Xanthine oxidase catalyzes the oxidation of retinol |
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Authors: | Taibi Gennaro Nicotra Concetta M A |
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Institution: | Dipartimento di Oncologia Sperimentale e Applicazioni Cliniche, Università di Palermo, Via del Vespro 129, 90127 Palermo, Italy. gtaibi@unipa.it |
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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. |
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