formyltransfer

Formyltransferase is an enzyme that catalyzes the transfer of a formyl group from 10-formyltetrahydrofolate (10-formyl-FH4) to a target molecule, typically an amino acid or a small molecule. This process is crucial in various biochemical pathways, including the synthesis of purines and pyrimidines, and the methylation cycle. The enzyme is found in various organisms, including bacteria, archaea, and eukaryotes, and plays a vital role in maintaining the balance of one-carbon units in cells.

The reaction catalyzed by formyltransferase involves the following steps:

1. The enzyme binds to 10-formyl-FH4 and the target molecule.

2. The formyl group is transferred from 10-formyl-FH4 to the target molecule, forming a new compound and tetrahydrofolate (FH4).

3. The enzyme releases the new compound and FH4, ready to catalyze another reaction.

Formyltransferase is a member of the transferase class of enzymes, which catalyze the transfer of functional groups between molecules. The enzyme is typically specific for the formyl group and the target molecule, ensuring that the reaction proceeds efficiently and accurately. The study of formyltransferase and its role in various biochemical pathways continues to be an active area of research, with potential applications in medicine and biotechnology.