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Literature summary for 1.14.15.1 extracted from

  • Asciutto, E.K.; Dang, M.; Pochapsky, S.S.; Madura, J.D.; Pochapsky, T.C.
    Experimentally restrained molecular dynamics simulations for characterizing the open states of cytochrome P450cam (2011), Biochemistry, 50, 1664-1671.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression of P450cam C334A in Escherichia coli NCM533 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

Localization

Localization Comment Organism GeneOntology No. Textmining
soluble
-
Pseudomonas putida
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ heme protein Pseudomonas putida

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
46000
-
1 * 46000 Pseudomonas putida

Organism

Organism UniProt Comment Textmining
Pseudomonas putida P00183
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant P450cam C334A from Escherichia coli NCM533. Protein purification includes a protamine sulfate cut to precipitate nucleic acids, and an ammonium sulfate cut to isolate CYP101A1 Pseudomonas putida

Subunits

Subunits Comment Organism
monomer 1 * 46000 Pseudomonas putida
More three-dimensional structure and dynamics of the open and closed states of CYP101A1, NMR analysis and molecular dynamics simulations, overview Pseudomonas putida

Synonyms

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

Cofactor

Cofactor Comment Organism Structure
heme
-
Pseudomonas putida

General Information

General Information Comment Organism
additional information CYP101A1 is a soluble monomeric heme-containing camphor monooxygenase Pseudomonas putida