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Literature summary extracted from
- Active site diversification of P450cam with indole generates catalysts for benzylic oxidation reactions (2015), Beilstein J. Org. Chem., 11, 1713-1720 .
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 1.14.15.1 | recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) | Pseudomonas putida |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 1.14.15.1 | C136S | site-directed mutagenesis, putidaredoxin binding compared to wild-type | Pseudomonas putida |
| 1.14.15.1 | C285S | site-directed mutagenesis, putidaredoxin binding compared to wild-type | Pseudomonas putida |
| 1.14.15.1 | C58S | site-directed mutagenesis, putidaredoxin binding compared to wild-type | Pseudomonas putida |
| 1.14.15.1 | C85S | site-directed mutagenesis, putidaredoxin binding compared to wild-type | Pseudomonas putida |
| 1.14.15.1 | E14C/S29C/C85S/C73S | site-directed mutagenesis, putidaredoxin binding compared to wild-type | Pseudomonas putida |
| 1.14.15.1 | Q227C | site-directed mutagenesis, putidaredoxin binding compared to wild-type | Pseudomonas putida |
| 1.14.15.1 | Q272C | site-directed mutagenesis, putidaredoxin binding compared to wild-type | Pseudomonas putida |
| 1.14.15.1 | S190C | site-directed mutagenesis, putidaredoxin binding compared to wild-type | Pseudomonas putida |
| 1.14.15.1 | S48C | site-directed mutagenesis, putidaredoxin binding compared to wild-type | Pseudomonas putida |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.14.15.1 | Metyrapone | enzyme P450cam bound to metyrapone is constrained in the closed conformation | Pseudomonas putida |  |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.14.15.1 | additional information | - |
additional information | interaction thermodynamics between Pdx and various states of P450cam constrained in different conformations, overview | Pseudomonas putida |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.14.15.1 | Fe2+ | enzyme-bound | Pseudomonas putida | |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.14.15.1 | (+)-camphor + reduced putidaredoxin + O2 | Pseudomonas putida | - |
(+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.14.15.1 | Pseudomonas putida | P00183 | - |
- |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.14.15.1 | (+)-camphor + reduced putidaredoxin + O2 | - |
Pseudomonas putida | (+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O | - |
? | |
| 1.14.15.1 | additional information | enzyme 450cam binds camphor and converts from the closed to open conformation upon binding putidaredoxin, the binding thermodynamics of Pdx differ when the conformation of P450cam is held in different states, thermodynamic analysis, overview | Pseudomonas putida | ? | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.14.15.1 | camphor monooxygenase | - |
Pseudomonas putida |
| 1.14.15.1 | CYP101A1 | - |
Pseudomonas putida |
| 1.14.15.1 | P450cam | - |
Pseudomonas putida |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 1.14.15.1 | 20 | - |
assay at | Pseudomonas putida |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 1.14.15.1 | 7.2 | - |
assay at | Pseudomonas putida |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.14.15.1 | cytochrome P450 | - |
Pseudomonas putida | |
| 1.14.15.1 | putidaredoxin | Pdx, the enzyme is highly specific for its reductase, with an absolute requirement for the native putidaredoxin (Pdx) to provide the second electron transfer, binding kinetics and thermodynamics with wild-type and mutant enzymes, overview. Upon binding ferric P450cam, Pdx is now known to trigger a conformational change in the enzyme, which may provide the trigger to coordinate enzyme turnover and protect the enzyme from oxidative damage | Pseudomonas putida |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 1.14.15.1 | evolution | cytochrome P450cam (CYP101) from Pseudomonas putida is the model enzyme for the P450 superfamily | Pseudomonas putida |
| 1.14.15.1 | additional information | double electron-electron resonance measurements of intermolecular distances in the Pdx/P450cam complex show that the geometry of the complex is nearly identical for the open and closed states of P450cam | Pseudomonas putida |
| 1.14.15.1 | physiological function | cytochrome P450cam carries out the conversion of camphor to 5-exohydroxycamphor under conditions in which the bacterium uses camphor as the primary carbon source for growth | Pseudomonas putida |
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