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One-carbon transfer enzymes are a group of enzymes responsible for transferring one-carbon units (e.g., methyl, methylene, formyl groups) between molecules, thereby connecting diverse metabolic pathways crucial for cellular function[1][5][7][8]. They mediate reactions in nucleotide biosynthesis, amino acid metabolism (serine, glycine, methionine), DNA and histone methylation, redox balance, and neurotransmitter synthesis, integrating nutritional, energetic, and epigenetic controls in the cell[2][4][5][7]. Key enzymes include serine hydroxymethyltransferase (SHMT1/2), methionine synthase, thymidylate synthase, dihydrofolate reductase (DHFR), and various methyltransferases, among others[3][6]. Defects in these enzymes or their pathways can lead to cancer, cardiovascular, and neurodevelopmental disorders, and are targeted by drugs such as methotrexate and 5-fluorouracil in cancer therapy, where they block critical steps in DNA synthesis or methyl group transfer[3][6]. Importantly, "one-carbon transfer enzymes" refers to a class—not a single molecular target—spanning multiple enzyme families with closely related but distinct functions. For structured data, individual canonical enzyme names (such as "Thymidylate synthase" or "Serine hydroxymethyltransferase 1") should be specified, because "one-carbon transfer enzyme" is too broad to serve as a unique target[3][5][6]. Note: "One-carbon transfer enzymes" is not a singular molecule, but a functional/molecular class. This makes the target name too broad and ill-defined for precise therapeutic, structural, or drug-target annotation, so is_incorrect: true applies in the context of unique drug target identification[3][5][6].
Inhibition of folate-dependent enzymes (e.g., thymidylate synthase, dihydrofolate reductase); Inhibition of methyltransferases; Inhibition of serine/glycine conversion and their utilization.
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