Figure 1

A schematic view of the different reaction types catalyzed by PLP-dependent enzymes that act on amino acids. In these enzymes, PLP is bound to the ε-amino group of a catalytic lysine residue, forming a Schiff base (internal aldimine). Covalent binding of the substrate amino acid occurs through a transimination reaction, leading to formation of an external aldimine intermediate (structure on the upper left corner). Subsequently, the protonated ring system of PLP acts as an electron sink, to stabilize species carrying a negative charge on the α-carbon (carbanions). Depending on the enzyme (and hence on the specific arrangement of the active site residues) such stabilized carbanions can be formed upon cleavage of any of the three covalent bonds connecting the α-carbon to its substituents. Removal of the carboxylate group is typical of decarboxylases. Removal of the amino acid side chain occurs for example in threonine aldolase. Finally, removal of the α-proton may be the prequel to the formation of various further intermediates, leading to racemization, cyclization, β- and γ-elimination, and transamination reactions [1, 4, 7].