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Literature summary extracted from

  • OuYang, B.; Pochapsky, S.S.; Pagani, G.M.; Pochapsky, T.C.
    Specific effects of potassium ion binding on wild-type and L358P cytochrome P450cam (2006), Biochemistry, 45, 14379-14388.
    View publication on PubMedView publication on EuropePMC

Protein Variants

EC Number Protein Variants Comment Organism
1.14.15.1 L358P site-directed mutagenesis, spin-state equilibrium in the L358P mutant is more sensitive to K+ than the wild-type enzyme Pseudomonas putida

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.14.15.1 Fe3+ the enzyme requires K+ to drive formation of the characteristic high-spin state of the heme Fe3+ upon substrate binding Pseudomonas putida
1.14.15.1 K+ effects of potassium ion binding on camphor-bound oxidized, camphor-bound reduced, and on CO-bound reduced wild-type and L358P enzyme, detailed overview, the enzyme requires K+ to drive formation of the characteristic high-spin state of the heme Fe3+ upon substrate binding, K+ binding site, overview Pseudomonas putida
1.14.15.1 Tl+ can substitute for K+ and minimize the effects of K+ absence on conformational perturbences upon putdaredoxin binding 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 + O2 + reduced putidaredoxin Pseudomonas putida
-
 (+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.14.15.1 Pseudomonas putida
-
 variant C334A conferred to as wild-type
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.14.15.1 (+)-camphor + reduced putidaredoxin + O2 = (+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O K+ plays an important role in substrate binding and structural and conformational stability of the enzyme 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 CYP101
-
 Pseudomonas putida
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 25
-
 assay at Pseudomonas putida

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.14.15.1 7.4
-
-
 Pseudomonas putida

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.15.1 putidaredoxin binding causes conformational changes involving K+, in absence of K+ multiple conformations occur, overview Pseudomonas putida