EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.7.1.3 | 0.29 | - |
nitrate | pH 7.2, temperature not specified in the publication | Neurospora crassa |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.7.1.3 | Neurospora crassa | P08619 | - |
- |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
1.7.1.3 | 1.24 | - |
pH 7.2, temperature not specified in the publication | Neurospora crassa |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.7.1.3 | nitrate + NADPH + H+ | - |
Neurospora crassa | nitrite + NADP+ | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
1.7.1.3 | dimer | in presence of molybdenum cofactor, enzyme forms a dimer, gel filtration, sedimentation velocity analysis | Neurospora crassa |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.7.1.3 | nit-3 | - |
Neurospora crassa |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.7.1.3 | FAD | involved in electron transfer from NADPH to the enzyme molybdenum center where reduction of nitrate to nitrite takes place | Neurospora crassa | |
1.7.1.3 | heme | involved in electron transfer from NADPH to the enzyme molybdenum center where reduction of nitrate to nitrite takes place | Neurospora crassa | |
1.7.1.3 | 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 | |
1.7.1.3 | NADPH | - |
Neurospora crassa |