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Literature summary for 1.9.6.1 extracted from
- Purification and characterization of the periplasmic nitrate reductase from Thiosphaera pantotropha (1994), Eur. J. Biochem., 220, 117-124.
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| additional information | insensitive to inhibition by azide | Paracoccus pantotrophus |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| periplasm | - |
Paracoccus pantotrophus | - |
- |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Fe | contains 2.7 mol iron (of which 1.4 mol is presumably non-haem iron) per mol of protein (assuming a 110000 Da molecular mass) | Paracoccus pantotrophus |  |
| Mo | contains molybdenum, 0.9 mol molybdenum: 1 mol protein (assuminga 110000 Da molecular mass) | Paracoccus pantotrophus | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 16000 | - |
1 * 93000 + 1 * 16000, SDS-PAGE | Paracoccus pantotrophus |
| 93000 | - |
1 * 93000 + 1 * 16000, SDS-PAGE | Paracoccus pantotrophus |
| 110000 | - |
gel filtration | Paracoccus pantotrophus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Paracoccus pantotrophus | - |
mutant strain M6 | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Paracoccus pantotrophus |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| culture condition:anaerobically-grown cell | mutant strain (M-6) overproduces the enzyme activity under anaerobic growth conditions | Paracoccus pantotrophus | - |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 95 | - |
- |
Paracoccus pantotrophus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| nitrate + reduced methyl viologen | very high substrate specificity. The enzyme does not reduce any other oxocompound (chlorate, bromate, iodate, nitrite, molybdate, sulphate, thiosulphate, tetrathionate, selenate, dimethyl sulphoxide, trimethylamine-A-oxide, borate and arsenate) | Paracoccus pantotrophus | nitrite + oxidized methyl viologen + H2O | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| dimer | 1 * 93000 + 1 * 16000, SDS-PAGE | Paracoccus pantotrophus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| periplasmic nitrate reductase | - |
Paracoccus pantotrophus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 24 | - |
assay at | Paracoccus pantotrophus |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.3 | 8 | - |
Paracoccus pantotrophus |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 7 | 9.5 | pH 7.0: about 70% of maximal activity, pH 9.5: about 60% of maximal activity | Paracoccus pantotrophus |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| cytochrome c552 | the enzyme is a complex of a 93000 Da polypeptide and a 16000 Da nitrate-oxidizable cytochrome c552, cytochrome c552 contains two c-type heme moieties | Paracoccus pantotrophus | |
| heme | contains 1.3 mol heme per mol of protein (assuminga 110-kDa molecular mass) | Paracoccus pantotrophus | |
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