formyltransferase

Formyltransferases are enzymes that catalyze the transfer of a formyl group (-CHO) from a donor molecule to an acceptor substrate. The best-known formyl donors are 10-formyltetrahydrofolate (10-formyl-THF), and many formyltransferases participate in one-carbon metabolism by attaching the formyl moiety to nucleophilic nitrogens or amino groups in their substrates. The reactions help furnish essential building blocks for nucleotide synthesis and protein synthesis, linking formylation steps to folate metabolism and cellular growth.

Prominent examples include glycinamide ribonucleotide transformylase, which transfers a formyl group from 10-formyl-THF to glycinamide ribonucleotide (GAR) to form formylglycinamide ribonucleotide (FGAR) in de novo purine biosynthesis; and methionyl-tRNA formyltransferase, which formylates the initiating methionyl-tRNA (Met-tRNAfMet) to generate formylmethionyl-tRNAfMet, enabling initiation of protein synthesis in bacteria and some organelles.

Distribution and significance: formyltransferases are found in bacteria and in organelles such as mitochondria and plastids that utilize formylated initiator tRNA, and in pathways of folate metabolism that supply the 10-formyl-THF donor. Because many formyltransferases depend on 10-formyl-THF, they intersect with folate metabolism and are potential targets for antimicrobial agents that disrupt nucleotide biosynthesis or translation initiation.