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Molecule Parameter List for Larg

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
Larg participated asMoleculeSum total ofEnzymeSubstrate of an enzymeProduct of an enzymeSubstrate in ReactionProduct in Reaction
No. of occurrences1001000

Accession and Pathway Details
Accession NameAccession No.Accession TypePathway Link
  • NOS_Phosph_
    regulation
  • 20Pathway
    NOS 
    This model features the phosphorylation of rat brain neuronal NOS expressed in E. coli or Sf9 cells, which leads to a decrease in Vmax of the phosphorylated enzyme, with little change of both the Km for L-arginine and Kact for CaM. This is based on Hayashi Y. et al. J Biol Chem. (1999) 274(29):20597-602. They report of phosphorylatin being carried out by CaM kinases I alpha, II alpha and IV. The rates used have been obtained from their paper and from other reported experimental data.

    Larg acting as a Molecule in  
    NOS_Phosph_regulation Network
    NameAccession NamePathway NameInitial Conc.
    (uM)
    Volume
    (fL)
    Buffered
    Larg
  • NOS_Phosph_
    regulation

    Accession No. : 20
  • NOS
    Pathway No. : 90
    1000.0016667No

    Larg acting as a Substrate for an Enzyme in  
    NOS_Phosph_regulation Network
    Enzyme Molecule /
    Enzyme Activity
    Accession NamePathway NameKm (uM)kcat (s^-1)RatioEnzyme TypeReagents
    Ca-CaMnNOS  /
    kenz
  • NOS_Phosph_
    regulation

    Accession No. : 20
  • NOS
    Pathway No. : 90
    1016.6674explicit E-S complexSubstrate
    Larg

    Product
    NO
    cit
    Km for purified NOS is estimated between 1 - 10 uM. (Prog in Neurobiology, 2001, 64: 365-391) Vmax for unphosporylated NOS, the active form, is 500-1500 nmol/nmol/min (Montellano et al., 1998, JBC,26(12): 1185-1189). Hayashi et al., JBC, 1999, 274(29):20597-20602 report Vmax (nmol/min/mg) of nNOS Unphosporylated at 95.7 (+-) 4.2



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