1, with different properties: transamination is a process in which the α-amino group of an α-amino acid is converted into an α-keto acid under the catalysis of transaminase. Deamination is the removal of amino groups from molecules. [1] The human liver decomposes amino acids through deamination.

2. Different functions: transamination is a way of deamination of amino acids. In fact, it can be seen that the amino group of amino acid has been exchanged with the keto group of α -keto acid. Deamination is an enzymatic reaction of deamination of organic compounds in cells and the first step of amino acid metabolism in vivo.

3. Different methods: Many amino acids are deaminated by purine nucleotide cycle in muscle. The reaction is catalyzed by transaminase and its coenzyme pyridoxal phosphate, which is a derivative of vitamin B6. The most important transaminase in human body are alanine transaminase and aspartate transaminase.

Extended data:

Preventive measures for deamination:

1. Most amino acids in the body are deaminated by transamination. Among the 20 α -amino acids involved in protein synthesis, except glycine, lysine, threonine and proline, all of them can participate in transaminase catalysis. The most important amino receptor for transamination is α? Ketoglutaric acid produces glutamic acid as a newly produced amino acid.

2. Further transfer the amino group in glutamic acid to oxaloacetic acid to generate α? Ketoglutaric acid and aspartic acid, or converted into pyruvate. Generate alpha? Ketoglutaric acid and alanine, through the second transamination reaction, regenerate α? oxoglutarate

3. Transamination is reversible, so the equilibrium constant is about 1. The direction of the reaction depends on the relative concentrations of the four reactants. Therefore, transamination is also an important way to synthesize some amino acids (non-essential amino acids) in vivo.

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