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Literature summary 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.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

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

Protein Variants

EC Number Protein Variants Comment Organism
1.14.15.1 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

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

Organism

EC Number Organism UniProt Comment Textmining
1.14.15.1 Pseudomonas putida
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.14.15.1 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)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 CYP101A1
-
Pseudomonas putida
1.14.15.1 cytochrome p450cam
-
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 cytochrome P450cam Pseudomonas putida
1.14.15.1 putidaredoxin
-
Pseudomonas putida

General Information

EC Number General Information Comment Organism
1.14.15.1 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