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Molecule Parameter List for nNOS | 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 |
Accession and Pathway Details | |
| Accession Name | Accession No. | Accession Type | Pathway Link | NOS_Phosph_
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. |
nNOS acting as a Molecule in NOS_Phosph_regulation Network
| Name | Accession Name | Pathway Name | Initial Conc.
(uM) | Volume
(fL) | Buffered | | nNOS | NOS_Phosph_
regulation
Accession No. : 20 | NOS
Pathway No. : 90 | 0.5 | 0.0016667 | No | | neuronal Nitric Oxide Synthase. Found in the neurons, activity is dependent on CaM binding, in response to Ca levels. Molecular weight ~160 kDa. This is unphosporylated form of nNOS. |
nNOS acting as a Substrate for 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 | NOS_Phosph_
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 | NOS_Phosph_
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 | NOS_Phosph_
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. |
nNOS 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 | NOS_Phosph_
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). |
nNOS acting as a Product 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 | NOS_Phosph_
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. |
| Database compilation and code copyright (C) 2022, Upinder S. Bhalla and NCBS/TIFR
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