title: Cloning of the cDNAs coding for two novel molybdo-flavoproteins showing high similarity with aldehyde oxidase and xanthine oxidoreductase.
abstract: The cDNAs coding for two novel mouse molybdo-flavoproteins, AOH1 and AOH2 (aldehyde oxidase homolog 1 and 2), were isolated. The AOH1 and AOH2 cDNAs code for polypeptides of 1336 amino acids. The two proteins have similar primary structure and show striking amino acid identity with aldehyde oxidase and xanthine oxidoreductase, two other molybdo-flavoenzymes. AOH1 and AOH2 contain consensus sequences for a molybdopterin-binding site and two distinct 2Fe-2S redox centers. In its native conformation, AOH1 has a molecular weight consistent with a homotetrameric structure. Transfection of the AOH1 and AOH2 cDNAs results in the production of proteins with phenanthridine but not hypoxanthine oxidizing activity. Furthermore, the AOH1 protein has benzaldehyde oxidizing activity with electrophoretic characteristics identical to those of a previously identified aldehyde oxidase isoenzyme (Holmes, R. S. (1979) Biochem. Genet. 17, 517-528). The AOH1 transcript is expressed in the hepatocytes of the adult and fetal liver and in spermatogonia. In liver, the AOH1 protein is synthesized in a gender-specific fashion. The expression of AOH2 is limited to keratinized epithelia and the basal layer of the epidermis and hair folliculi. The selective cell and tissue distribution of AOH1 and AOH2 mRNAs is consistent with the localization of the respective protein products.
authors.affiliation: Laboratory of Molecular Biology, Centro Catullo e Daniela Borgomainerio, Istituto di Ricerche Farmacologiche "Mario Negri," via Eritrea, 62, 20157 Milano, Italy.
authors.forename: M
authors.initials: M
authors.lastname: Terao
authors.forename: M
authors.initials: M
authors.lastname: Kurosaki
authors.forename: G
authors.initials: G
authors.lastname: Saltini
authors.forename: S
authors.initials: S
authors.lastname: Demontis
authors.forename: M
authors.initials: M
authors.lastname: Marini
authors.forename: M
authors.initials: M
authors.lastname: Salmona
authors.forename: E
authors.initials: E
authors.lastname: Garattini
mesh_terms: D042931:Aldehyde Oxidase; D000445:Aldehyde Oxidoreductases / Q000235:genetics; D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D001665:Binding Sites; D003001:Cloning, Molecular; D003067:Coenzymes; D016384:Consensus Sequence; D018076:DNA, Complementary; D003901:Desulfovibrio / Q000201:enzymology; D019143:Evolution, Molecular; D005260:Female; D006801:Humans; D008297:Male; D008667:Metalloproteins / Q000378:metabolism; D051379:Mice; D024101:Mitochondrial Proteins; D008969:Molecular Sequence Data; D008982:Molybdenum; D000090006:Molybdenum Cofactors; D010088:Oxidoreductases / Q000235:genetics* / Q000378:metabolism; D010802:Phylogeny; D010940:Plant Proteins / Q000235:genetics; D011621:Pteridines / Q000378:metabolism; D011994:Recombinant Proteins / Q000096:biosynthesis; D017386:Sequence Homology, Amino Acid; D012727:Sex Characteristics; D014018:Tissue Distribution; D014969:Xanthine Oxidase / Q000235:genetics; D000099188:Alternative Oxidase
chemical_list: D042931:Aldehyde Oxidase; D000445:Aldehyde Oxidoreductases; D003067:Coenzymes; D018076:DNA, Complementary; D008667:Metalloproteins; D024101:Mitochondrial Proteins; D008982:Molybdenum; D000090006:Molybdenum Cofactors; D010088:Oxidoreductases; D010940:Plant Proteins; D011621:Pteridines; D011994:Recombinant Proteins; D014969:Xanthine Oxidase; D000099188:Alternative Oxidase; C022261:molybdopterin