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Literature summary for 1.14.13.39 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
Search for more literature for 1.14.13.39

Activating Compound

Activating Compound Comment Organism Structure
Calmodulin required for catalysis Mus musculus

Cloned(Commentary)

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

Metals/Ions

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Mus musculus
-
-
-

Purification (Commentary)

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 L-arginine + 3 NADPH + 3 H+ + 4 O2
-
 Mus musculus 2 citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
-
 ?
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

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

Temperature Optimum [°C]

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

pH Optimum

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

Cofactor

Cofactor Comment Organism Structure
FAD required for catalysis Mus musculus
FMN required for catalysis Mus musculus
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
NADPH required for catalysis Mus musculus
tetrahydrobiopterin the cofactor tetrahydrobiopterin binds along the side of the heme Mus musculus