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  1. Most amino acids are deaminated by transamination reaction catalysed by aminotransferases or transaminases. The -amino group present in an amino acid is transferred to an -keto acid to

  2. Amine groups can be transferred or removed through transamination or deamination, respectively. Transamination. Transamination is the transfer of an amine group from an amino acid to a keto acid (amino acid without an amine group), thus creating a new amino acid and keto acid as shown below.

  3. 10.2: Amino Acids Degradation Generally the first step in the breakdown of amino acids is the removal of the amino group, usually through a reaction known as transamination. The carbon skeletons of the amino acids undergo further reactions to form compounds that can either be used for the synthesis of glucose or the synthesis of ketone bodies.

  4. Amino acids are degraded to yield NH 4+, which enters the urea cycle, and a carbon skeleton that can enter metabolic pathways to generate ATP, glucose, and fatty acids. Amino acids are also used to produce NO, neurotransmitters, and catecholamines.

  5. In their conversion to metabolic intermediates, the amino acids first undergo deamination. The primary goal of deamination is to excrete excess nitrogen (as urea) and then use or convert (to glucose) the remaining carbon skeleton.

  6. Deamination is usually accomplished by a transamination reaction in which the –NH 2 group of the amino acid is exchanged with the keto group of α-ketoglutarate, forming a new α-keto acid plus glutamate.

  7. Transamination, Deamination & Ammonia Removal as Urea. The first step in catabolizing, or breaking down, an amino acid is the removal of its amine group (-\(\ce{NH3}\)). Amine groups can be transferred or removed through transamination or deamination, respectively.