Camphor 5-monooxygenase


In enzymology, a camphor 5-monooxygenase is an enzyme that catalyzes the chemical reaction
The 3 substrates of this enzyme are -camphor, putidaredoxin, and O2, whereas its 3 products are -exo-5-hydroxycamphor, oxidized putidaredoxin, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with reduced iron-sulfur protein as one donor, and incorporation o one atom of oxygen into the other donor. The systematic name of this enzyme class is -camphor,reduced putidaredoxin:oxygen oxidoreductase . Other names in common use include camphor 5-exo-methylene hydroxylase, 2-bornanone 5-exo-hydroxylase, bornanone 5-exo-hydroxylase, camphor 5-exo-hydroxylase, camphor 5-exohydroxylase, camphor hydroxylase, d-camphor monooxygenase, methylene hydroxylase, methylene monooxygenase, D-camphor-exo-hydroxylase, and camphor methylene hydroxylase. It employs one cofactor, heme.

Structural studies

As of late 2007, 58 structures have been solved for this class of enzymes, with PDB accession codes,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, and.