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Transferases are an important class of enzymes that play a vital role in various biochemical processes by catalyzing the transfer of functional groups from one molecule to another. These enzymes are ubiquitous in nature and are involved in a wide range of metabolic pathways, including the synthesis and degradation of biomolecules such as carbohydrates, proteins, lipids, and nucleic acids. The importance of transferases extends beyond basic metabolism; they are also critical in industrial applications, medical diagnostics, and pharmaceutical development. Creative Enzymes is pleased to offer a comprehensive selection of transferases, including human SULT1B1, native bovine protein kinase A, modified T7 RNA polymerase, and more than 300 others to meet your specific needs.
Transferases are enzymes that catalyze the transfer of a specific functional group, such as a methyl, glycosyl, acyl, phosphate, or amino group, from a donor molecule to an acceptor molecule. The general reaction catalyzed by transferases can be represented as follows:
Donor-X + Acceptor → Donor + Acceptor-X
In this reaction, "X" represents the functional group to be transferred. The donor molecule, which originally contains the functional group, transfers it to the acceptor molecule, resulting in the formation of a new compound.
Transferases are classified under the EC (Enzyme Commission) number 2, which designates them based on the type of group they transfer. The classification system provides a structured way to categorize these enzymes based on their specificity and the type of functional group involved.
Transferases are classified into several subclasses based on the type of functional group they transfer. Some of the major subclasses include:
Glycosyltransferases catalyze the transfer of glycosyl groups (sugar moieties) from a donor molecule, typically a nucleotide sugar, to an acceptor molecule, often a carbohydrate, protein, or lipid (e.g., peptidoglycan glycosyltransferase, 4-α-glucanotransferase, D-inositol-3-phosphate glycosyltransferase). These enzymes are essential for the biosynthesis of oligosaccharides, polysaccharides, and glycoconjugates. Glycosyltransferases are crucial in the production of glycoproteins and glycolipids, which have applications in drug development, vaccine production, and the food industry.
Kinases are enzymes that transfer phosphate groups from high-energy molecules such as ATP to specific substrates, usually proteins, lipids, or nucleotides (e.g., native Bacillus stearothermophilus pyruvate kinase, native rat calmodulin-dependent protein kinase II, native T4-infected Escherichia coli polynucleotide kinase). This phosphorylation process is critical for the regulation of various cellular processes, including signal transduction, metabolism, and cell division. Kinases are extensively studied in cancer research because dysregulation of kinase activity is often associated with cancer progression. Kinase inhibitors are used as targeted therapies in oncology.
Aminotransferases catalyze the transfer of amino groups from an amino acid to a keto acid, playing a key role in amino acid metabolism and the synthesis of non-essential amino acids (e.g., native human aspartate aminotransferase, UDP-4-amino-4-deoxy-L-arabinose aminotransferase). Aminotransferases are used in diagnostic tests for liver function (e.g., AST and ALT tests) and in the production of amino acids for pharmaceutical and nutritional purposes.
Acyltransferases transfer acyl groups from one molecule to another. These enzymes are involved in lipid metabolism, including the synthesis and remodeling of phospholipids, triglycerides, and cholesteryl esters (e.g., phosphatidylcholine-sterol O-acyltransferase, long-chain-alcohol O-fatty-acyltransferase). Acyltransferases are used in the food industry for the synthesis of structured lipids and in the pharmaceutical industry for the development of lipid-based drug delivery systems.
Methyltransferases transfer methyl groups from a donor molecule, such as S-adenosylmethionine (SAM), to an acceptor molecule, which is often DNA, RNA, proteins, or small molecules. Methylation is a key epigenetic modification that regulates gene expression and protein function. Methyltransferases are important in epigenetic research, where they are being studied for their role in gene regulation and disease. They are also targets for drug development in cancer and neurodegenerative diseases.
Phosphotransferases catalyze the transfer of phosphate groups to various substrates, including sugars, proteins, and nucleotides. This group includes the kinases mentioned above, as well as other enzymes such as nucleotidyltransferases. Phosphotransferases are essential for energy metabolism, signal transduction, and nucleic acid synthesis. They are widely used in the study of metabolic diseases, cancer, and infectious diseases.
Transferases have a wide range of applications in various fields, including research, medicine, agriculture, and industry. Their ability to catalyze specific and efficient biochemical reactions makes them invaluable tools in both natural processes and engineered systems.
Transferases are extensively used in biomedical research to understand cellular processes and disease mechanisms. For example:
Transferases are used in a variety of industrial processes where their catalytic capabilities are harnessed to produce chemicals, biofuels and pharmaceuticals:
Transferases also play a role in environmental applications, including the bioremediation of pollutants and the sustainable production of biofuels:
In agriculture, transferases are used to increase crop yields, improve plant resistance to disease, and develop biofortified crops:
From medical research and diagnostics to industrial biotechnology and environmental sustainability, transferases are at the forefront of innovation, driving progress in diverse fields. Through continuous research, Creative Enzymes provides a wide range of high-quality enzymes for current applications and continues to expand applications to offer new solutions to some of the world's most pressing challenges. For inquiries and questions, please don't hesitate to contact us.
