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Literature summary for 1.14.15.1 extracted from
- Hot-spot residues in the cytochrome P450cam-putidaredoxin binding interface (2014), ChemBioChem, 15, 80-86 .
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| D125A | site-directed mutagenesis | Pseudomonas putida |
| H352A | site-directed mutagenesis | Pseudomonas putida |
| H361A | site-directed mutagenesis | Pseudomonas putida |
| additional information | interaction analysis of enzyme wild-type and mutant (D125A, H352A, and H361A) proteins with putidaredoxxin wild-type and mutant (Y33A, S42A, and S44A) proteins, kinetics, overview | Pseudomonas putida |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | enzyme-cofactor interaction kinetics of wild-type and mutant enzymes, steady-state and stopped-flow reaction kinetics, overview | Pseudomonas putida |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Fe2+ | in putidaredoxin (Pdx), a ferredoxin containing a [2Fe-2S] cluster | Pseudomonas putida |  |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| (+)-camphor + reduced putidaredoxin + O2 | Pseudomonas putida | - |
(+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Pseudomonas putida | P00183 | - |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| (+)-camphor + reduced putidaredoxin + NADH + H+ + O2 | the catalytic cycle of P450cam requires two electrons, both of which are donated by putidaredoxin (Pdx), a ferredoxin containing a [2Fe-2S] cluster, structures of the Pdx-P450cam complex, overview | Pseudomonas putida | (+)-exo-5-hydroxycamphor + oxidized putidaredoxin + NAD+ + H2O | - |
? | |
| (+)-camphor + reduced putidaredoxin + O2 | - |
Pseudomonas putida | (+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| cytochrome p450cam | - |
Pseudomonas putida |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 22 | - |
assay at | Pseudomonas putida |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 17.9 | - |
NADH | pH 7.4, 22°C, recombinant mutant H352A enzyme with mutant S42A putidaredoxin | Pseudomonas putida | |
| 26.3 | - |
NADH | pH 7.4, 22°C, recombinant mutant D125A enzyme with mutant Y33A putidaredoxin | Pseudomonas putida | |
| 34.1 | - |
NADH | pH 7.4, 22°C, recombinant mutant H361A enzyme with wild-type putidaredoxin | Pseudomonas putida | |
| 34.1 | - |
NADH | pH 7.4, 22°C, recombinant wild-type enzyme with mutant S42A putidaredoxin | Pseudomonas putida | |
| 34.9 | - |
NADH | pH 7.4, 22°C, recombinant wild-type enzyme with mutant Y33A putidaredoxin | Pseudomonas putida | |
| 36.3 | - |
NADH | pH 7.4, 22°C, recombinant mutant H352A enzyme with wild-type putidaredoxin | Pseudomonas putida | |
| 37.4 | - |
NADH | pH 7.4, 22°C, recombinant wild-type enzyme with mutant S44Aputidaredoxin | Pseudomonas putida | |
| 38.2 | - |
NADH | pH 7.4, 22°C, recombinant wild-type enzyme with wild-type putidaredoxin | Pseudomonas putida | |
| 40.3 | - |
NADH | pH 7.4, 22°C, recombinant mutant D125A enzyme with wild-type putidaredoxin | Pseudomonas putida | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.4 | - |
assay at | Pseudomonas putida |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| cytochrome P450 | - |
Pseudomonas putida | |
| NADH | - |
Pseudomonas putida | |
| putidaredoxin | the catalytic cycle of P450cam requires two electrons, both of which are donated by putidaredoxin (Pdx), a ferredoxin containing a [2Fe-2S] cluster, structures of the Pdx-P450cam complex, potential electron transfer pathways and interactions between Pdx Asp38 and P450cam Arg112, as well as hydrophobic contacts between the Pdx Trp106 and P450cam residues, favorable interactions exist between Pdx Tyr33 and P450cam Asp125, as well as between Pdx Ser42 and P450cam His352, overview | Pseudomonas putida |
General Information
| General Information | Comment | Organism |
|---|---|---|
| malfunction | alanine substitutions of the residues involved in putidaredoxin-enzyme interactions do not influence the rates of electron transfer, interaction analysis of enzyme wild-type and mutant (D125A, H352A, and H361A) proteins with putidaredoxxin wild-type and mutant (Y33A, S42A, and S44A) proteins, kinetics, overview | Pseudomonas putida |
| additional information | structures of the Pdx-P450cam complex, potential electron transfer pathways and interactions between Pdx Asp38 and P450cam Arg112, as well as hydrophobic contacts between the Pdx Trp106 and P450cam residues, favorable interactions exist between Pdx Tyr33 and P450cam Asp125, as well as between Pdx Ser42 and P450cam His352, overview | Pseudomonas putida |
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