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Literature summary extracted from

  • Spolitak, T.; Dawson, J.H.; Ballou, D.P.
    Rapid kinetics investigations of peracid oxidation of ferric cytochrome P450cam: nature and possible function of compound ES (2006), J. Inorg. Biochem., 100, 2034-2044.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
1.14.15.1 Y75F the mutant shows an altered active site structure influencing catalysis Pseudomonas putida
1.14.15.1 Y96F the mutant shows an altered active site structure influencing catalysis Pseudomonas putida
1.14.15.1 Y96F/Y75F the mutant shows an altered active site structure influencing catalysis Pseudomonas putida

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.14.15.1 additional information
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 additional information stopped-flow kinetic analysis of the peracid oxidation of the wild-type enzyme and substrate-free ferric mutant enzymes overview Pseudomonas putida

Organism

EC Number Organism UniProt Comment Textmining
1.14.15.1 Pseudomonas putida P00183
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.15.1 3-chloroperbenzoic acid + O2 + reduced putidaredoxin compound I, ferryl iron plus a porphyrin pi-cation radical (Fe(IV)=O/Por(+)), and compound ES, Fe(IV)=O/Tyr(), in reactions of substrate-free ferric enzyme with 3-chloroperbenzoic acid, compound ES arises by intramolecular electron transfer from nearby tyrosines to the porphyrin pi-cation radical of compound I, active site changes influence electron transfer from nearby tyrosines and affect formation of intermediates, the tyrosyl radical is assigned to Tyr96 for wild type or to Tyr75 for the Y96F variant, overview Pseudomonas putida ?
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 ?

Synonyms

EC Number Synonyms Comment Organism
1.14.15.1 cytochrome p450cam
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 Pseudomonas putida

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.15.1 putidaredoxin
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 Pseudomonas putida