6533b7d4fe1ef96bd12627e2
RESEARCH PRODUCT
Xanthine oxidase catalyzes the oxidation of retinol.
Concetta M.a. NicotraGennaro Taibisubject
Xanthine OxidaseReceptors Retinoic Acidchemistry.chemical_elementTretinoinHydroxylationLigandsCatalysisHydroxylationchemistry.chemical_compoundRetinoidsDrug DiscoveryHumansXanthine oxidasePurine metabolismVitamin APharmacologychemistry.chemical_classificationHypoxanthinebiologyEthanolRetinol-Binding Proteins CellularGeneral MedicineGlutathioneEnzyme assayOxygenRetinol-Binding ProteinsKineticsEnzymechemistryBiochemistryXanthine dehydrogenaseMolybdenumbiology.proteinXanthine oxidase retinol oxidation retinaldehyde oxidation retinoic acid biosynthesis cellular retinoid binding protein (CRBP) Cellular retinoic acid binding protein (CRABP) retinol binding protein (RBP)description
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.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2007-09-13 | Journal of enzyme inhibition and medicinal chemistry |