Activating Compound | Comment | Organism | Structure |
---|---|---|---|
Calmodulin | Ca2+-calmodulin binds between the reductase and oxygenase domains to activate nitric-oxide synthesis. The enzyme adopts an ensemble of open and closed conformational states and that Ca2+-calmodulin binding induces a dramatic rearrangement of the reductase domain. Calmodulin-specific activation triggers release and rotation of the FMN subdomain to expose the flavin for electron transfer to the heme | Rattus norvegicus |
Cloned (Comment) | Organism |
---|---|
untagged nNOS dimer protein is expressed using a recombinant baculovirus/Sf9 insect cell system | Rattus norvegicus |
Localization | Comment | Organism | GeneOntology No. | Textmining |
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Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-arginine + 3 NADPH + 3 H+ + 4 O2 | Rattus norvegicus | nitric-oxide synthase (NOS) is required in mammals to generate nitric-oxide for regulating blood pressure, synaptic response, and immune defense | 2 L-citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Rattus norvegicus | P29476 | - |
- |
Purification (Comment) | Organism |
---|---|
- |
Rattus norvegicus |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
neuron | - |
Rattus norvegicus | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-arginine + 3 NADPH + 3 H+ + 4 O2 | nitric-oxide synthase (NOS) is required in mammals to generate nitric-oxide for regulating blood pressure, synaptic response, and immune defense | Rattus norvegicus | 2 L-citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O | - |
? | |
L-arginine + 3 NADPH + 3 H+ + 4 O2 | proposed conformational model for nitric oxide synthesis by the enzyme. Nitric oxide synthesis involves two distinct changes in the holoenzyme complex: 1. an extended-to-closed conformational equilibrium that brings the reductase domains together in a cross-monomer arrangement, and 2. release and rotation of the FMN domain triggered by CaM binding that positions the FMN cofactor for electron transfer across to the adjacent oxygenase domain in the closed state | Rattus norvegicus | 2 L-citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O | - |
? |
Subunits | Comment | Organism |
---|---|---|
homodimer | the enzyme is a large homodimer with a reductase and an oxygenase domains that coordinate a multistep, interdomain electron transfer mechanism to oxidize L-arginine and generate nitric oxide | Rattus norvegicus |
Synonyms | Comment | Organism |
---|---|---|
nNOS | - |
Rattus norvegicus |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FMN | proposed conformational model for nitric oxide synthesis by the enzyme. Nitric oxide synthesis involves two distinct changes in the holoenzyme complex: 1. an extended-to-closed conformational equilibrium that brings the reductase domains together in a cross-monomer arrangement, and 2. release and rotation of the FMN domain triggered by CaM binding that positions the FMN cofactor for electron transfer across to the adjacent oxygenase domain in the closed state | Rattus norvegicus |
General Information | Comment | Organism |
---|---|---|
physiological function | nitric-oxide synthase (NOS) is required in mammals to generate nitric-oxide for regulating blood pressure, synaptic response, and immune defense | Rattus norvegicus |