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Literature summary for 1.14.13.39 extracted from

  • Yokom, A.L.; Morishima, Y.; Lau, M.; Su, M.; Glukhova, A.; Osawa, Y.; Southworth, D.R.
    Architecture of the nitric-oxide synthase holoenzyme reveals large conformational changes and a calmodulin-driven release of the FMN domain (2014), J. Biol. Chem., 289, 16855-16865 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.14.13.39

Activating Compound

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(Commentary)

Cloned (Comment) Organism
untagged nNOS dimer protein is expressed using a recombinant baculovirus/Sf9 insect cell system Rattus norvegicus

Localization

Localization Comment Organism GeneOntology No. Textmining

Natural Substrates/ Products (Substrates)

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
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 ?

Organism

Organism UniProt Comment Textmining
Rattus norvegicus P29476
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-

Purification (Commentary)

Purification (Comment) Organism
-
 Rattus norvegicus

Source Tissue

Source Tissue Comment Organism Textmining
neuron
-
 Rattus norvegicus
-

Substrates and Products (Substrate)

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

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

Synonyms Comment Organism
nNOS
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 Rattus norvegicus

Cofactor

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

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