TY - JOUR
T1 - Evolution, expression, and substrate specificities of aldehyde oxidase enzymes in eukaryotes
AU - Terao, Mineko
AU - Garattini, Enrico
AU - Romão, Maria João
AU - Leimkühler, Silke
N1 - This work was supported by Deutsche Forschungsgemeinschaft Grant Le1171/8-3 (to S. L.).
FCT-MCTES, research unit UCIBIO (UID/Multi/04378/2019).
project PTDC/BBB-BEP/1185/2014 (to M. J. R.).
Fondazione Italo Monzino and the Associazione per la Ricerca sul Cancro (AIRC) (to E. G.).
PY - 2020/4/17
Y1 - 2020/4/17
N2 - Aldehyde oxidases (AOXs) are a small group of enzymes belonging to the larger family of molybdo-flavoenzymes, along with the well-characterized xanthine oxidoreductase. The two major types of reactions that are catalyzed by AOXs are the hydroxylation of heterocycles and the oxidation of aldehydes to their corresponding carboxylic acids. Different animal species have different complements of AOX genes. The two extremes are represented in humans and rodents; whereas the human genome contains a single active gene (AOX1), those of rodents, such as mice, are endowed with four genes (Aox1-4), clustering on the same chromosome, each encoding a functionally distinct AOX enzyme. It still remains enigmatic why some species have numerous AOX enzymes, whereas others harbor only one functional enzyme. At present, little is known about the physiological relevance of AOX enzymes in humans and their additional forms in other mammals. These enzymes are expressed in the liver and play an important role in the metabolisms of drugs and other xenobiotics. In this review, we discuss the expression, tissue-specific roles, and substrate specificities of the different mammalian AOX enzymes and highlight insights into their physiological roles.
AB - Aldehyde oxidases (AOXs) are a small group of enzymes belonging to the larger family of molybdo-flavoenzymes, along with the well-characterized xanthine oxidoreductase. The two major types of reactions that are catalyzed by AOXs are the hydroxylation of heterocycles and the oxidation of aldehydes to their corresponding carboxylic acids. Different animal species have different complements of AOX genes. The two extremes are represented in humans and rodents; whereas the human genome contains a single active gene (AOX1), those of rodents, such as mice, are endowed with four genes (Aox1-4), clustering on the same chromosome, each encoding a functionally distinct AOX enzyme. It still remains enigmatic why some species have numerous AOX enzymes, whereas others harbor only one functional enzyme. At present, little is known about the physiological relevance of AOX enzymes in humans and their additional forms in other mammals. These enzymes are expressed in the liver and play an important role in the metabolisms of drugs and other xenobiotics. In this review, we discuss the expression, tissue-specific roles, and substrate specificities of the different mammalian AOX enzymes and highlight insights into their physiological roles.
UR - http://www.scopus.com/inward/record.url?scp=85083521832&partnerID=8YFLogxK
U2 - 10.1074/jbc.REV119.007741
DO - 10.1074/jbc.REV119.007741
M3 - Review article
C2 - 32144208
AN - SCOPUS:85083521832
VL - 295
SP - 5377
EP - 5389
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 16
ER -