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Transferase
Class of enzymes which transfer functional groups between molecules / From Wikipedia, the free encyclopedia
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.
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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:
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.