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

BRENDA support

Literature summary for 1.14.15.1 extracted from

  • Lee, Y.T.; Wilson, R.F.; Rupniewski, I.; Goodin, D.B.
    P450cam visits an open conformation in the absence of substrate (2010), Biochemistry, 49, 3412-3419.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
overexpression of P450cam mutant C334A in Escherichia coli strain BL21(DE3) Pseudomonas putida

Crystallization (Commentary)

Crystallization (Comment) Organism
camphor-free or camphor-bound P450cam mutant C334A in the absence of substrate and at high and low K+ concentration, protein in 50 mM Tris, pH 7.4, with or without 2-4 mM camphor, mixed with crystallization solution containing 50 mM Tris, pH 7.4, and 12-22% PEG 8000 with and without 200 mM K+, sitting drop vapour diffusion method, 6°C, X-ray diffraction structure determination and analysis at 1.50-1.79 A resolution Pseudomonas putida

Protein Variants

Protein Variants Comment Organism
C334A the mutation of P450cam increases the protein stability compared to the wild-type enzyme Pseudomonas putida

Organism

Organism UniProt Comment Textmining
Pseudomonas putida P00183
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant P450cam mutant C334A from Escherichia coli strain BL21(DE3) by anion exchange chromatography and gel filtration Pseudomonas putida

Subunits

Subunits Comment Organism
More the camphor-free structure is in an open conformation characterized by a water-filled channel created by the retraction of the F and G helices, disorder of the B' helix, and loss of the K+ binding. site. Presence of K+ alone does not alter the open conformation, while camphor alone is sufficient for closure of the channel Pseudomonas putida

Synonyms

Synonyms Comment Organism
P450cam
-
Pseudomonas putida