In mammals, xanthine oxidase (E.C. 18.104.22.168) catalyzes the hydroxylation of a wide variety of heterocyclic substrates such aspurines, pyrimidines, and pterins, in addition to aldehydes  as all-trans-retinaldehyde [2–5]. Here, we show that buttermilkxanthine oxidase was capable to oxidizing all-trans-retinol (t-ROL) to all-trans-retinaldehyde (t-RAL) that was successivelyoxidized to all-trans-retinoic acid (t-RA). A rise in the enzyme activity, when t-ROL-CRBP complex was assayed, with respectto the free t-ROL, was observed. Furthermore, treatment of the enzyme with Na2S and glutathione resulted in a significantincrement in catalytic activity toward t-ROL and t-RAL, due to the reconstitution of the native structural organization of themolybdenum centre of molybdopterin cofactor of the desulfo form of xanthine oxidase.
|Rivista||Journal of Enzyme Inhibition and Medicinal Chemistry|
|Stato di pubblicazione||Published - 2007|
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