Xanthine Oxidase Catalyzes the Oxidation of Retinol

Taibi G; Nicotra Cma

    Risultato della ricerca: Article

    10 Citazioni (Scopus)

    Abstract

    In mammals, xanthine oxidase (E.C. 1.17.3.2) catalyzes the hydroxylation of a wide variety of heterocyclic substrates such as purines, pyrimidines, and pterins, in addition to aldehydes [1] as all-trans-retinaldehyde [2–5]. Here, we show that buttermilk xanthine oxidase was capable to oxidizing all-trans-retinol (t-ROL) to all-trans-retinaldehyde (t-RAL) that was successively oxidized to all-trans-retinoic acid (t-RA). A rise in the enzyme activity, when t-ROL-CRBP complex was assayed, with respect to the free t-ROL, was observed. Furthermore, treatment of the enzyme with Na2S and glutathione resulted in a significant increment in catalytic activity toward t-ROL and t-RAL, due to the reconstitution of the native structural organization of the molybdenum centre of molybdopterin cofactor of the desulfo form of xanthine oxidase.
    Lingua originaleEnglish
    pagine (da-a)471-476
    RivistaJournal of Enzyme Inhibition and Medicinal Chemistry
    Volume22 (4)
    Stato di pubblicazionePublished - 2007

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    Xanthine Oxidase
    Retinaldehyde
    Vitamin A
    Pterins
    Pyrimidines
    Enzymes
    Hydroxylation
    Tretinoin
    Aldehydes
    Glutathione
    Mammals
    Oxidoreductases

    All Science Journal Classification (ASJC) codes

    • Drug Discovery
    • Biochemistry
    • Biochemistry, Genetics and Molecular Biology(all)
    • Organic Chemistry

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    Xanthine Oxidase Catalyzes the Oxidation of Retinol. / Taibi G; Nicotra Cma.

    In: Journal of Enzyme Inhibition and Medicinal Chemistry, Vol. 22 (4), 2007, pag. 471-476.

    Risultato della ricerca: Article

    @article{ed8552fc722a416ca2f1b0a3cdfa7685,
    title = "Xanthine Oxidase Catalyzes the Oxidation of Retinol",
    abstract = "In mammals, xanthine oxidase (E.C. 1.17.3.2) catalyzes the hydroxylation of a wide variety of heterocyclic substrates such as purines, pyrimidines, and pterins, in addition to aldehydes [1] as all-trans-retinaldehyde [2–5]. Here, we show that buttermilk xanthine oxidase was capable to oxidizing all-trans-retinol (t-ROL) to all-trans-retinaldehyde (t-RAL) that was successively oxidized to all-trans-retinoic acid (t-RA). A rise in the enzyme activity, when t-ROL-CRBP complex was assayed, with respect to the free t-ROL, was observed. Furthermore, treatment of the enzyme with Na2S and glutathione resulted in a significant increment in catalytic activity toward t-ROL and t-RAL, due to the reconstitution of the native structural organization of the molybdenum centre of molybdopterin cofactor of the desulfo form of xanthine oxidase.",
    keywords = "Xanthine oxidase, retinol oxidation, retinaldehyde oxidation, retinoic acid biosynthesis, cellular retinoid binding protein (CRBP), Cellular retinoic acid binding protein (CRABP), retinol binding protein (RBP)",
    author = "{Taibi G; Nicotra Cma} and Concetta Nicotra and Gennaro Taibi",
    year = "2007",
    language = "English",
    volume = "22 (4)",
    pages = "471--476",
    journal = "Journal of Enzyme Inhibition and Medicinal Chemistry",
    issn = "1475-6366",
    publisher = "Informa Healthcare",

    }

    TY - JOUR

    T1 - Xanthine Oxidase Catalyzes the Oxidation of Retinol

    AU - Taibi G; Nicotra Cma

    AU - Nicotra, Concetta

    AU - Taibi, Gennaro

    PY - 2007

    Y1 - 2007

    N2 - In mammals, xanthine oxidase (E.C. 1.17.3.2) catalyzes the hydroxylation of a wide variety of heterocyclic substrates such as purines, pyrimidines, and pterins, in addition to aldehydes [1] as all-trans-retinaldehyde [2–5]. Here, we show that buttermilk xanthine oxidase was capable to oxidizing all-trans-retinol (t-ROL) to all-trans-retinaldehyde (t-RAL) that was successively oxidized to all-trans-retinoic acid (t-RA). A rise in the enzyme activity, when t-ROL-CRBP complex was assayed, with respect to the free t-ROL, was observed. Furthermore, treatment of the enzyme with Na2S and glutathione resulted in a significant increment in catalytic activity toward t-ROL and t-RAL, due to the reconstitution of the native structural organization of the molybdenum centre of molybdopterin cofactor of the desulfo form of xanthine oxidase.

    AB - In mammals, xanthine oxidase (E.C. 1.17.3.2) catalyzes the hydroxylation of a wide variety of heterocyclic substrates such as purines, pyrimidines, and pterins, in addition to aldehydes [1] as all-trans-retinaldehyde [2–5]. Here, we show that buttermilk xanthine oxidase was capable to oxidizing all-trans-retinol (t-ROL) to all-trans-retinaldehyde (t-RAL) that was successively oxidized to all-trans-retinoic acid (t-RA). A rise in the enzyme activity, when t-ROL-CRBP complex was assayed, with respect to the free t-ROL, was observed. Furthermore, treatment of the enzyme with Na2S and glutathione resulted in a significant increment in catalytic activity toward t-ROL and t-RAL, due to the reconstitution of the native structural organization of the molybdenum centre of molybdopterin cofactor of the desulfo form of xanthine oxidase.

    KW - Xanthine oxidase, retinol oxidation, retinaldehyde oxidation, retinoic acid biosynthesis, cellular retinoid binding protein (CRBP), Cellular retinoic acid binding protein (CRABP), retinol binding protein (RBP)

    UR - http://hdl.handle.net/10447/27353

    M3 - Article

    VL - 22 (4)

    SP - 471

    EP - 476

    JO - Journal of Enzyme Inhibition and Medicinal Chemistry

    JF - Journal of Enzyme Inhibition and Medicinal Chemistry

    SN - 1475-6366

    ER -