Transferase

In biochemistry, a transferase is any one of a class of enzymes that catalyse the transfer of specific functional groups (e.g. a methyl or glycosyl group) from one molecule (called the donor) to another (called the acceptor).^[2] They are involved in hundreds of different biochemical pathways throughout biology, and are integral to some of life's most important processes.

Transferases are involved in myriad reactions in the cell. Three examples of these reactions are the activity of coenzyme A (CoA) transferase, which transfers thiol esters,^[3] the action of N-acetyltransferase, which is part of the pathway that metabolizes tryptophan,^[4] and the regulation of pyruvate dehydrogenase (PDH), which converts pyruvate to acetyl CoA.^[5] Transferases are also utilized during translation. In this case, an amino acid chain is the functional group transferred by a peptidyl transferase. The transfer involves the removal of the growing amino acid chain from the tRNA molecule in the A-site of the ribosome and its subsequent addition to the amino acid attached to the tRNA in the P-site.^[6]

Mechanistically, an enzyme that catalyzed the following reaction would be a transferase:

${\displaystyle {\ce {X-R + Y}}\quad {\xrightarrow[{\text{ transferase }}]{}}\quad {\ce {X + Y-R}}}$

In the above reaction (where the dash represents a bond, not a minus sign), X would be the donor, and Y would be the acceptor.^[7] R denotes the functional group transferred as a result of transferase activity. The donor is often a coenzyme.