During the transamination process, the enzyme transaminases use Pyridoxal pyrophosphate as a cofactor.
All transamination reactions, as well as several amino acid oxylation and deamination processes, involve the coenzyme pyridoxal phosphate. The aminotransferase enzyme's epsilon-amino group of a particular lysine group forms a Schiff-base bond with the aldehyde group of pyridoxal phosphate.
The epsilon-amino group of the lysine residue in the active site is replaced by the alpha-amino group of the amino acid substrate. The ensuing intermediate, a quinoid, undergoes deprotonation to become an aldimine, which is then protonated to become a ketimine by accepting a proton in a different position. Ketamine undergoes hydrolysis, leaving the amino group on the protein complex intact.
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