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Literature summary extracted from

  • Hiruma, Y.; Gupta, A.; Kloosterman, A.; Olijve, C.; Olmez, B.; Hass, M.A.; Ubbink, M.
    Hot-spot residues in the cytochrome p450cam-putidaredoxin binding interface (2014), ChemBioChem, 15, 80-86.
    View publication on PubMed

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.14.15.1 additional information
-
 additional information steady-state turnover activities of the P450cam catalytic cycle, overview Pseudomonas putida

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.14.15.1 Fe2+ the enzyme contains [2Fe-2S] cluster and cytochrome P450 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 + reduced putidaredoxin + O2 Pseudomonas putida
-
 (+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
-
 ?

Organism

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.15.1 (+)-camphor + reduced putidaredoxin + O2
-
 Pseudomonas putida (+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
-
 ?
1.14.15.1 (+)-camphor + reduced putidaredoxin + O2 the enzyme shows regio- and stereospecific hydroxylation. Activation and cleavage of the oxygen molecule in the P450cam catalytic cycle is accompanied by two electron transfers from putidaredoxin. Ferric P450cam can accept the first electron from diverse chemical reductants and putidaredoxin homologues, but the second requires putidaredoxin as donor Pseudomonas putida (+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.14.15.1 CYP101A1
-
 Pseudomonas putida
1.14.15.1 P450cam
-
 Pseudomonas putida

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.15.1 cytochrome P450 cytochrome P450cam, importance and role of the polar residues, e.g. Tyr33, involved in the Pdx-P450cam interaction, overview. Interaction key residues are Pdx Asp38, Arg66, and Trp106, as well as P450cam Arg109 and Arg112, crystal structure of the Pdx-P450cam complex Pseudomonas putida
1.14.15.1 putidaredoxin the physiological electron transfer partner protein contains a [2Fe-2S] cluster, energetic importance and role of the polar residues, e.g. Tyr33, involved in the Pdx-P450cam interaction, overview. Interaction key residues are Pdx Asp38, Arg66, and Trp106, as well as P450cam Arg109 and Arg112, crystal structure of the Pdx-P450cam complex Pseudomonas putida