Abstract
Aldehyde oxidases (AOX) belong to the xanthine oxidase (XO) family of enzymes that contain a Mo catalytic site (Moco), two 2Fe-2S centres and an FAD site involved in electron transfer. Reactivity appears to be conferred solely by the Mo centre, while specificity is controlled by amino acid residues in the binding pocket that differ in both enzymes. XO is involved in the last steps of purine catabolism and converts xanthine to uric acid with formation of superoxide. AOX also accepts O2 as the final electron acceptor and has also an important role in cellular redox stress. AOX is an enzyme with a still unclear physiological role but is involved in drug metabolism. Along with cyt P450, it metabolizes different classes of drugs and xenobiotics being an enzyme of emerging significance in phase-I drug metabolism and pharmacokinetics. The crystallization and structure determination of human AOX1 and mouseAOX3 brought new insights into structure and mechanisms underlying substrate/inhibitor binding as well as catalytic activities. The elucidation of the 3D structure of hAOX1 in free form and in complex with substrate phthalazine and noncompetitive inhibitor thioridazine revealed novel structural features and a new and unexpected inhibition site structurally conserved among AOXs and XOs.
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