page_title: Phytanoyl-CoA dioxygenase
hierarchical_section_title: Phytanoyl-CoA dioxygenase
caption_attribution_description: English: PyMol rendering of human phytanoyl-CoA 2-hydroxylase (PAHX, PhyH) from PDB 2A1X. The Fe(II) cofactor is shown as an orange sphere, coordinated by two histidine and one aspartate residue (shown in green) and by the 2-oxoglutarate cosubstrate (shown in yellow).
context_page_description: In enzymology, a phytanoyl-CoA dioxygenase is an enzyme that catalyzes the chemical reaction
  phytanoyl-CoA + 2-oxoglutarate + O₂ 2-hydroxyphytanoyl-CoA + succinate + CO₂
  The three substrates of this enzyme are phytanoyl-CoA, 2-oxoglutarate, 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 that performs the actual oxidation reaction.
context_section_description: In enzymology, a phytanoyl-CoA dioxygenase (EC 1.14.11.18) is an enzyme that catalyzes the chemical reaction
  phytanoyl-CoA + 2-oxoglutarate + O₂  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.
caption: The structure of human PAHX (PDB: 2A1X​). The Fe(II) cofactor is shown as an orange sphere, coordinated by two histidine and one aspartate residue (shown in green) and by the 2-oxoglutarate cosubstrate (shown in yellow).[1]
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