|
Enter a Search String | | Special character and space not allowed in the query term.
Search string should be at least 2 characters long. |
Molecule Parameter List for NM-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 |
| NM-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 | | NMArginine | 74 | Pathway |
NMArginine | 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 NMArginine to neuronal nitric oxide synthase.
Model shows the substrate (NM-Arginine) binding to nNOS in a two-step reversible fashion. First there is rapid binding equilibrium between Im-nNOS and NM-Arginine to form an intermediate that contains bound imidazole and NM-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.
|
NM-Arginine acting as a Molecule in NMArginine Network
| Name | Accession Name | Pathway Name | Initial Conc.
(uM) | Volume
(fL) | Buffered | | NM-Arginine | NMArginine
Accession No. : 74 | NMArginine
Pathway No. : 310 | 6000 | 0.0016667 | No | | N-methylarginine, an alternative substrate forneuronal Nitric Oxide Synthase Abu-Soud HM et al. Biochemistry. 1999 Sep 21;38(38):12446-51. |
NM-Arginine acting as a Substrate in a reaction in NMArginine 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 | NM-Arginine_
binding | NMArginine
Accession No. : 74 | NMArginine
Pathway No. : 310 | 25
(uM^-1 s^-1) | 42500
(s^-1) | Kd(bf) = 1700(uM) | - | Substrate
Im-nNOS
NM-Arginine
Product
Im-nNOS-NM-Argin
ine
| | Binding of NM-Arginine to Imidazole bound rat brainneuronal Nitric Oxide Synthase. Only Kd is known, Kf and Kb need to be approximated accordingly to match kinetic profiles. Due to lack ofappropriate graphs the choice of Kf and Kb here is arbitrary and matches only the Kd. Kd = 1.7mM = 1700uM. 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
This Copyright is applied to ensure that the contents of this database remain freely available. Please see FAQ for details. |
|
