The Transamination Reaction in Amino Acid Synthesis is Catalyzed by an Aminotransferase
In amino acid synthesis, the transamination reaction is catalyzed by an enzyme called an aminotransferase. This reversible biochemical reaction transfers an amino group from one amino acid to another. As a result, a new b-amino acid is formed. It is a biologically and chemically important process that is important in metabolism.
All amino acids participate in this reaction. However, some nonessential amino acids are made through processes other than transamination. Transamination is the most common reaction type. Other types include transamidation and double replacement.
A transaminase is a type of enzyme that catalyzes a variety of steps in the amino acid pathway. These reactions are reversible and highly enantioselective. They can also be used for kinetic resolution of racemic compounds. There are various types of transaminases, including o-TAs, p-TAs, and l-TAs. Among them, o-TAs are the most active and specific for a-amino acids.
The first stage of the transamination process is initiated by the formation of a Schiff base. This is the linkage formed by the aldehyde group of an enzymatic Lys residue and a positively charged pyridinium ion. An e-amino group from the amino acid is then transferred to the PLP.
During the second phase of the transamination process, the a-keto acid is formed. As a result, the carbonyl group of the amino acid is transferred to the carbonyl group of a keto acid.
The a-keto carboxylic acids are then converted into acetoacetyl-CoA. Acetoacetyl-CoA is then used to synthesize fatty acids.