KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | Michaelis-Menten kinetics | Paracoccus pantotrophus |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
periplasm | - |
Paracoccus pantotrophus | - |
- |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Iron | in the two hemes of cytochrome cd1 | Paracoccus pantotrophus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Paracoccus pantotrophus | P72181 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
nitrite + H2O + reduced cytochrome cd1 | anaerobic assay conditions | Paracoccus pantotrophus | nitric oxide + H+ + cytochrome cd1 | - |
? |
Synonyms | Comment | Organism |
---|---|---|
nitrite reductase | - |
Paracoccus pantotrophus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Paracoccus pantotrophus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6 | - |
- |
Paracoccus pantotrophus |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
6 | 7 | - |
Paracoccus pantotrophus |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
cytochrome cd1 | the c heme is located in a predominantly alpha-helical domain of the enzyme, whereas the d1 heme resides in a beta-propeller structure | Paracoccus pantotrophus | |
heme | two hemes in cytochrome cd1, the c heme is located in a predominantly alpha-helical domain of the enzyme, whereas the d1 heme resides in a beta-propeller structure | Paracoccus pantotrophus |