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Uridine-cytidine kinase is a key enzyme family in pyrimidine metabolism, phosphorylating uridine and cytidine as the first step of the salvage pathway critical for RNA and DNA synthesis. Two well-characterized human isoforms are UCK1, which is ubiquitously expressed in healthy tissues, and UCK2, which is mainly expressed in placenta and several cancer types, making it a biomarker and therapeutic target in oncology. The enzyme has a well-defined structure with active-site residues conferring specificity for ribonucleosides, and magnesium ions acting as cofactors. UCK2 is frequently overexpressed in tumors and plays a role in the bioactivation of nucleoside analog drugs, with potential implications for cancer treatment. Inhibition or modulation of UCK activity affects cell proliferation, apoptosis, and potentially immune responses
Prodrug activation: UCK2 phosphorylates nucleoside analog drugs to their cytotoxic monophosphate forms in tumor cells Enzyme inhibition: Drugs inhibiting UCK2 block pyrimidine salvage, impairing nucleotide synthesis and tumor growth
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