Inhibitors | Comment | Organism | Structure |
---|---|---|---|
nitrate | at high substrate concentration, substrate inhibition occurs, mechanism of substrate inhibition in Nap, and kinetics, overview | Cereibacter sphaeroides |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | steady-state kinetics during activation and inactivation of the enzyme, chronoamperometry, overview. The inactive species exists under three redox states, and the active form must exist in different redox states within the catalytic cycle | Cereibacter sphaeroides |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
periplasm | - |
Cereibacter sphaeroides | - |
- |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Molybdenum | within the molybdenum cofactor. The coordination sphere of the Mo ion consists of the four thiolate ligands of two pyranopterins, a sulfur atom from a cysteine that attaches the MoCo to the protein backbone, and a sixth inorganic ligand, proposed to be oxygen or more recently sulfur | Cereibacter sphaeroides |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
2 ferrocytochrome + 2 H+ + nitrate | Cereibacter sphaeroides | - |
2 ferricytochrome + nitrite | - |
? | |
2 ferrocytochrome + 2 H+ + nitrate | Cereibacter sphaeroides DSM 158 | - |
2 ferricytochrome + nitrite | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Cereibacter sphaeroides | Q53176 | - |
- |
Cereibacter sphaeroides DSM 158 | Q53176 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
2 ferrocytochrome + 2 H+ + nitrate | - |
Cereibacter sphaeroides | 2 ferricytochrome + nitrite | - |
? | |
2 ferrocytochrome + 2 H+ + nitrate | - |
Cereibacter sphaeroides DSM 158 | 2 ferricytochrome + nitrite | - |
? | |
additional information | the MoCo in Rhodobacter sphaeroides periplasmic nitrate reductase (NapAB) is subject to a slow, irreversible reductive activation | Cereibacter sphaeroides | ? | - |
? | |
additional information | the MoCo in Rhodobacter sphaeroides periplasmic nitrate reductase (NapAB) is subject to a slow, irreversible reductive activation | Cereibacter sphaeroides DSM 158 | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
heterodimer | - |
Cereibacter sphaeroides |
Synonyms | Comment | Organism |
---|---|---|
NapA | - |
Cereibacter sphaeroides |
periplasmic nitrate reductase | - |
Cereibacter sphaeroides |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Cereibacter sphaeroides |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6 | - |
assay at | Cereibacter sphaeroides |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
cytochrome c | two surface-exposed c-type hemes, NapB | Cereibacter sphaeroides | |
molybdenum cofactor | i.e. MoCo, the EPR signature of the MoCo is heterogeneous. The MoCo in Rhodobacter sphaeroides periplasmic nitrate reductase (NapAB) is subject to a slow, irreversible reductive activation. The inactive form features an open, oxidized pyranopterin, which is closed upon reduction. Distict from that, a slow, reversible inactivation/reactivation process occurs at high nitrate concentration, overview | Cereibacter sphaeroides | |
[4Fe-4S] cluster | in close proximity to the MoCo | Cereibacter sphaeroides |
General Information | Comment | Organism |
---|---|---|
evolution | the enzyme belongs to the DMSO reductase family | Cereibacter sphaeroides |