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Literature summary extracted from

  • Hayashi, T.; Harada, K.; Sakurai, K.; Shimada, H.; Hirota, S.
    A role of the heme-7-propionate side chain in cytochrome P450cam as a gate for regulating the access of water molecules to the substrate-binding site (2009), J. Am. Chem. Soc., 131, 1398-1400.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.14.15.1 the reconstituted P450cam at 1.8 A resolution reveals that the asymmetric one-legged heme is incorporated into the heme pocket in the same plane and in essentially the same conformation as the heme of the wild-type. A unique array of water molecules extending from the Tyr96 residue to the outside of the protein are present in the crystal structure Pseudomonas putida

Protein Variants

EC Number Protein Variants Comment Organism
1.14.15.1 additional information removal of heme-7-propionate decreases the (+)-camphor affinity by approximately 3fold, but exerts less of an influence on the other steps of the catalytic cycle of the monooxygenation reaction catalyzed by P450cam, does not exert an influence on the structure and electronic properties of the heme Pseudomonas putida

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.14.15.1 Iron purified reconstituted P450cam exhibits the ferrous CO-bound P450cam spectrum with the characteristic Soret band at 446 nm, indicating that the thiolate of Cys357 is ligated to the heme iron of the one-legged heme as seen in the wild-type protein Pseudomonas putida

Organism

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

Purification (Commentary)

EC Number Purification (Comment) Organism
1.14.15.1
-
 Pseudomonas putida

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.15.1 (+)-camphor + O2 + reduced putidaredoxin the 7-propionate side chain plays a role in maintaining the high affinity of cytochrome P450cam for its substrate, the Asp297 and Gln322 residues are capable of undergoing a 7-propionate-associated conformational change in the protein interior Pseudomonas putida exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
-
 ?

Synonyms

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

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.15.1 putidaredoxin
-
 Pseudomonas putida