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Literature summary extracted from

  • Tyson, C.T.; Lipscomb, J.D.; Gunsalus, I.C.
    The role of putidaredoxin and P450 cam in methylene hydroxylation (1972), J. Biol. Chem., 247, 5777-5784.
    View publication on PubMed

General Stability

EC Number General Stability Organism
1.14.15.1 freeze-thawing, less than 5% loss of activity of cytochrome P450cam in the presence of camphor Pseudomonas putida
1.14.15.1 putidaredoxin suffers degradation by repeated cycles of freezing and thawing Pseudomonas putida

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.14.15.1 cytoplasm
-
Pseudomonas putida 5737
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.14.15.1 Fe2+ requirement, enzyme complex with two FeS-protein components Pseudomonas putida

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.14.15.1 additional information
-
putidaredoxin reductase: MW 43000 Da, putidaredoxin: MW 12500 Da, cytochrome P450cam: MW 45000 Da, Pseudomonas putida PpG786, ultracentrifugal, diffusion and amino acid analysis 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 + putidaredoxin + O2 Pseudomonas putida
-
(R)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O i.e. (+)-exo-5-hydroxycamphor ?

Organism

EC Number Organism UniProt Comment Textmining
1.14.15.1 Pseudomonas putida
-
PpG786, mutant derived from PpG1
-
1.14.15.1 Pseudomonas putida
-
Accession Number PC00183
-

Oxidation Stability

EC Number Oxidation Stability Organism
1.14.15.1 under aerobic conditions, cytochrome P450cam decays at 25°C with t1/2 of 180 min to cytochrome P420, not rapidly in the presence of camphor Pseudomonas putida

Purification (Commentary)

EC Number Purification (Comment) Organism
1.14.15.1 PpG786 Pseudomonas putida

Reaction

EC Number Reaction Comment Organism Reaction ID
1.14.15.1 (+)-camphor + reduced putidaredoxin + O2 = (+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O multi-component mixed function oxidase, consisting of putidaredoxin reductase, putidaredoxin and cytochrome P450cam, heme-thiolate protein Pseudomonas putida

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.15.1 (+)-camphor + putidaredoxin + O2
-
Pseudomonas putida (R)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O i.e. (+)-exo-5-hydroxycamphor ?
1.14.15.1 (+)-camphor + putidaredoxin + O2 the (+)- and (-)-enantiomers serve as substrates Pseudomonas putida (R)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O i.e. (+)-exo-5-hydroxycamphor ?
1.14.15.1 1,2-campholide + putidaredoxin + O2
-
Pseudomonas putida 5-exo-hydroxy-1,2-campholide + oxidized putidaredoxin + H2O
-
?
1.14.15.1 additional information
-
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 7.4
-
assay at Pseudomonas putida

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.15.1 cytochrome m
-
Pseudomonas putida
1.14.15.1 FMN
-
Pseudomonas putida
1.14.15.1 NADH requirement, reduces reductase flavoprotein and putidaredoxin, but not P450cam, in the absence of camphor Pseudomonas putida
1.14.15.1 putidaredoxin cannot be replaced by other FeS-proteins or the phospholipid of the hepatic microsomal P450 system Pseudomonas putida