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Literature summary extracted from

  • Hiruma, Y.; Gupta, A.; Kloosterman, A.; Olijve, C.; Oelmez, B.; Hass, M.; Ubbink, M.
    Hot-spot residues in the cytochrome P450cam-putidaredoxin binding interface (2014), ChemBioChem, 15, 80-86 .
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
1.14.15.1 D125A site-directed mutagenesis Pseudomonas putida
1.14.15.1 H352A site-directed mutagenesis Pseudomonas putida
1.14.15.1 H361A site-directed mutagenesis Pseudomonas putida
1.14.15.1 additional information interaction analysis of enzyme wild-type and mutant (D125A, H352A, and H361A) proteins with putidaredoxxin wild-type and mutant (Y33A, S42A, and S44A) proteins, kinetics, overview 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 enzyme-cofactor interaction kinetics of wild-type and mutant enzymes, steady-state and stopped-flow reaction kinetics, overview Pseudomonas putida

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.14.15.1 Fe2+ in putidaredoxin (Pdx), a ferredoxin containing a [2Fe-2S] cluster 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 P00183
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.15.1 (+)-camphor + reduced putidaredoxin + NADH + H+ + O2 the catalytic cycle of P450cam requires two electrons, both of which are donated by putidaredoxin (Pdx), a ferredoxin containing a [2Fe-2S] cluster, structures of the Pdx-P450cam complex, overview Pseudomonas putida (+)-exo-5-hydroxycamphor + oxidized putidaredoxin + NAD+ + H2O
-
?
1.14.15.1 (+)-camphor + reduced putidaredoxin + O2
-
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 22
-
assay at Pseudomonas putida

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.14.15.1 17.9
-
NADH pH 7.4, 22°C, recombinant mutant H352A enzyme with mutant S42A putidaredoxin Pseudomonas putida
1.14.15.1 26.3
-
NADH pH 7.4, 22°C, recombinant mutant D125A enzyme with mutant Y33A putidaredoxin Pseudomonas putida
1.14.15.1 34.1
-
NADH pH 7.4, 22°C, recombinant mutant H361A enzyme with wild-type putidaredoxin Pseudomonas putida
1.14.15.1 34.1
-
NADH pH 7.4, 22°C, recombinant wild-type enzyme with mutant S42A putidaredoxin Pseudomonas putida
1.14.15.1 34.9
-
NADH pH 7.4, 22°C, recombinant wild-type enzyme with mutant Y33A putidaredoxin Pseudomonas putida
1.14.15.1 36.3
-
NADH pH 7.4, 22°C, recombinant mutant H352A enzyme with wild-type putidaredoxin Pseudomonas putida
1.14.15.1 37.4
-
NADH pH 7.4, 22°C, recombinant wild-type enzyme with mutant S44Aputidaredoxin Pseudomonas putida
1.14.15.1 38.2
-
NADH pH 7.4, 22°C, recombinant wild-type enzyme with wild-type putidaredoxin Pseudomonas putida
1.14.15.1 40.3
-
NADH pH 7.4, 22°C, recombinant mutant D125A enzyme with wild-type putidaredoxin 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 P450
-
Pseudomonas putida
1.14.15.1 NADH
-
Pseudomonas putida
1.14.15.1 putidaredoxin the catalytic cycle of P450cam requires two electrons, both of which are donated by putidaredoxin (Pdx), a ferredoxin containing a [2Fe-2S] cluster, structures of the Pdx-P450cam complex, potential electron transfer pathways and interactions between Pdx Asp38 and P450cam Arg112, as well as hydrophobic contacts between the Pdx Trp106 and P450cam residues, favorable interactions exist between Pdx Tyr33 and P450cam Asp125, as well as between Pdx Ser42 and P450cam His352, overview Pseudomonas putida

General Information

EC Number General Information Comment Organism
1.14.15.1 malfunction alanine substitutions of the residues involved in putidaredoxin-enzyme interactions do not influence the rates of electron transfer, interaction analysis of enzyme wild-type and mutant (D125A, H352A, and H361A) proteins with putidaredoxxin wild-type and mutant (Y33A, S42A, and S44A) proteins, kinetics, overview Pseudomonas putida
1.14.15.1 additional information structures of the Pdx-P450cam complex, potential electron transfer pathways and interactions between Pdx Asp38 and P450cam Arg112, as well as hydrophobic contacts between the Pdx Trp106 and P450cam residues, favorable interactions exist between Pdx Tyr33 and P450cam Asp125, as well as between Pdx Ser42 and P450cam His352, overview Pseudomonas putida