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Literature summary extracted from

  • Li, D.; Kabir, M.; Stuehr, D.J.; Rousseau, D.L.; Yeh, S.R.
    Substrate- and isoform-specific dioxygen complexes of nitric oxide synthase (2007), J. Am. Chem. Soc., 129, 6943-6951.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.14.13.39 Calmodulin required for catalysis Mus musculus

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.14.13.39 expression of the oxygenase domain of inducible nitric oxide synthase in Escherichia coli Mus musculus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.14.13.39 Ca2+ required for catalysis Mus musculus
1.14.13.39 Fe2+ in the heme cofactor, substrate-ligand interaction in the Fe2+-O2 complex, overview Mus musculus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.14.13.39 2 L-arginine + 3 NADPH + 3 H+ + 4 O2 Mus musculus
-
 2 citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.14.13.39 Mus musculus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.14.13.39 recombinant enzyme oxygenase domain from Escherichia coli in the absence of both Arg and tetrahydrobiopterin Mus musculus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.13.39 2 L-arginine + 3 NADPH + 3 H+ + 4 O2
-
 Mus musculus 2 citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
-
 ?
1.14.13.39 2 L-arginine + 3 NADPH + 3 H+ + 4 O2 NOS catalyzes the formation of NO via a consecutive two-step reaction. In the first step, L-arginine is converted to N-hydroxy-L-arginine, in the second step, N-hydroxy-L-arginine is further converted to citrulline and nitric oxide, two different mechanisms, overview. During catalysis, mediated by calcium/calmodulin, electrons flow from NADPH through FAD and FMN in the reductase domain of one subunit of the homodimer to the oxygenase domain of the other subunit, substrate-ligand interaction in the Fe2+-O2 complex, overview Mus musculus 2 citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.14.13.39 inducible NOS
-
 Mus musculus
1.14.13.39 iNOS
-
 Mus musculus
1.14.13.39 nitric oxide synthase
-
 Mus musculus
1.14.13.39 NOS
-
 Mus musculus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.14.13.39 22
-
 assay at room temperature Mus musculus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.14.13.39 7.6
-
 assay at Mus musculus

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.13.39 FAD required for catalysis Mus musculus
1.14.13.39 FMN required for catalysis Mus musculus
1.14.13.39 heme the heme is coordinated by a cysteine residue on the proximal side, and the substrates, Arg or N-hydroxy-L-arginine, bind above the heme iron atom in the distal pocket, while the cofactor, tetrahydrobiopterin, binds along the side of the heme Mus musculus
1.14.13.39 NADPH required for catalysis Mus musculus
1.14.13.39 tetrahydrobiopterin the cofactor tetrahydrobiopterin binds along the side of the heme Mus musculus