Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.14.15.1 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
Search for more literature for 1.14.15.1

KM Value [mM]

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

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ the enzyme contains [2Fe-2S] cluster and cytochrome P450 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
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(+)-camphor + reduced putidaredoxin + O2
-
 Pseudomonas putida (+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
-
 ?
(+)-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

Synonyms Comment Organism
CYP101A1
-
 Pseudomonas putida
P450cam
-
 Pseudomonas putida

Cofactor

Cofactor Comment Organism Structure
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
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