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Molecule Parameter List for PP1A

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
PP1A participated asMoleculeSum total ofEnzymeSubstrate of an enzymeProduct of an enzymeSubstrate in ReactionProduct in Reaction
No. of occurrences1013001

Accession and Pathway Details
Accession NameAccession No.Accession TypePathway Link
  • Mammalian_cell_
    cycle
  • 85Network
    Growth CELLDIV Rb_grp 
    IE_GRP CycB_Grp Cdc20_Grp 
    Cdh1_grp E2F CycA_Grp 
    CycE_grp Early_Response_Genes Delayed_Response_Genes 
    CycD_Grp 
    This is a fairly complete mass-action reimplementation of the Novak and Tyson mammalian cell cycle model. It is inexact on two counts. First, it replaces many rather abstracted equations with mass action and Michaelis-Menten forms of enzymes. Second, it does not handle the halving of cellular volume at the division point. Within these limitations, the model does most of what the original paper shows including oscillation of the relevant molecules.

    PP1A acting as a Molecule in  
    Mammalian_cell_cycle Network
    NameAccession NamePathway NameInitial Conc.
    (uM)
    Volume
    (fL)
    Buffered
    PP1A
  • Mammalian_cell_
    cycle

    Accession No. : 85
  • Rb_grp
    Pathway No. : 1071
    0200No

    PP1A acting as an Enzyme in  
    Mammalian_cell_cycle Network
    Enzyme Molecule /
    Enzyme Activity
    Accession NamePathway NameKm (uM)kcat (s^-1)RatioEnzyme TypeReagents
    PP1A /
    k19
  • Mammalian_cell_
    cycle

    Accession No. : 85
  • Rb_grp
    Pathway No. : 1071
    10020004explicit E-S complexSubstrate
    Rb_P

    Product
    Rb
    This is part of Eqn 20. k19 = 20. It is meant to represent a dephosph step of Rb_p. rate is k19*PP1A. rate in MM form is kcat * PP1A * Rb_P / (Km + Rb_P) Assume Km << Rb_P. To do so, Km = 0.01 Then kcat = k19. 7 Apr 2005. Actually should include substrate term. Take Km = 10 >> sub. Then kcat = Km * k19 = 200 18 April. Actually substrate levels are near 10. So need to scale up. Km = 100, kcat = Km * k19 = 2000

    PP1A acting as a Substrate for an Enzyme in  
    Mammalian_cell_cycle Network
     Enzyme Molecule /
    Enzyme Activity
    Accession NamePathway NameKm (uM)kcat (s^-1)RatioEnzyme TypeReagents
    1CycE  /
    k21_phiE
  • Mammalian_cell_
    cycle

    Accession No. : 85
  • CELLDIV
    Pathway No. : 1070
    9.9996825004explicit E-S complexSubstrate
    PP1A

    Product
    PP1
        Rate is just K21 * phiE * [CycE]. K21 = 1, phiE = 25. So rate= 25 * [CycE] MM rate = kcat * E.S/(Km + S) Let Km << S, then we get rate = kcat * E So if Km = 0.01, kcat = 25 7 Apr 2005. Actually should include substrate term. So, Km = 10, kcat = Km * K21 * phiE = 250 18 Apr 2005. Speeded up 10x.
    2CycA  /
    k21_phiE_A
  • Mammalian_cell_
    cycle

    Accession No. : 85
  • CELLDIV
    Pathway No. : 1070
    9.9996825004explicit E-S complexSubstrate
    PP1A

    Product
    PP1
        phiE is also used for the reaction catalyzed by A. So rates are identical to k21_phiE
    3CycB  /
    k21_phiB
  • Mammalian_cell_
    cycle

    Accession No. : 85
  • CELLDIV
    Pathway No. : 1070
    102004explicit E-S complexSubstrate
    PP1A

    Product
    PP1
        phiB = 2. See calculation for k21_phiE

    PP1A acting as a Product in a reaction in  
    Mammalian_cell_cycle 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
    k21b
  • Mammalian_cell_
    cycle

    Accession No. : 85
  • Rb_grp
    Pathway No. : 1071
    10
    (s^-1)
    0
    (s^-1)
    --Substrate
    PP1

    Product
    PP1A
    A dummy back reaction, implicit in the form of equation 19 18 Apr 2005. Speeded up 10x.



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