Structural basis for the role of mammalian aldehyde oxidases in the metabolism of drugs and xenobiotics

Maria João Romão, Catarina Coelho, Teresa Santos-Silva, Alessandro Foti, Mineko Terao, Enrico Garattini, Silke Leimkühler

Research output: Contribution to journalReview articlepeer-review


Aldehyde oxidases (AOXs) are molybdo-flavoenzymes characterized by broad substrate specificity, oxidizing aromatic/aliphatic aldehydes into the corresponding carboxylic acids and hydroxylating various heteroaromatic rings. Mammals are characterized by a complement of species-specific AOX isoenzymes, that varies from one in humans (AOX1) to four in rodents (AOX1, AOX2, AOX3 and AOX4). The physiological function of mammalian AOX isoenzymes is unknown, although human AOX1 is an emerging enzyme in phase-I drug metabolism. Indeed, the number of therapeutic molecules under development which act as AOX substrates is increasing. The recent crystallization and structure determination of human AOX1 as well as mouse AOX3 has brought new insights into the mechanisms underlying substrate/inhibitor binding as well as the catalytic activity of this class of enzymes.

Original languageEnglish
Pages (from-to)39-47
Number of pages9
JournalCurrent Opinion in Chemical Biology
Publication statusPublished - Apr 2017


  • Aldehyde Oxidase
  • Animals
  • Enzyme Inhibitors
  • Humans
  • Mammals
  • Pharmaceutical Preparations
  • Polymorphism, Single Nucleotide
  • Xenobiotics
  • Journal Article
  • Review


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