  • 0.066666714explicit E-S complexSubstrate
    MAPK*

    Product
    MAPK-tyr
        See MKP1-tyr-deph



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