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Literature summary extracted from

  • Swart, M.; Groenhof, A.R.; Ehlers, A.W.; Lammertsma, K.
    Substrate binding in the active site of cytochrome P450cam (2005), Chem. Phys. Lett., 403, 35-41.
No PubMed abstract available

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
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.14.15.1 (+)-camphor + reduced putidaredoxin + O2 = (+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O active binding of substrate camphor, analysis by density functional theory calculations, residue Tyr96 is important forming a strong hydrogen bond, catalytic cycle of cytochrome P450, the strong hydrogen bonding is not affected by the enzyme's environment, reaction mechanism, 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
-
 Pseudomonas putida (+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.14.15.1 cytochrome p450cam
-
 Pseudomonas putida
1.14.15.1 moe the enzyme belongs to the family of cytochrome P450 enzymes Pseudomonas putida

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.15.1 putidaredoxin
-
 Pseudomonas putida