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Molecule Parameter List for CaM-Ca4 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| 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 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| CaM-Ca4 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 |
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. | |||
CaM-Ca4 acting as a Molecule in NOS_Phosph_regulation Network
| Name | Accession Name | Pathway Name | Initial Conc. (uM) | Volume (fL) | Buffered | |
| CaM-Ca4 | regulation Accession No. : 20 | NOS Pathway No. : 90 | 20 | 0.0016667 | Yes | |
CaM-Ca4 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 |
| Ca-CaMbind_nNOS | regulation Accession No. : 20 | NOS Pathway No. : 90 | 3.25 (uM^-1 s^-1) | 0.05 (s^-1) | Kd(bf) = 0.0154(uM) | - | Substrate CaM-Ca4 nNOS Product Ca-CaMnNOS |
| Those binding CaM have a high Kd, including nNOS, ~<=10nM. The binding of CaM to nNOS has been demonstrated to act as the trigger necessary for electron transfer and catalytic activity. (Marletta, Biochemistry, 1997;36:12337-12345). | |||||||