Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Iron | required | Mus musculus | |
Iron | 0.9-1.2 mol heme per mol of dimer | Mus musculus | |
Iron | protoporphyrin IX heme | Mus musculus | |
Iron | heme-iron | Mus musculus |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
130000 | - |
2 * 130000, SDS-PAGE | Mus musculus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mus musculus | - |
cytokine-inducible in macrophage | - |
Purification (Comment) | Organism |
---|---|
dimeric enzyme and subunits | Mus musculus |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
2 L-arginine + 3 NADPH + 3 H+ + 4 O2 = 2 L-citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O | structure-function study of macrophage enzyme | Mus musculus |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
macrophage | RAW 264.7 cells | Mus musculus | - |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
1.1 | - |
purified enzyme | Mus musculus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
2 L-arginine + 3 NADPH + 4 O2 + 3 H+ | capacity to synthesize NO only through dimerization and binding of heme and tetrahydrobiopterin | Mus musculus | 2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O | - |
? | |
additional information | dimeric enzyme and subunits are equivalent in catalyzing electron transfer from NADPH to cytochrome c, dichlorophenolindiphenol, and ferricyanide | Mus musculus | ? | - |
? | |
additional information | D-arginine is no substrate | Mus musculus | ? | - |
? | |
Ngamma-hydroxy-L-arginine + NADPH + O2 | - |
Mus musculus | citrulline + NADP+ + NO | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer | 2 * 130000, SDS-PAGE | Mus musculus |
More | D-arginine inhibits reconstitution of dimer from subunits | Mus musculus |
More | subunit composition of dimeric enzyme | Mus musculus |
More | dissociation of dimer into subunits at pH 6.8 | Mus musculus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Mus musculus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.8 | - |
assay at | Mus musculus |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
5,6,7,8-tetrahydro-L-biopterin | required | Mus musculus | |
5,6,7,8-tetrahydro-L-biopterin | 0.19 mol bound per mol of dimer | Mus musculus | |
Calmodulin | required | Mus musculus | |
FAD | 0.49 mol per mol of dimer | Mus musculus | |
FMN | required | Mus musculus | |
FMN | 0.71 mol per mol of dimer | Mus musculus | |
NADPH | dependent on | Mus musculus | |
NADPH | at high concentration inhibits dimer reconstitution from subunits | Mus musculus |