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Literature summary extracted from

  • Kuznetsov, V.Y.; Poulos, T.L.; Sevrioukova, I.F.
    Putidaredoxin-to-cytochrome P450cam electron transfer: differences between the two reductive steps required for catalysis (2006), Biochemistry, 45, 11934-11944.
    View publication on PubMedView publication on EuropePMC

Protein Variants

EC Number Protein Variants Comment Organism
1.14.15.1 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
1.14.15.1 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
1.14.15.1 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
1.14.15.1 R66A site-directed mutagenesis, reduced mutant electron transfer activity and increased Kd values for ferric P450cam compared to the wild-type enzyme Pseudomonas putida
1.14.15.1 R66E site-directed mutagenesis, reduced mutant electron transfer activity and increased Kd values for ferric P450cam compared to the wild-type enzyme Pseudomonas putida
1.14.15.1 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
1.14.15.1 W106F site-directed mutagenesis, reduced mutant electron transfer activity and increased Kd values for ferric P450cam compared to the wild-type enzyme Pseudomonas putida
1.14.15.1 Y33A site-directed mutagenesis, reduced mutant electron transfer activity and increased Kd values for ferric P450cam compared to the wild-type enzyme Pseudomonas putida
1.14.15.1 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]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.14.15.1 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

EC Number Metals/Ions Comment Organism Structure
1.14.15.1 Fe2+ the reaction cycle requires two distinct electron transfer processes from the [2Fe-2S] containing putidaredoxin to P450cam 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 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

EC Number Organism UniProt Comment Textmining
1.14.15.1 Pseudomonas putida
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.14.15.1 (+)-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
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.15.1 (+)-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
-
 ?
1.14.15.1 (+)-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

EC Number Synonyms Comment Organism
1.14.15.1 cytochrome p450cam
-
 Pseudomonas putida

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.14.15.1 25
-
 assay at Pseudomonas putida

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.14.15.1 7.5
-
 assay at Pseudomonas putida

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.15.1 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