Aminotransferase-catalyzed transamination occurs in two steps. In the first step, the α-amino group of an amino acid is transferred to the enzyme, yielding the corresponding α-keto acid and aminated enzyme.
The first step in amino acid cleavage is the removal of the α-amino group. Key steps in amino acid degradation include deamination catalyzed by pyridoxal phosphate-dependent transaminases, oxidoreductases or carbon-oxygen lyases, decarboxylase reactions, and rearrangements of the carbon backbone catalyzed by isomerases. increase.
In general, the first step in amino acid degradation is the removal of the amino group, usually by a reaction known as transamination. The carbon backbone of amino acids reacts further to form compounds that can be used to synthesize glucose or ketone bodies.
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