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.
Iron(II)-dependent oxygenases are widespread in micro-organisms, plants and animals are involved in many pathways of medical importance (the hypoxia response, carnitine biosynthesis, adult Refsum's disease) and biotechnological importance (most notably biosynthesis of cephalosporins, cephamycins and clavulanic acid). A sequence related enzyme, IPNS (which does not use 2-oxoglutarate) catalyses a key step in the biosynthesis of the penicillin nucleus.
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