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Molecule Parameter List for NOH-Arginine

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
NOH-Arginine participated asMoleculeSum total ofEnzymeSubstrate of an enzymeProduct of an enzymeSubstrate in ReactionProduct in Reaction
No. of occurrences1000010

Accession and Pathway Details
Accession NameAccession No.Accession TypePathway Link
NOHArginine75Pathway
NOHArginine 
This model is taken from the Abu-Soud HM et al. Biochemistry. 1999 Sep 21;38(38):12446-51. This model shows kinetic binding of NOHArginine to neuronal nitric oxide synthase.
Model shows the substrate (NOH-Arginine) binding to nNOS in a two-step reversible fashion. First there is rapid binding equilibrium between Im-nNOS and NOH-Arginine to form an intermediate that contains bound imidazole and NOH-arginine. This is followed by a slower conformational change in the Im-enzyme-substrate complex that is associated with release of bound imidazole and generation of a modified enzyme-substrate complex which is detected due to spectral change. Rates approximated based on data in Table 2. The rates for first reaction are not exact since only Kd known and appropriate graphs do not exist for matching the kinetic profile.

NOH-Arginine acting as a Molecule in  
NOHArginine Network
NameAccession NamePathway NameInitial Conc.
(uM)
Volume
(fL)
Buffered
NOH-ArginineNOHArginine
Accession No. : 75
NOHArginine
Pathway No. : 311
60000.0016667No
N-hydroxyarginine, an alternative substrate forneuronal Nitric Oxide Synthase Abu-Soud HM et al. Biochemistry. 1999 Sep 21;38(38):12446-51.

NOH-Arginine acting as a Substrate in a reaction in  
NOHArginine 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
  • NOH-Arginine_
    binding
  • NOHArginine
    Accession No. : 75
    NOHArginine
    Pathway No. : 311
    25
    (uM^-1 s^-1)
    67500
    (s^-1)
    Kd(bf) = 2700(uM)-Substrate
    Im-nNOS
    NOH-Arginine

    Product
  • Im-nNOS-NOH-Argi
    nine

  • Binding of NOH-Arginine to Imidazole bound rat brainneuronal Nitric Oxide Synthase.Only Kd is known, Kf and Kb need to be approximatedaccordingly to match kinetic profiles. Due to lack ofappropriate graphs the choice of Kf and Kb here isarbitrary and matches only the Kd.Kd = 2.7mM = 2700uM. Abu-Soud HM et al. Biochemistry. 1999 Sep 21;38(38):12446-51.



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