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Molecule Parameter List for Homoarginine | 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 |
| Homoarginine 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 | | HomoArginine | 73 | Pathway |
HomoArginine | 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 HomoArginine to neuronal nitric oxide synthase.
Model shows the substrate (Homorginine) binding to nNOS in a two-step reversible fashion. First there is rapid binding equilibrium between Im-nNOS and Homoarginine to form an intermediate that contains bound imidazole and homoarginine. 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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Homoarginine acting as a Molecule in HomoArginine Network
| Name | Accession Name | Pathway Name | Initial Conc.
(uM) | Volume
(fL) | Buffered | | Homoarginine | HomoArginine
Accession No. : 73 | HomoArginine
Pathway No. : 309 | 6000 | 0.0016667 | No | | Homoarginine, an alternative substrate forneuronal Nitric Oxide Synthase Abu-Soud HM et al. Biochemistry. 1999 Sep 21;38(38):12446-51. |
Homoarginine acting as a Substrate in a reaction in HomoArginine 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 | Homoarginine_
binding | HomoArginine
Accession No. : 73 | HomoArginine
Pathway No. : 309 | 25
(uM^-1 s^-1) | 250000
(s^-1) | Kd(bf) = 10000(uM) | - | Substrate
Homoarginine
Im-nNOS
Product
Im-nNOS-Homoargi
nine
| | Binding of Homoarginine 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 of appropriate graphs the choice of Kf and Kb here is arbitrary and matches only the Kd. Kd = 10mM = 10000uM, Abu-Soud HM et al. Biochemistry. 1999 Sep 21;38(38):12446-51. |
| Database compilation and code copyright (C) 2022, Upinder S. Bhalla and NCBS/TIFR
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