Single-carbon transferase

Single-carbon transferases are a class of enzymes responsible for transferring one-carbon groups (e.g., methyl, formyl, methylene) from a donor to an acceptor molecule in various cellular biochemical pathways[7][6]. This category includes key enzymes of one-carbon metabolism, particularly those dependent on the folate or methionine cycles, such as serine hydroxymethyltransferase (SHMT), methylenetetrahydrofolate reductase (MTHFR), dihydrofolate reductase (DHFR), and methionine synthase[1][2][4]. These enzymes are essential for the biosynthesis of nucleotides, amino acids, and methyl donors, and therefore play critical roles in DNA/RNA synthesis, protein production, redox balance, and epigenetic regulation through methylation reactions[1][2][3]. Disruption or dysregulation of single-carbon transferase activity is implicated in diseases such as cancer, cardiovascular, and neurodegenerative disorders, with these enzymes serving as established therapeutic targets—especially in antimetabolite cancer chemotherapy (e.g., antifolate drugs)[1][5]. The term "Single-carbon transfer enzymes" is not a canonical name for a single molecular target; it refers to a biochemical enzyme class, not a unique protein, receptor, or gene. Enzyme Commission (EC) number 2.1 is generally associated with these, particularly the methyltransferases[7]. For structured databases or drug targeting purposes, entries should typically be made for individual enzymes within this class (e.g., DHFR, SHMT), not the class as a whole. If a canonical target is needed, replace with a specific enzyme name such as "Serine hydroxymethyltransferase" or "Dihydrofolate reductase."

Other names

One-carbon transferaseSingle-carbon group transferaseOne-carbon metabolism enzymesFolate-dependent enzymes

Inhibition of folate cycle enzymes (e.g., dihydrofolate reductase inhibition), Blockage of nucleotide synthesis, Blockage of methylation/demethylation reactions