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Molecule Parameter List for NOS* | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| 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. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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| NOS* 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 | 3 | 1 | 0 |
Accession and Pathway Details |
| Accession Name | Accession No. | Accession Type | Pathway Link |
regulation | 20 | Pathway | 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. | |||
NOS* acting as a Molecule in NOS_Phosph_regulation Network
| Name | Accession Name | Pathway Name | Initial Conc. (uM) | Volume (fL) | Buffered | |
| NOS* | regulation Accession No. : 20 | NOS Pathway No. : 90 | 0 | 0.0016667 | No | |
| Phosporylated NOS, by CaM kinases, with lowering of Vmax, but little change in Km for Arg and Kact for CaM. (Hayashi et al., JBC, 1999, 274(29):20597-20602) | ||||||
NOS* acting as a Product of an Enzyme in NOS_Phosph_regulation Network
| Enzyme Molecule / Enzyme Activity | Accession Name | Pathway Name | Km (uM) | kcat (s^-1) | Ratio | Enzyme Type | Reagents | |
| 1 | CaMKIV / kenz | regulation Accession No. : 20 | NOS Pathway No. : 90 | 5 | 18 | 4 | explicit E-S complex | Substrate nNOS Product NOS* |
| Hayashi et al., 1999, JBC,274(29):20597-20602. and other reported data from different sources. | ||||||||
| 2 | CaMKIIalpha / kenz | regulation Accession No. : 20 | NOS Pathway No. : 90 | 5 | 28.5 | 4 | explicit E-S complex | Substrate nNOS Product NOS* |
| Hayashi et al., 1999, JBC,274(29):20597-20602. and from various other literature datas. | ||||||||
| 3 | CaMKIalpha / kenz | regulation Accession No. : 20 | NOS Pathway No. : 90 | 5 | 17 | 4 | explicit E-S complex | Substrate nNOS Product NOS* |
| enzyme parameters used from different literature. Hayashi et al., 1999, JBC,274(29):20597-20602. | ||||||||
NOS* acting as a Substrate in a reaction in NOS_Phosph_regulation 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 |
| dephosporyl | regulation Accession No. : 20 | NOS Pathway No. : 90 | 13.9 (s^-1) | 0 (s^-1) | - | - | Substrate NOS* Product nNOS |
| kf -13.9 These rates used to keep the basal level of nNOS at reasonable experimental levels. | |||||||
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