@article {Rom{\~a}o201739,
	title = {Structural basis for the role of mammalian aldehyde oxidases in the metabolism of drugs and xenobiotics},
	journal = {Current Opinion in Chemical Biology},
	volume = {37},
	year = {2017},
	note = {<p>Biocatalysis \&amp; biotransformation * Bioinorganic Chemistry</p>
},
	pages = {39 - 47},
	abstract = {<p>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.</p>
},
	issn = {1367-5931},
	doi = {https://doi.org/10.1016/j.cbpa.2017.01.005},
	url = {http://www.sciencedirect.com/science/article/pii/S1367593117300066},
	author = {Rom{\~a}o, Maria Jo{\~a}o and Coelho, Catarina and Santos-Silva, Teresa and Foti, Alessandro and Terao, Mineko and Garattini, Enrico and Leimk{\"u}hler, Silke}
}
