This enzyme belongs to
the family of iron(II)-dependent oxygenases, which typically incorporate one atom of dioxygen into the substrate and one atom into the succinate carboxylate group. The mechanism is complex, but is believed to involve ordered binding of 2-oxoglutarate to the
iron(II) containing enzyme followed by substrate. Binding of substrate causes displacement of a water molecule from the iron(II) cofactor, leaving a vacant coordination position to which dioxygen binds. A rearrangement occurs to form a high energy iron-oxygen species (which is generally thought to be an iron(IV)=O species) that performs the actual oxidation reaction.[2][3]
Nomenclature
The
systematic name of this enzyme class is phytanoyl-CoA, 2-oxoglutarate:oxygen oxidoreductase (2-hydroxylating). These enzymes are also called phytanoyl-CoA hydroxylases and phytanoyl-CoA alpha-hydroxylases.[4]
Iron(II) and 2OG-dependent oxygenases are common in
microorganisms, plants, and animals; the
human genome is predicted to contain about 80 examples, and the
model plantArabidopsis thaliana likely contains more.[2] In plants and microorganisms this enzyme family is associated with a large diversity of oxidative reactions.[6]