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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 occurrences1001100

Accession and Pathway Details
Accession NameAccession No.Accession TypePathway Link
  • Ajay_Bhalla_
    2004_PKM_MKP3_
    Tuning
  • 77Network
    Shared_Object_Ajay_Bhalla_2004_PKM_MKP3_Tuning PKC PLA2 
    PLCbeta Ras Gq 
    MAPK EGFR Sos 
    PLC_g CaMKII CaM 
    PP1 PP2B PKA 
    AC MKP3 PKM 
    This model is based on Ajay SM, Bhalla US. Eur J Neurosci. 2004 Nov;20(10):2671-80. This is the feedforward model with MPK3 from figure 8a.

    craf-1 acting as a Molecule in  
    Ajay_Bhalla_2004_PKM_MKP3_Tuning Network
    NameAccession NamePathway NameInitial Conc.
    (uM)
    Volume
    (fL)
    Buffered
    craf-1
  • Ajay_Bhalla_
    2004_PKM_MKP3_
    Tuning

    Accession No. : 77
  • MAPK
    Pathway No. : 335
    0.51.5No
    Couldn't find any ref to the actual conc of craf-1 but I should try Strom et al Oncogene 5 pp 345 In line with the other kinases in the cascade, I estimate the conc to be 0.2 uM. To init we use 0.15, which is close to equil 16 May 2003: Changing to synaptic levels. Increasing 2.5 fold to 0.5 uM. See Mihaly et al 1991 Brain Res 547(2):309-14 and Morice et al 1999 Eur J Neurosci 11(6):1995-2006

    craf-1 acting as a Substrate for an Enzyme in  
    Ajay_Bhalla_2004_PKM_MKP3_Tuning Network
    Enzyme Molecule /
    Enzyme Activity
    Accession NamePathway NameKm (uM)kcat (s^-1)RatioEnzyme TypeReagents
    PKC-active  /
    PKC-act-raf
  • Ajay_Bhalla_
    2004_PKM_MKP3_
    Tuning

    Accession No. : 77
  • Shared_Object_
    Ajay_Bhalla_
    2004_PKM_MKP3_
    Tuning

    Pathway No. : 329
  • 20.000244explicit 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 3 Aug 2004. Lowered Km from 66.66 to 3.33, to match that of PKC-inact-GAP

    craf-1 acting as a Product of an Enzyme in  
    Ajay_Bhalla_2004_PKM_MKP3_Tuning Network
    Enzyme Molecule /
    Enzyme Activity
    Accession NamePathway NameKm (uM)kcat (s^-1)RatioEnzyme TypeReagents
    PPhosphatase2A  /
    craf-deph
  • Ajay_Bhalla_
    2004_PKM_MKP3_
    Tuning

    Accession No. : 77
  • Shared_Object_
    Ajay_Bhalla_
    2004_PKM_MKP3_
    Tuning

    Pathway No. : 329
  • 15.656864explicit E-S complexSubstrate
    craf-1*

    Product
    craf-1
    See parent PPhosphatase2A for parms



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