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 |
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 |
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 |
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 | ? | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.14.13.39 | Mus musculus | - |
- |
- |
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 | ? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.14.13.39 | inducible nitric-oxide synthase | - |
Mus musculus |
1.14.13.39 | iNOS | - |
Mus musculus |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
1.14.13.39 | 22 | - |
assay at room temperature | Mus musculus |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
1.14.13.39 | 7.4 | - |
ligand interaction assay at | Mus musculus |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.14.13.39 | NADPH | - |
Mus musculus | |
1.14.13.39 | tetrahydrobiopterin | binding analysis | Mus musculus |