Transfer of an amino group from an amino acid to an alpha keto acid is done by?

Ans:A.)TransaminaseTransaminase (Amino-transferases) transfer an a-amino (NH3+) group from L amino acid to an alpha keto acid.OVERVIEW OF AMINO ACID DEGRADATION* There are several steps involved in the degradation of amino acids.1. The a-amino group must be removed from the amino acid. This can be done either transamination or oxidative deamination .In transamination, enzymes, known as aminotransferases, act to remove the amino group from specific amino acids and transfer them to another molecule.Almost every amino acid has a specific aminotransferase. ALT: Transfers amino group from alanine to a-ketoglutarate, resulting in the formation of glutamate and pyruvate.AST: Transfers amino group from glutamate to oxaloacetate, resulting in the formation of aspaate and a-ketoglutarate. Oxidative deamination acts to remove the amino group from glutamate and release it as ammonia.Stimulators: ADP and GDP activate glutamate dehydrogenase.Inhibitors: ATP and GTP inhibit glutamate dehydrogenase.2. Once the a-amino group is removed from the amino acid, the ammonia moiety must then be transpoed to the liver for metabolism into urea. This transpo occurs with the help of alanine and glutamine..3. Once in the liver, the ammonia moiety is transformed into urea the urea cycle .4. The remaining carbon skeleton are then degraded into intermediates of the citric acid cycle or can be used as building blocks for other molecules .5. The branched-chain amino acids (valine, isoleucine, leucine) require specific enzyme complexes in order to be fully degraded .