Methionyl-tRNA formyltransferase

In enzymology, a methionyl-tRNA formyltransferase is an enzyme that catalyzes the chemical reaction


 * 10-formyltetrahydrofolate + L-methionyl-tRNAfMet + H2O $$\rightleftharpoons$$ tetrahydrofolate + N-formylmethionyl-tRNAfMet

The 3 substrates of this enzyme are 10-formyltetrahydrofolate, L-methionyl-tRNAfMet, and H2O, whereas its two products are tetrahydrofolate and N-formylmethionyl-tRNAfMet.

This enzyme belongs to the family of transferases that transfer one-carbon groups, specifically the hydroxymethyl-, formyl- and related transferases. The systematic name of this enzyme class is 10-formyltetrahydrofolate:L-methionyl-tRNA N-formyltransferase. Other names in common use include N10-formyltetrahydrofolic-methionyl-transfer ribonucleic, transformylase, formylmethionyl-transfer ribonucleic synthetase, methionyl ribonucleic formyltransferase, methionyl-tRNA Met formyltransferase, methionyl-tRNA transformylase, methionyl-transfer RNA transformylase, methionyl-transfer ribonucleate methyltransferase, and methionyl-transfer ribonucleic transformylase. This enzyme participates in 3 metabolic pathways: methionine metabolism, one carbon pool by folate, and aminoacyl-trna biosynthesis.

Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and.