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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 as | Molecule | Sum total of | Enzyme | Substrate of an enzyme | Product of an enzyme | Substrate in Reaction | Product in Reaction | No. of occurrences | 1 | 0 | 0 | 0 | 0 | 1 | 0 |
Accession and Pathway Details | |
Accession Name | Accession No. | Accession Type | Pathway Link | NOHArginine | 75 | Pathway | 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.
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NOH-Arginine acting as a Molecule in NOHArginine Network
Name | Accession Name | Pathway Name | Initial Conc. (uM) | Volume (fL) | Buffered | NOH-Arginine | NOHArginine Accession No. : 75 | NOHArginine Pathway No. : 311 | 6000 | 0.0016667 | No | 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. |
Name | Accession Name | Pathway Name | Kf | Kb | Kd | tau | Reagents | 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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