Literature summary for 1.14.15.1 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.

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Protein Variants

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

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
additional information	-	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

Organism	UniProt	Comment	Textmining
Pseudomonas putida	P00183	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
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	?	-	?

Synonyms

Synonyms	Comment	Organism
cytochrome p450cam	-	Pseudomonas putida

Cofactor

Cofactor	Comment	Organism	Structure
putidaredoxin	-	Pseudomonas putida

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Release 2023.1 (January 2023)