Any feedback?
Literature summary extracted from
- Effect of alcohols on binding of camphor to cytochrome P450cam: spectroscopic and stopped flow transient kinetic studies (2006), Arch. Biochem. Biophys., 455, 154-162.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 1.14.15.1 | overexpression in Escherichia coli strain BL21(DE3) | 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 | spectroscopic and stopped flow transient kinetic studies | Pseudomonas putida |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.14.15.1 | Fe2+ | heme iron in a heme pocket | 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 + O2 + reduced putidaredoxin | Pseudomonas putida | - |
(+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.14.15.1 | Pseudomonas putida | P00183 | - |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 1.14.15.1 | recombinant enzyme from Escherichia coli strain BL21(DE3) | 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 | (+)-camphor + O2 + reduced putidaredoxin | binding of camphor is strongly dependent on the concentration of alcohols, alcohol expels camphor out of the heme cavity of the enzyme by affecting tertiary structure of Cyt P450cam as well as by modifying the solubility properties of camphor in aqueous medium, overview | Pseudomonas putida | (+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O | - |
? | |
| 1.14.15.1 | additional information | release of the substrate is caused both due to increased solubility of the substrate in solution in presence of alcohol and due to change in the tertiary structure of the active site of the enzyme, addition of alcohols to cytochrome P450cam causes a small change in the secondary structural elements but a significant change in the tertiary structural organization of the enzyme | Pseudomonas putida | ? | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 1.14.15.1 | More | release of the substrate is caused both due to increased solubility of the substrate in solution in presence of alcohol and due to change in the tertiary structure of the active site of the enzyme, addition of alcohols to cytochrome P450cam causes a small change in the secondary structural elements but a significant change in the tertiary structural organization of the enzyme | Pseudomonas putida |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.14.15.1 | CYP101 | - |
Pseudomonas putida |
| 1.14.15.1 | Cyt P450cam | - |
Pseudomonas putida |
| 1.14.15.1 | cytochrome p450cam | - |
Pseudomonas putida |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 1.14.15.1 | 7.4 | - |
assay at | Pseudomonas putida |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.14.15.1 | putidaredoxin | - |
Pseudomonas putida |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
