Guinea pig liver aldehyde oxidase as a sulfoxide reductase: Its purification and characterization

Yoshihara, Shu; Tatsumi, Kiyoshi

doi:10.1016/0003-9861(85)90495-3

Cited by 56 publications

(28 citation statements)

References 43 publications

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“…This suggests that the catalytically active forms of mouse AOH1 and AO have a similar multimeric structure, which is compatible with that of a tetramer consisting of four identical subunits of approximately 150 kDa each. At present, we do not know why, under our experimental conditions, mouse AO behaves as a homotetramer rather than a homodimer, like AOs of other origin (18,19).…”

Section: Molecular Cloning Of the Aoh1 And Aoh2 Cdnas-screening Of Thmentioning

confidence: 71%

“…In their active conformation, AO and XOR proteins are believed to be homodimers with an approximate molecular mass of 300 kDa (18,19). Thus, we deemed it of interest to investigate the structure of the catalytically active form of AOH1.…”

Section: Molecular Cloning Of the Aoh1 And Aoh2 Cdnas-screening Of Thmentioning

confidence: 99%

“…XOR and AO have a striking number of similarities. They act on a partially overlapping set of substrates, which include N-heterocyclic compounds (17), have a high level of amino acid identity (1), as well as similar molecular weights and secondary/tertiary structure (18,19). In addition, the corresponding genes have a common origin, as recently indicated by the high degree of conservation of the exon/intron junctions (20 -22).…”

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confidence: 99%

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Cloning of the cDNAs Coding for Two Novel Molybdo-flavoproteins Showing High Similarity with Aldehyde Oxidase and Xanthine Oxidoreductase

Terao

Kurosaki

Saltini

et al. 2000

Journal of Biological Chemistry

113

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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.

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Section: Molecular Cloning Of the Aoh1 And Aoh2 Cdnas-screening Of Thmentioning

confidence: 71%

Section: Molecular Cloning Of the Aoh1 And Aoh2 Cdnas-screening Of Thmentioning

confidence: 99%

mentioning

confidence: 99%

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Cloning of the cDNAs Coding for Two Novel Molybdo-flavoproteins Showing High Similarity with Aldehyde Oxidase and Xanthine Oxidoreductase

Terao

Kurosaki

Saltini

et al. 2000

Journal of Biological Chemistry

113

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“…The first possibility is that IAAld oxidase itself has a catalytic activity to form IAA from Trp, and APX c'r some other factor(s) promotes the activity. Animal aldehyde oxidase, which contains two FAD, two Mo, eight Fe, and two coenzyme Qlo as prosthetic groups, has broad substrate specificity (Rajagopalan and Handler, 1966;Felsted et al, 1973;Yoshihara and Tatsumi, 1985). The enzyme also has various catalytic activities other than oxidation of aldehydes, such as oxidation of nitrogen-containing heterocyclic compounds (Hall and Krenitsky, 1986), reduction of diphenyl sulfoxide (Yoshihara and Tatsumi, 1986), nitroreduction of aromatic heterocyclic compounds (Bauer and Howard, 1991), and oxime-metabolizing activity (Tatsumi and Ishigai, 1987).…”

Section: Discussionmentioning

confidence: 99%

An in Vitro System of Indole-3-Acetic Acid Formation from Tryptophan in Maize (Zea mays) Coleoptile Extracts

Koshiba

Matsuyama

1993

Plant Physiol.

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“…The amino acid sequences of guinea pig AO have not been reported and the existence of 130 kDa minor subunit has been controversial. 9,31) Thus, it seemed likely that the existence or absence of the 130 kDa minor subunit correlates to the amino acid sequences of 188Lue and 189Pro as seen in human, monkey, rat, mouse, and possibly bovine. However, some factors other than the amino acid sequences might be required for the formation of the 130 kDa subunit in rabbit.…”

Section: Activity Of Monkey Ao Containing 130 Kda Subunitmentioning

confidence: 99%

Properties of 130 kDa Subunit of Monkey Aldehyde Oxidase

Asakawa

Itoh

Adachi

et al. 2008

Biological & Pharmaceutical Bulletin

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Aldehyde oxidase (AO, EC 1.2.3.1) is a major member of the molybdenum hydroxylase family along with xanthine oxidase. Both enzymes consist of a homodimer with a subunit molecular mass of about 150 kDa. Each subunit contains a molybdopterin cofactor, a flavin-adenine dinucleotide (FAD), and two different 2Fe-2S redox centers that are essential for catalytic activity. AO catalyzes the oxidation of a wide range of endogenous and exogenous aldehydes and N-heterocyclic aromatic compounds. Representative N-heterocyclic-containing drugs that serve as substrates for AO are famciclovir, methotrexate, 6-mercaptopurine, and cinchona alkaloids. [1][2][3][4][5][6] The oxidation mode by cytosolic AO is a nucleophilic attack at an electron-deficient carbon, which is different from an electrophilic attack at an electron-rich carbon by microsomal cytochrome P450, indicating that AO has complementary substrate specificities with P450 in the metabolism of xenobiotics. In addition, AO can catalyze in vitro reduction of a variety of functional groups including sulfoxides, N-oxides, azo dyes, and N-hydroxycarbamoyl substituents in the presence of an appropriate electron donor. 6) In fact, the atypical antipsychotic drug, ziprasidone, is mostly metabolized to its reductive ring-cleaved S-methyldihydroziprasidone by AO in human. 7,8) One of characteristics of AO is a marked species difference. For example, Sugihara et al. 9) investigated the enzyme activity in several animal species using a few model substrates with relatively simple chemical structures. Extremely high benzaldehyde oxidase activity was observed in monkey and low activity in guinea pig. 2-Hydroxypyrimidine was oxidized at the highest rate in rabbit and rat and at a low rate in mouse. Monkey showed the highest phthalazine oxidase activity among the animal species studied. N 1 -methylnicotinamide oxidase activity was highest in rabbit and low in rat and mouse. Preliminary experiments demonstrated that human AO shows similar substrate specificity to that of monkey. Further, many medicines have been reported to show significant species differences in AO-catalyzed metabolism. They include an ocular hypotensive agent, brimonidine, 10) an antiviral drug, famciclovir and 6-deoxypenciclovir, 11) an antineoplastic drug, methotrexate, 12,13) an ultra-short acting hypnotic, zaleplon, 14) and an oral antitumor agent, zebularine. 15)Thus, it is now well established that the variations of AO activity may be dependent on not only animal species, but also on the chemical structures of the substrate. Roughly speaking, AO activity is high in monkey and human, moderate to low in rat and mouse, and deficient in dog. We have been studying the metabolism of RS-8359, [(Ϯ)-4-(4-cyanoanilino)-5,6-dihydro-7-hydroxy-7H-cyclopenta-[d]-pyrimidine], which is a reversible and selective monoamine oxidase A (MAO-A) inhibitor 16,17) and has been developed as an anti-depressant. 18,19) The main metabolic pathway of the compound is the AO-catalyzed 2-oxidation on the pyrimidine ring of the molecule. Simi...

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Guinea pig liver aldehyde oxidase as a sulfoxide reductase: Its purification and characterization

Cited by 56 publications

References 43 publications

Cloning of the cDNAs Coding for Two Novel Molybdo-flavoproteins Showing High Similarity with Aldehyde Oxidase and Xanthine Oxidoreductase

Cloning of the cDNAs Coding for Two Novel Molybdo-flavoproteins Showing High Similarity with Aldehyde Oxidase and Xanthine Oxidoreductase

An in Vitro System of Indole-3-Acetic Acid Formation from Tryptophan in Maize (Zea mays) Coleoptile Extracts

Properties of 130 kDa Subunit of Monkey Aldehyde Oxidase

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