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Literature summary extracted from

  • Basom, E.; Spearman, J.; Thielges, M.
    Conformational landscape and the selectivity of cytochrome P450cam (2015), J. Phys. Chem. B, 119, 6620-6627 .
    View publication on PubMed

Application

EC Number Application Comment Organism
1.14.15.1 additional information knowledge of the conformational landscape is central to understanding P450 activity, which has important practical ramifications for the design of therapeutics with optimized pharmacokinetics, and the manipulation of P450s, and possibly other enzymes, for biotechnological applications Pseudomonas putida

Protein Variants

EC Number Protein Variants Comment Organism
1.14.15.1 Y96F site-directed mutagenesis, population and dynamics of the conformational states are largely unaltered by the Y96F mutation compared to the wild-type enzyme 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 + reduced putidaredoxin + O2 Pseudomonas putida
-
(+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.14.15.1 Pseudomonas putida P00183
-
-

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
-
?
1.14.15.1 additional information enzyme P450cam catalyzes the regioselective hydroxylation of d-camphor to 5-exo-hydroxycamphor. P450cam hydroxylates thiocamphor with a regioselectivity lower than camphor but higher than norcamphor. The high regioselectivity of camphor hydroxylation, the hydrogen bond (H-bond) between the camphor ketone and the side chain of active site residue Y96 influences the local electrostatics of the active site but has little effect on either the relative populations of conformational states or the nature of the energy landscapes within the conformations. Infrared spectrometric analysis of enzyme-substrate intercations, overview Pseudomonas putida ?
-
?
1.14.15.1 norcamphor + reduced putidaredoxin + O2
-
Pseudomonas putida ? + oxidized putidaredoxin + H2O
-
?
1.14.15.1 thiocamphor + reduced putidaredoxin + O2
-
Pseudomonas putida ? + oxidized putidaredoxin + H2O
-
?

Synonyms

EC Number Synonyms Comment Organism
1.14.15.1 cytochrome p450cam
-
Pseudomonas putida
1.14.15.1 P450cam
-
Pseudomonas putida

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.14.15.1 22
-
assay at room temperature Pseudomonas putida

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.14.15.1 7 7.4 assay at Pseudomonas putida

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.15.1 cytochrome P-450
-
Pseudomonas putida
1.14.15.1 putidaredoxin
-
Pseudomonas putida