KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.29 | - |
nitrate | pH 7.2, temperature not specified in the publication | Neurospora crassa |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Neurospora crassa | P08619 | - |
- |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
1.24 | - |
pH 7.2, temperature not specified in the publication | Neurospora crassa |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
nitrate + NADPH + H+ | - |
Neurospora crassa | nitrite + NADP+ | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer | in presence of molybdenum cofactor, enzyme forms a dimer, gel filtration, sedimentation velocity analysis | Neurospora crassa |
Synonyms | Comment | Organism |
---|---|---|
nit-3 | - |
Neurospora crassa |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FAD | involved in electron transfer from NADPH to the enzyme molybdenum center where reduction of nitrate to nitrite takes place | Neurospora crassa | |
heme | involved in electron transfer from NADPH to the enzyme molybdenum center where reduction of nitrate to nitrite takes place | Neurospora crassa | |
molybdenum cofactor | cofactor is necessary and sufficient to induce dimer formation. The molybdenum center of nitrate reductase reconstituted in vitro from apo-enzyme and cofactor shows an EPR spectrum identical to holo-enzyme. Insertion of this cofactor into the enzyme occurs independent from the insertion of any other NR redox cofactor | Neurospora crassa | |
NADPH | - |
Neurospora crassa |