Transferase
Enzymes that catalyze the transfer of functional groups between molecules
Transferase is an enzyme that catalyzes the transfer of a chemical group, such as a methyl or a phosphate group, from one molecule to another. These enzymes are responsible for the transfer of functional groups, which are crucial for biological processes such as the metabolism of carbohydrates, lipids and amino acids.
Examples of transferases include:
1. Kinases, which transfer a phosphate group from ATP to a substrate, regulating various cellular processes such as metabolism and cell signaling.
2. Methyltransferases, which transfer a methyl group from S-adenosylmethionine to a substrate, modifying the activity of DNA, RNA, and proteins.
3. Glycosyltransferases, which transfer a sugar unit from an activated sugar donor molecule to an acceptor molecule, for example during the biosynthesis of glycoproteins and glycolipids.
4. Acyltransferases, which transfer an acyl group from a donor molecule to an acceptor molecule, for example during the synthesis of lipids such as phospholipids.
5. Ubiquitin ligases, which transfer ubiquitin from an E2 conjugating enzyme to a substrate protein, marking the protein for degradation by the proteasome.
Overall, transferases play a vital role in the regulation of biological processes by controlling the transfer of functional groups between different molecules.
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