Cytochrome P450cam monooxygenase (P450cam (also known as CYP101A1))

Cytochrome P450cam monooxygenase (P450cam, CYP101A1) is a bacterial heme-thiolate enzyme primarily known for catalyzing the hydroxylation of camphor to 5-exo-hydroxycamphor in *Pseudomonas putida*.[1][5][6] It is the prototypical member of the cytochrome P450 superfamily and has been extensively studied as a structural and mechanistic model for mammalian P450 enzymes.[4] P450cam uses electrons transferred from NADH via ferredoxin and ferredoxin reductase to activate molecular oxygen, inserting one atom of oxygen into the substrate while reducing the other to water.[1] Its active site contains a heme iron coordinated by a conserved cysteine thiolate ligand and excludes water upon substrate binding to enable catalysis.[3] While not itself a therapeutic drug target, P450cam has been fundamental in elucidating the catalytic mechanisms, substrate selectivity, conformational flexibility, and inhibitor interactions of the broader cytochrome P450 family, including the human isoforms involved in drug metabolism and xenobiotic detoxification[2][7].

Other names

Cytochrome P450camCYP101A1camphor 5-monooxygenase

Monooxygenation (insertion of one atom of molecular oxygen into organic substrate, utilizing a heme cofactor and electron transfer)