Transferases are a particular class of enzymes that transfer a specific functional group from a donor to an acceptor. Transferases are responsible for catalyzing thousands of reactions in the body, making numerous processes possible.
The role of transferases spans a wide variety of domains.
Single carbon transferases are involved in the transfer for single-carbon groups from donor to acceptor. They’re found in a variety of contexts, including the transfer of amido, carbamoyl, methyl, and hydroxymethyl reactions.
Aldehyde and ketone transferases are also heavily involved in reactions that include aldehydes and ketones. Transferase enzymes in this category, including transaldolases and transketolases and, are responsible for the transfer of the dihydroxyacetone functional group to G3P.
Acyl transferases transfer acyl groups to acceptors, turning the donor into an alkyl group.
Nitrogenous transferases. This group of enzymes includes examples such as transaminase and some oximinotransferases.
Phosphorous transferases is an enzyme that helps to transfer phosphorous-containing groups from one molecule to another. Phosphate acceptors include phosphate groups, nitrogenous groups, alcohols, and carboxy groups.
Sulfur transferases subdivide into a range of different categories, which include sulfotransferases and alkylthio groups, the most discussed enzyme in this group is alcohol sulfotransferase. People who are low on this enzyme tend to experience higher rates of liver disease.
Metal transferases, these include enzymes capable of transferring tungsten and molybdenum-containing groups.
The first example of a “transferase” enzyme was noted in 1930 by researcher D. M. Needham after observing the formation of a keto acid from an amino acid. Needham had been studying pigeon breast tissue when he noted that a particular amino acid was no longer present after coming into contact with a specific enzyme.
Later it was discovered that the reaction could be reversed. You could take a keto acid and convert it back into an amino acid by adding the correct molecular groups. Later in the 1930s, following several influential papers, it became clear that there were laboratory methods for producing amino acids by transfer.
Later, new types of transferase were found. In 1953, for instance, researchers found that the UDP-glucose pyrophosphorylase enzyme was a transferase. It would reversibly produce G1P and UTP from UDP-glucose.
In the 1960s, researchers continued to make significant transferase discoveries. Nobel prize-winning researcher Julius Axelrod found that the mechanism behind the breakdown of catecholamine was mediated by catechol-O-methyltransferase - another type of transferase that involved the passing of molecular groups from the donor to the acceptor.
There is considerable evidence that deficiencies in certain transferases play a vital role in the emergence of diseases.
Researchers, for instance, believe that sudden infant death syndrome might be the result of insufficient choline acetyltransferase. On post-mortem, infants with SIDS have lower levels of this enzyme in their hypothalamus and striatum. This situation appears to induce the production of fewer neurons in the vagus system, perhaps interrupting the ability of the child to perform life-sustaining autonomic functions.
Decreased production of choline acetyltransferase is also a hallmark of Alzheimer’s disease.