Mammalian aldehyde oxidases: genetics, evolution and biochemistry

被引:138
作者
Garattini, E. [1 ]
Fratelli, M. [1 ]
Terao, M. [1 ]
机构
[1] Ist Ric Farmacol Mario Negri, Mol Biol Lab, I-20156 Milan, Italy
关键词
aldehyde oxidase; molybdo-flavoenzyme; AOX1; AOH1; AOH2; AOH3; drug metabolism; pseudogene;
D O I
10.1007/s00018-007-7398-y
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Mammalian aldehyde oxidases are a small group of proteins belonging to the larger family of molybdo-flavoenzymes along with xanthine oxidoreductase and other bacterial enzymes. The two general types of reactions catalyzed by aldehyde oxidases are the hydroxylation of heterocycles and the oxidation of aldehydes into the corresponding carboxylic acids. Different animal species are characterized by a different complement of aldehyde oxidase genes. Humans contain a single active gene, while marsupials and rodents are characterized by four such genes clustering at a short distance on the same chromosome. At present, little is known about the physiological relevance of aldehyde oxidases in humans and other mammals, although these enzymes are known to play a role in the metabolism of drugs and compounds of toxicological importance in the liver. The present article provides an overview of the current knowledge of genetics, evolution, structure, enzymology, tissue distribution and regulation of mammalian aldehyde oxidases.
引用
收藏
页码:1019 / 1048
页数:30
相关论文
共 160 条
[11]   ABA3 is a molybdenum cofactor sulfurase required for activation of aldehyde oxidase and xanthine dehydrogenase in Arabidopsis thaliana [J].
Bittner, F ;
Oreb, M ;
Mendel, RR .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2001, 276 (44) :40381-40384
[12]  
Bittner F, 2010, PLANT CELL MONOGR, V17, P119, DOI 10.1007/978-3-642-10613-2_6
[13]   EFFECTS OF CINNAMON ON XANTHINE DEHYDROGENASE, ALDEHYDE OXIDASE, AND PYRIDOXAL OXIDASE ACTIVITY DURING DEVELOPMENT IN DROSOPHILA-MELANOGASTER [J].
BROWDER, LW ;
WILLIAMSON, JH .
DEVELOPMENTAL BIOLOGY, 1976, 53 (02) :241-249
[14]   Analysis of the electron paramagnetic resonance properties of the [2Fe-2S]1+ centers in molybdenum enzymes of the xanthine oxidase family:: Assignment of signals I and II [J].
Caldeira, J ;
Belle, V ;
Asso, M ;
Guigliarelli, B ;
Moura, I ;
Moura, JJG ;
Bertrand, P .
BIOCHEMISTRY, 2000, 39 (10) :2700-2707
[15]  
Calzi ML, 1995, J BIOL CHEM, V270, P31037, DOI 10.1074/jbc.270.52.31037
[16]   Kinetics and interactions of molybdenum and iron-sulfur centers in bacterial enzymes of the xanthine oxidase family:: Mechanistic implications [J].
Canne, C ;
Lowe, DJ ;
Fetzner, S ;
Adams, B ;
Smith, AT ;
Kappl, R ;
Bray, RC ;
Hüttermann, J .
BIOCHEMISTRY, 1999, 38 (42) :14077-14087
[17]  
Chladek J, 1997, PHYSIOL RES, V46, P371
[18]  
CLARKE SE, 1995, DRUG METAB DISPOS, V23, P251
[19]   TISSUE-SPECIFIC AND SUBSTRATE-SPECIFIC DETECTION OF ALDEHYDE AND PYRIDOXAL OXIDASE IN LARVAL AND IMAGINAL TISSUES OF DROSOPHILA-MELANOGASTER [J].
CYPHER, JJ ;
TEDESCO, JL ;
COURTRIGHT, JB ;
KUMARAN, AK .
BIOCHEMICAL GENETICS, 1982, 20 (3-4) :315-332
[20]   INVITRO PIGMENT FORMATION FROM TRYPTAMINE - ROLE OF INDOLE-3-ACETALDEHYDE [J].
DAS, PK ;
GUHA, SR .
BIOCHEMICAL PHARMACOLOGY, 1985, 34 (15) :2663-2667