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Literature summary extracted from

  • Marechal, A.; Mattioli, T.A.; Stuehr, D.J.; Santolini, J.
    Activation of peroxynitrite by inducible nitric-oxide synthase: a direct source of nitrative stress (2007), J. Biol. Chem., 282, 14101-14112.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.14.13.39 expression of the C-terminally His-tagged iNOS oxygenase domain, iNOSoxy, in Escherichia coli strain BL21 Mus musculus

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.14.13.39 L-arginine inhibits peroxynitrite activation Mus musculus
1.14.13.39 additional information although H4B binding seems unable to affect iNOSoxy capacity to activate peroxynitrite decomposition, the binding of Arg and citrulline at the distal side of the heme pocket drastically reduces peroxynitrite activation Mus musculus
1.14.13.39 tetrahydrobiopterin inhibits peroxynitrite activation Mus musculus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.14.13.39 additional information
-
additional information kinetic analysis of the interaction between peroxynitrite and the oxygenase domain of inducible NOS at three different pH values, 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
-
?
1.14.13.39 additional information Mus musculus the enzyme exclusively performs the nitric oxide synthesis, an essential biological mediator, and of peroxynitrite, a well known cytotoxic agent involved innumerouspathophysiological processes, NOSs have the unique ability to both produce and activate peroxynitrite, overview ?
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.14.13.39 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 substrate and product binding analysis Mus musculus 2 citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
-
?
1.14.13.39 additional information the enzyme exclusively performs the nitric oxide synthesis, an essential biological mediator, and of peroxynitrite, a well known cytotoxic agent involved innumerouspathophysiological processes, NOSs have the unique ability to both produce and activate peroxynitrite, overview Mus musculus ?
-
?
1.14.13.39 additional information interaction between peroxynitrite and the oxygenase domain of inducible NOS Mus musculus ?
-
?
1.14.13.39 peroxynitrite + 4-hydroxyphenylacetic acid + NADPH + H+ oxidation and nitration, although H4B binding seems unable to affect iNOSoxy capacity to activate peroxynitrite decomposition, the binding of Arg and citrulline at the distal side of the heme pocket drastically reduces peroxynitrite activation Mus musculus 4-hydroxyl-3-nitro-phenylacetic acid + NADP+ + H2O product dimers ?

Synonyms

EC Number Synonyms Comment Organism
1.14.13.39 inducible nitric-oxide synthase
-
Mus musculus
1.14.13.39 iNOS
-
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 7.4
-
ligand interaction assay at Mus musculus

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.13.39 NADPH
-
Mus musculus
1.14.13.39 tetrahydrobiopterin binding analysis Mus musculus