Amino acid degradation deamination

Most of the ammonia generated in amino acid degradation is produced by the oxidative deamination of glutamate. Additional ammonia is produced in several other reactions catalyzed by the following enzymes ... 

In general, amino acid degradation begins with deamination. Most deamination is accomplished by transamination reactions, which are followed by oxidative deaminations that produce ammonia. Although most deaminations are catalyzed by glutamate dehydrogenase, other enzymes also contribute to ammonia formation. Ammonia is prepared for excretion by the enzymes of the urea cycle. Aspartate and CO, also contribute atoms to urea. 

Strecker Degradation (Oxidative Deamination), Mild oxidizing agents such as aqueous sodium hypochlorite or aqueous A-bromosuccinimide, cause decarboxylation and concurrent deamination of amino acids to give aldehydes. 

Ammonification. This process proceeds in steps (1) The breakage of the peptide linkage between amino acids A and B, followed by (2) The deamination of the amino acids and formation of NHJ. The electron carrier (e.g., NAD+, NADP+) involved in such reactions depends on the type of protein undergoing degradation and the species of organism mediating the reaction. These reactions are catalyzed by enzymes. 

During the degradation of most amino acids, the a-amino group is initially removed by transamination or deamination. Various mechanisms are available for this, and these are discussed in greater detail in B. The carbon skeletons that are left over after deamination undergo further degradation in various ways. 

Degradative pathways for most amino acids begin by removal of the a-amino nitrogen. There are two major routes of deamination Transamination and oxidative deamination. 

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