Camphor 5-monooxygenase (P450cam)

Camphor 5-monooxygenase, commonly known as P450cam or CYP101A1, is a soluble cytochrome P450 enzyme derived from the soil bacterium Pseudomonas putida. It initiates the microbial degradation of camphor by catalyzing the regioselective hydroxylation of (+)-camphor to (+)-exo-5-hydroxycamphor, a reaction that requires molecular oxygen and a specific electron transport chain involving putidaredoxin and putidaredoxin reductase. Historically, P450cam is significant as the first cytochrome P450 to have its three-dimensional structure solved by X-ray crystallography, serving as the definitive model for understanding the catalytic mechanisms and structural biology of the entire P450 superfamily. While it is not a therapeutic target in human medicine, its high selectivity and well-characterized active site make it a valuable tool in biocatalysis and protein engineering for the synthesis of hydroxylated terpenoids and the degradation of environmental pollutants. It is also frequently used in research as a surrogate for studying the fundamental principles of heme-mediated monooxygenation and drug metabolism.

Other names

Cytochrome P450camCYP101A1Camphor 5-exo-hydroxylase2-bornanone 5-exo-hydroxylaseMethylene hydroxylaseD-camphor-exo-hydroxylasecamC

The enzyme catalyzes the regioselective and stereoselective 5-exo-hydroxylation of (+)-camphor using molecular oxygen and electrons transferred from NADH via a specific redox chain consisting of putidaredoxin reductase and putidaredoxin.