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Literature summary for 1.18.1.5 extracted from
- Purification and properties of putidaredoxin reductase (1983), J. Biol. Chem., 258, 2593-2598.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Pseudomonas putida | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| simple purification procedure | Pseudomonas putida |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 34.4 | - |
pH 8.0, temperature not specified in the publication | Pseudomonas putida |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | reductase is a two-eleetron acceptor with no stable semiquinone intermediate being formed either during reduction or air reoxidation | Pseudomonas putida | ? | - |
? |  |
| reduced putidaredoxin + ferricytochrome c | the physiological electron acceptor, putidaredoxin, can be used to transfer electrons to ferri-cytochrome c in a putidaredoxin-dependent cytochrome c reductase assay | Pseudomonas putida | oxidized putidaredoxin + ferrocytochrome c | - |
? | |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| FAD | 1 mol FAD per mol of protein. Charge-transfer bands indicate a close association of the pyridine nucleotide and the reduced flavin | Pseudomonas putida | |
| NAD+ | charge-transfer bands indicate a close association of the pyridine nucleotide and the reduced flavin | Pseudomonas putida | |
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