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Literature summary for 1.14.15.1 extracted from
- Comparison of the complexes formed by cytochrome P450cam with cytochrome b5 and putidaredoxin, two effectors of camphor hydroxylase activity (2006), Biochemistry, 45, 3887-3897.
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Fe2+ | a cytochrome P450 enzyme | Pseudomonas putida |  |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| (+)-camphor + O2 + reduced putidaredoxin | Pseudomonas putida | - |
(+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Pseudomonas putida | P00183 | - |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| (+)-camphor + O2 + reduced putidaredoxin | - |
Pseudomonas putida | (+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | secondary structure and localization of perturbation sites of cytochrome b5 and putidaredoxin, overview | Pseudomonas putida |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| camphor hydroxylase | - |
Pseudomonas putida |
| CYP101 | - |
Pseudomonas putida |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | - |
assay at | Pseudomonas putida |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | enzymatic substrate turnover with cytochrome b5 as the effector | Pseudomonas putida |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| cytochrome b5 | a cytochrome P450 enzyme, cytochrome b5 is bound in the reduced CYP101-camphor-carbon monoxide complex, cytochrome b5 perturbs many of the same resonances in the complex as Pdx, including those for residues involved in substrate access to and orientation within the active site of CYP101, chemical shifts, overview | Pseudomonas putida | |
| putidaredoxin | the physiological reductant and effector | Pseudomonas putida |
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