Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.14.15.1 extracted from

  • Pochapsky, S.S.; Dang, M.; OuYang, B.; Simorellis, A.K.; Pochapsky, T.C.
    Redox-dependent dynamics in cytochrome P450cam (2009), Biochemistry, 48, 4254-4261.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
mutant C334A transformed into chemically competent Escherichia coli NCM533 cells Pseudomonas putida

Protein Variants

Protein Variants Comment Organism
C334A is identical spectroscopically and enzymatically to wild-type but does not dimerize in solution at high concentrations Pseudomonas putida

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ local protein backbone dynamics of CYP101 depend upon the oxidation and ligation state of the heme iron Pseudomonas putida

Organism

Organism UniProt Comment Textmining
Pseudomonas putida
-
-
-

Purification (Commentary)

Purification (Comment) Organism
by gel filtration Pseudomonas putida

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(+)-camphor + O2 + reduced putidaredoxin the reduced enzyme exhibits lower-amplitude motions of secondary structural features than the oxidized enzyme on all of the time scales accessible, and these differences are more pronounced in regions of the enzyme involved in substrate access to the active site (B' helix and beta3 and beta5 sheets) and binding of putidaredoxin (C and L helices), the iron-sulfur protein that acts as the effector and reductant of CYP101 in vivo Pseudomonas putida (+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
-
?

Synonyms

Synonyms Comment Organism
camphor hydroxylase cytochrome P450cam
-
Pseudomonas putida
CYP101
-
Pseudomonas putida
P450cam
-
Pseudomonas putida

Cofactor

Cofactor Comment Organism Structure
putidaredoxin
-
Pseudomonas putida