Activating Compound | Comment | Organism | Structure |
---|---|---|---|
Calmodulin | activates the neuronal NOS by binding and inhibiting the suppression through the C-terminal tail of the enzyme, overview | Rattus norvegicus |
Cloned (Comment) | Organism |
---|---|
expression of His-tagged wild-type enzyme and untagged truncation mutant enzyme in Escherichia coli strain BL21(DE3) | Rattus norvegicus |
Protein Variants | Comment | Organism |
---|---|---|
additional information | construction of a truncated mutant lacking the terminal half of the C-terminus, i.e. residues from Ile1413 to Ser1429. The mutation has almost no impact on NADP+ release, flavin reduction, flavin autoxidation, heme reduction, reductase activity, or NO synthesis activity, but does prevent an increase in FMN shielding that normally occurs in response to NADPH binding. Additional removal of the C-terminal alpha-helix, residues 1401 to 1412, significantly increases the NADP+ release rate, flavin autoxidation, and NADPH oxidase activity, and causes hyper-deshielding of the FMN cofactor associated with increased reductase activity and slightly diminished heme reduction and NO synthesis. Further removal of residues downstream from Gly1396, a full C-terminus truncation, amplifies the aforementioned effects and in addition altered NADP+ interaction with FAD, relieves the kinetic suppression on flavin reduction, and further diminishes heme reduction and NO synthesis | Rattus norvegicus |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | kinetics | Rattus norvegicus |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Fe2+ | in the heme cofactor | Rattus norvegicus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Rattus norvegicus | three unique structural elements are involved in the catalytic suppression of NOS: an autoinhibitory element in the FMN binding module, a CD2A loop in the connecting subdomain, and a C-terminal extension or tail, the C-terminal tail of nNOS is a regulatory element that suppresses nNOS activities in the absence of bound calmodulin, it may help stabilize the FMN-shielded conformation by holding the FMN module up against the FNR module as required for inter-flavin electron transfer, mechanism, overview | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Rattus norvegicus | - |
- |
- |
Purification (Comment) | Organism |
---|---|
recombinant His-tagged wild-type enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, recombinant truncation mutant from Escherichia coli strain BL21(DE3) by sequential 2',5'-ADP and calmodulin affinity chromatography | Rattus norvegicus |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
brain | nNOS | Rattus norvegicus | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | three unique structural elements are involved in the catalytic suppression of NOS: an autoinhibitory element in the FMN binding module, a CD2A loop in the connecting subdomain, and a C-terminal extension or tail, the C-terminal tail of nNOS is a regulatory element that suppresses nNOS activities in the absence of bound calmodulin, it may help stabilize the FMN-shielded conformation by holding the FMN module up against the FNR module as required for inter-flavin electron transfer, mechanism, overview | Rattus norvegicus | ? | - |
? | |
additional information | the reduced recombinant trunaction mutant nNOSr performs autooxidation in presence of NADPH, interactions, overview | Rattus norvegicus | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | nNOS reductase structure homology modeling, overview | Rattus norvegicus |
Synonyms | Comment | Organism |
---|---|---|
neuronal nitric oxide synthase | - |
Rattus norvegicus |
nNOS | - |
Rattus norvegicus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
22 | - |
assay at room temperature | Rattus norvegicus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.6 | - |
assay at | Rattus norvegicus |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FMN | an inverse correlation exists between FMN shielding and the cytochrome c reductase activity | Rattus norvegicus | |
heme | an inverse correlation exists between FMN shielding and the cytochrome c reductase activity | Rattus norvegicus | |
NADPH | binding structure of NADP(H) to wild-type and truncation mutant enzyme lacking parts of the C-terminus, overview | Rattus norvegicus |