Literature summary for 1.14.15.1 extracted from

Asciutto, E.K.; Young, M.J.; Madura, J.; Pochapsky, S.S.; Pochapsky, T.C.
Solution structural ensembles of substrate-free cytochrome P450(cam) (2012), Biochemistry, 51, 3383-3393.

Search for more literature for 1.14.15.1

Cloned(Commentary)

Cloned (Comment)	Organism
expression of C334A enzyme mutant in Escherichia coli strain NCM533	Pseudomonas putida

Protein Variants

Protein Variants	Comment	Organism
C334A	site-directed mutagenesis, the C334A mutant is spectroscopically and enzymatically identical to the wild type but does not form dimers in solution, and so is more suitable for NMR structure analysis than the wild type enzyme	Pseudomonas putida

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Fe2+	cytochrome P450 containing enzyme	Pseudomonas putida

Organism

Organism	UniProt	Comment	Textmining
Pseudomonas putida	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant C334A enzyme mutant from Escherichia coli strain NCM533 by ammonium sulfate fractionation, dialysis, anion exchange chromatography, and gel filtration	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	-	?

Synonyms

Synonyms	Comment	Organism
CYP101A1	-	Pseudomonas putida
cytochrome p450cam	-	Pseudomonas putida

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7.4	-	assay at	Pseudomonas putida

Cofactor

Cofactor	Comment	Organism	Structure
cytochrome P450	cytochrome P450cam	Pseudomonas putida
putidaredoxin	-	Pseudomonas putida

General Information

General Information	Comment	Organism
additional information	NMR structure analysis of the enzyme CYP101A1 with substrate (+)-camphor bound the active site and substrate-free enzyme after removal of (+)-camphor, molecular dynamics simulations and modeling, overview. Portions of a beta-rich region adjacent to the active site shift so as to partially occupy the vacancy left by removal of substrate. The accessible volume of the active site is reduced in the substrate-free enzyme relative to the substrate-bound structure	Pseudomonas putida

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Release 2023.1 (January 2023)