EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
1.14.15.1 | T252A | the mutant can epoxidize olefins like 5-methylenyl-camphor, but is ineffective in camphor hydroxylation | Pseudomonas putida |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
1.14.15.1 | Iron | heme iron | Pseudomonas putida |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.14.15.1 | (+)-camphor + O2 + reduced putidaredoxin | Pseudomonas putida | - |
(+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.14.15.1 | Pseudomonas putida | - |
- |
- |
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 | (+)-camphor + O2 + reduced putidaredoxin | wild-type enzyme, but not mutant T252A | Pseudomonas putida | (+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O | - |
? | |
1.14.15.1 | 5-methylenyl-camphor + O2 + reduced putidaredoxin | wild-type enzyme and mutant T252A, in absence of the primary oxidant species of P450, the precursor species FeOOH can effect double bond activation of 5-methylenyl-camphor initiated by a homolytic cleavage of the O-O-bond and formation of an OH radical bound to the secondary oxidant by hydrogen bonding interaction, overview | Pseudomonas putida | ? | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.14.15.1 | cytochrome p450cam | - |
Pseudomonas putida |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.14.15.1 | putidaredoxin | - |
Pseudomonas putida |