Abstract
The group of enzymes collectively and descriptively known as the molybdenum iron-sulphur flavin hydroxylases includes aldehyde oxidase, xanthine oxidase, and xanthine dehydrogenase. As a group and as individuals, they are among the most unique of proteins. The promiscuity of these enzymes is reflected in their behavior with respect to substrates. Distinctions between aldehyde and xanthine oxidases and between xanthine oxidase and dehydrogenase have not always been made. Aldehyde oxidase, xanthine oxidase, and xanthine dehydrogenase catalyze, though at widely different rates, the hydroxylation of a wide variety of purines, pteridines, pyrimidines, other heterocyclic nitrogenous compounds, and aldehydes, whether aliphatic, aromatic, or heteroaromatic. These enzymes differ not only in substrate specificity but also with respect to the position on the substrate that is hydroxylated. This is most evident with substrates, such as purines and pteridines, having more than one site available for hydroxylation.
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