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Amino acid + FAD + H2O ----- -Keto acid + NH 3 + FADH2 Non-oxidative deamination Amino acids such as serine and histidine are deaminated non-oxidatively The other reactions involved in the catabolism of amino acids are decarboxylation, transulfuration, desulfuration, dehydration etc. Decarboxylation
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. Keto acids and/or carbon skeletons are what remains after amino acids have had their nitrogen group removed by deamination or transamination.
Figure 1. An overview of amino acid metabolism. 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.
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.
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.
30 de dic. de 2018 · Catabolism of amino acids from amino acid pool takes place by deamination and decarboxylation as in Fig. 13.1. Conversion of amino acids into glucose and fatty acids. A cell can utilize fixed number of amino acids from amino acid pool for its functions.
Transamination. 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.
