EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
1.14.13.39 | Iron | protoporphyrin IX heme | Mus musculus |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
1.14.13.39 | 56000 | - |
2 * 56000, oxygenase subunit domain, SDS-PAGE | Mus musculus |
1.14.13.39 | 74000 | - |
reductase subunit domain, gel filtration | Mus musculus |
1.14.13.39 | 112000 | - |
oxygenase subunit domain, gel filtration | Mus musculus |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.14.13.39 | Mus musculus | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
1.14.13.39 | dimeric enzyme and subunits | Mus musculus |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
1.14.13.39 | 2 L-arginine + 3 NADPH + 3 H+ + 4 O2 = 2 L-citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O | subunits align in head-to-head manner with oxygenase domains interacting to form a dimer and reductase domains existing as independent extensions | Mus musculus |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
1.14.13.39 | macrophage | RAW 264.7 cells | Mus musculus | - |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
1.14.13.39 | 1.1 | - |
purified enzyme | Mus musculus |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.14.13.39 | 2 L-arginine + 3 NADPH + 4 O2 + 3 H+ | - |
Mus musculus | 2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O | - |
? | |
1.14.13.39 | oxidized cytochrome c + NADPH + O2 | - |
Mus musculus | reduced cytochrome c + NADP+ + H2O | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
1.14.13.39 | dimer | 2 * 56000, oxygenase subunit domain, SDS-PAGE | Mus musculus |
1.14.13.39 | monomer | 1 * 74000, reductase domain, SDS-PAGE | Mus musculus |
1.14.13.39 | More | dimer formation, each subunit consists of: 1 oxygenase domain containing heme, tetrahydrobiopterin, substrate binding site and 1 reductase domain containing FAD, FMN, calmodulin, NADPH binding site | Mus musculus |
1.14.13.39 | More | dimeric structure is required for enzyme activity, interaction between subunits via oxygenase domains | Mus musculus |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.14.13.39 | Calmodulin | required | Mus musculus | |
1.14.13.39 | FAD | - |
Mus musculus | |
1.14.13.39 | FMN | - |
Mus musculus | |
1.14.13.39 | NADPH | - |
Mus musculus |