NCBS Home page
Accession List
Pathway List
Search
Authorized Users
Help
News archives

Enter a Search String

Special character and space not allowed in the query term. Search string should be at least 2 characters long.
Search in: Search for Match By

Molecule Parameter List for PP1-active

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
PP1-active participated asMoleculeSum total ofEnzymeSubstrate of an enzymeProduct of an enzymeSubstrate in ReactionProduct in Reaction
No. of occurrences1020000

Accession and Pathway Details
Accession NameAccession No.Accession TypePathway Link
  • simple_AMPAR_
    traff_model2
  • 61Network
    Shared_Object_simple_AMPAR_traff_model2 Membrane Internal 
    This is a highly simplified model of the AMPAR trafficking cycle that exhibits bistability. It is model 2 from Hayer and Bhalla, PLoS 2005. Its main purpose it to illustrate how the bistability arises.

    PP1-active acting as a Molecule in  
    simple_AMPAR_traff_model2 Network
    NameAccession NamePathway NameInitial Conc.
    (uM)
    Volume
    (fL)
    Buffered
    PP1-active
  • simple_AMPAR_
    traff_model2

    Accession No. : 61
  • Membrane
    Pathway No. : 255
    0.33330.01No

    PP1-active acting as an Enzyme in  
    simple_AMPAR_traff_model2 Network
     Enzyme Molecule /
    Enzyme Activity
    Accession NamePathway NameKm (uM)kcat (s^-1)RatioEnzyme TypeReagents
    1PP1-active /
    PP1
  • simple_AMPAR_
    traff_model2

    Accession No. : 61
  • Membrane
    Pathway No. : 255
    0.9999890.354explicit E-S complexSubstrate
    MR*

    Product
    MR
        Note that Km is halved from 2 to 1, as compared to original detailed model. This is because each substrate represents two subunits of the original detailed model.
    2PP1-active /
    PP1[1]
  • simple_AMPAR_
    traff_model2

    Accession No. : 61
  • Membrane
    Pathway No. : 255
    0.9999890.354explicit E-S complexSubstrate
    MR**

    Product
    MR*
        Note halving of Km from 2 to 1. See also notes for internal-PKA-act. Basically, the enzyme must act on two substrate subunits which are lumped in the current simplification of the original detailed model. We thank an anonymous reviewer for pointing this out.



    Database compilation and code copyright (C) 2022, Upinder S. Bhalla and NCBS/TIFR
    This Copyright is applied to ensure that the contents of this database remain freely available. Please see FAQ for details.