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Literature summary extracted from
- Spectroscopic and kinetic evidence for the crucial role of compound 0 in the P450cam-catalyzed hydroxylation of camphor by hydrogen peroxide (2015), Chemistry, 21, 15201-15210 .
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.14.15.1 | Iron | the hydroperoxo iron(III) intermediate P450camFeIII-OOH, i.e. Compound 0 involved in the natural catalytic cycle of P450cam, can be transiently observed in the peroxo-shunt oxidation of the substrate-free enzyme | Pseudomonas putida |  |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.14.15.1 | Pseudomonas putida | - |
- |
- |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.14.15.1 | (+)-camphor + O2 + reduced putidaredoxin | - |
Pseudomonas putida | exo-5-hydroxycamphor + oxidized putidaredoxin + H2O | - |
? | |
| 1.14.15.1 | additional information | the P450FeIII-OOH intermediate must be the oxidizing species. The mechanism of hydrogen peroxide binding to the substrate-free form of P450cam is mainly governed by the ability of H2O2 to undergo deprotonation at the hydroxo ligand coordinated to the iron(III) center under conditions of pH > pKP450 | Pseudomonas putida | ? | - |
? | |
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