TY  - JOUR
A1  - Romao, Maria Joao
A1  - Coelho, Catarina
A1  - Santos-Silva, Teresa
A1  - Foti, Alessandro
A1  - Terao, Mineko
A1  - Garattini, Enrico
A1  - Leimkühler, Silke
T1  - Structural basis for the role of mammalian aldehyde oxidases in the metabolism of drugs and xenobiotics
T2  - Current Opinion in Chemical Biology
N2  - 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.
Y1  - 2017
UR  - https://publishup.uni-potsdam.de/frontdoor/index/index/docId/55142
SN  - 1367-5931
SN  - 1879-0402
VL  - 37
SP  - 39
EP  - 47
PB  - Elsevier
CY  - Oxford
ER  -