Search results for " retinaldehyde oxidation"

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Xanthine oxidase catalyzes the oxidation of retinol.

2007

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 recons…

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)Journal of enzyme inhibition and medicinal chemistry
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