Cytochrome P450 cam

Cytochrome P450 camphor 5-monooxygenase is a bacterial enzyme originally from Pseudomonas putida, which catalyzes a critical step in the metabolism of camphor. In 1987, Cytochrome P450cam was the first cytochrome P450 three-dimensional protein structure solved by X-ray crystallography.[1]

Camphor 5-monooxygenase
Identifiers
OrganismPseudomonas putida
SymbolcamC
Alt. symbolscyp101
UniProtP00183
Other data
EC number1.14.15.1
Putidaredoxin
Identifiers
OrganismPseudomonas putida
SymbolcamB
Alt. symbolsPDX
UniProtP00259
Putidaredoxin reductase CamA
Identifiers
OrganismPseudomonas putida
SymbolcamA
Alt. symbolsPdr
UniProtP16640
Other data
EC number1.18.1.5

It is a heterotrimeric protein derived from the products of three genes: a cytochrome P450 enzyme (encoded by the CamC gene from the CYP family CYP101), a Putidaredoxin (encoded by the CamB gene) complexed with cofactors 2Fe-2S, a NADH-dependent Putidaredoxin reductase (encoded by the CamA gene).[2]

References
  1. Poulos, Thomas L.; Finzel, Barry C.; Howard, Andrew J. (June 1987). "High-resolution crystal structure of cytochrome P450cam". Journal of Molecular Biology. 195 (3): 687–700. doi:10.1016/0022-2836(87)90190-2.
  2. Li, Shuying; Wackett, Lawrence P. (1993). "Reductive dehalogenation by cytochrome P450CAM: Substrate binding and catalysis". Biochemistry. 32 (36): 9355–9361. doi:10.1021/bi00087a014.
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