Xanthine dehydrogenase
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Xanthine dehydrogenase, also known as XDH, is a protein that, in humans, is encoded by the XDH gene.[1][2]
Function
Xanthine dehydrogenase belongs to the group of molybdenum-containing hydroxylases involved in the oxidative metabolism of purines. The enzyme is a homodimer. Xanthine dehydrogenase can be converted to xanthine oxidase by reversible sulfhydryl oxidation or by irreversible proteolytic modification.[1]
Xanthine dehydrogenase catalyzes the following chemical reaction:
The three substrates of this enzyme are xanthine, NAD+, and H2O, whereas its three products are urate, NADH, and H+.
This enzyme participates in purine metabolism.
Nomenclature
This enzyme belongs to the family of oxidoreductases, to be specific, those acting on CH or CH2 groups with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is xanthine:NAD+ oxidoreductase. Other names in common use include NAD+-xanthine dehydrogenase, xanthine-NAD+ oxidoreductase, xanthine/NAD+ oxidoreductase, and xanthine oxidoreductase.
Clinical significance
Defects in xanthine dehydrogenase cause xanthinuria, may contribute to adult respiratory stress syndrome, and may potentiate influenza infection through an oxygen metabolite-dependent mechanism.[1] It has been shown that patients with lung adenocarcinoma tumors which have high levels of XDH gene expression have lower survivals.[3][4] Addiction to XDH protein has been used to target NSCLC tumors and cell lines in a precision oncology manner.[4]
See also
References
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Further reading
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External links
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