Protein Variants | Comment | Organism |
---|---|---|
D38A | site-directed mutagenesis, the mutant shows altered electron transfer activity with higher Kd values for ferric P450cam and about 20% of the first electron transferring ability compared to the wild-type enzyme, the mutant forms a complex with 1,3-dimethoxy-5-methyl-1,4-benzoquinone | Pseudomonas putida |
D38N | site-directed mutagenesis, the mutant shows altered electron transfer activity with higher Kd values for ferric P450cam and about 20% of the first electron transferring ability compared to the wild-type enzyme | Pseudomonas putida |
additional information | construction of the deletion mutant DELTA106, the mutant shows reduced electron transfer activity and increased Kd values for ferric P450cam compared to the wild-type enzyme | Pseudomonas putida |
R66A | site-directed mutagenesis, reduced mutant electron transfer activity and increased Kd values for ferric P450cam compared to the wild-type enzyme | Pseudomonas putida |
R66E | site-directed mutagenesis, reduced mutant electron transfer activity and increased Kd values for ferric P450cam compared to the wild-type enzyme | Pseudomonas putida |
W106A | site-directed mutagenesis, the mutant shows altered electron transfer activity with higher Kd values for ferric P450cam and about 20% of the first electron transferring ability compared to the wild-type enzyme | Pseudomonas putida |
W106F | site-directed mutagenesis, reduced mutant electron transfer activity and increased Kd values for ferric P450cam compared to the wild-type enzyme | Pseudomonas putida |
Y33A | site-directed mutagenesis, reduced mutant electron transfer activity and increased Kd values for ferric P450cam compared to the wild-type enzyme | Pseudomonas putida |
Y33F | site-directed mutagenesis, reduced mutant electron transfer activity and increased Kd values for ferric P450cam compared to the wild-type enzyme | Pseudomonas putida |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | stopped-flow kinetics of the reaction between putidaredoxin with 1,3-dimethoxy-5-methyl-1,4-benzoquinone, kinetics of the first and the second electron transfer to P450cam of wild-type and mutant enzymes | Pseudomonas putida |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Fe2+ | the reaction cycle requires two distinct electron transfer processes from the [2Fe-2S] containing putidaredoxin to P450cam | Pseudomonas putida |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
(+)-camphor + O2 + reduced putidaredoxin | Pseudomonas putida | terminal monooxygenase in a three-component camphor-hydroxylating system from Pseudomonas putida, the reaction cycle requires two distinct electron transfer processes from the [2Fe-2S] containing putidaredoxin to P450cam | (+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Pseudomonas putida | - |
- |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
(+)-camphor + reduced putidaredoxin + O2 = (+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O | reaction mechanism, and second reductive step of the mechanism of interaction and electron transfer, overview | Pseudomonas putida |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
(+)-camphor + O2 + reduced putidaredoxin | terminal monooxygenase in a three-component camphor-hydroxylating system from Pseudomonas putida, the reaction cycle requires two distinct electron transfer processes from the [2Fe-2S] containing putidaredoxin to P450cam | Pseudomonas putida | (+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O | - |
? | |
(+)-camphor + O2 + reduced putidaredoxin | second reductive step of the mechanism of interaction and electron transfer, overview | Pseudomonas putida | (+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O | - |
? |
Synonyms | Comment | Organism |
---|---|---|
cytochrome p450cam | - |
Pseudomonas putida |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Pseudomonas putida |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
assay at | Pseudomonas putida |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
putidaredoxin | the reaction cycle requires two distinct electron transfer processes from the [2Fe-2S] containing putidaredoxin to P450cam, altered binding and electron transfer with the putidaredoxin mutant C73S, structure and model of oxidized and reduced forms, overview | Pseudomonas putida |