One-carbon group transferase enzyme

One-carbon group transferase enzymes" refer to a broad class of enzymes that catalyze the transfer of one-carbon units (such as methyl, formyl, or hydroxymethyl groups) between molecules, a process essential for many cellular metabolic pathways. These enzymes, collectively classified under EC 2.1 (e.g., methyltransferases, formyltransferases, hydroxymethyltransferases), play central roles in folate metabolism, methionine cycle, nucleotide biosynthesis, amino acid metabolism, and methylation of DNA, RNA, and proteins[1][3][5][6][8]. Their activity maintains cellular proliferation, epigenetic regulation, and metabolic homeostasis. Malfunction or dysregulation is implicated in cancer, cardiovascular, neurodegenerative, and inflammatory diseases[2][4][5][7]. Several enzymes within this group (e.g., dihydrofolate reductase, thymidylate synthase, serine hydroxymethyltransferase, MTHFR) are established therapeutic targets, particularly in oncology, and are targeted by antifolate and related drugs[5][7]. Clinical monitoring may include homocysteine, SAM/SAH ratios, or specific enzyme expression as biomarkers. Inhibitors can cause typical antimetabolite toxicities (myelosuppression, mucositis). Overall, "one-carbon group transferase enzyme" is not the canonical name of a specific protein but describes a family of enzymes united by their core catalytic activity[6][8].

Other names

One-carbon transferaseSingle-carbon transferaseEC 2.1 enzymesMethyltransferase (category)Formyltransferase (category)Hydroxymethyltransferase (category)

Inhibition of folate-dependent one-carbon transferases blocks nucleotide and amino acid synthesis, leading to cytotoxicity in rapidly dividing cells (e.g., cancer chemotherapy)[5][7]. Inhibition of methyltransferase activity decreases methylation of DNA/RNA/proteins, altering gene expression[5][7].