Phytanoyl-CoA dioxygenase

In enzymology, a phytanoyl-CoA dioxygenase (EC 1.14.11.18) is an enzyme that catalyzes the chemical reaction

phytanoyl-CoA + 2-oxoglutarate + O₂ ${\displaystyle \rightleftharpoons }$ 2-hydroxyphytanoyl-CoA + succinate + CO₂

The three substrates of this enzyme are phytanoyl-CoA, 2-oxoglutarate (2OG), and O₂, whereas its three products are 2-hydroxyphytanoyl-CoA, succinate, and CO₂.

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.