Fig. 5. Computational analysis of the catalytic mechanism of the newly discovered TA. We applied a variety of computational tools to simulate the progression of the reaction within the active site of the enzyme. The Gibbs free energy of binding has also been estimated for each pose. Panel 1: binding of PLP within the active site and the close proximity of the K183 residue; panel 2: reaction between the PLP and the K183 residue to form the internal aldimine; panel 3: docking of o-xylylenediamine within the active site of the aldimine-functionalized TA; panel 4: docking of (S)-(−)-1-phenylethylamine within the active site of the aldimine-functionalized TA; panel 5: docking of (R)-(+)-1-phenylethylamine within the active site of the aldimine-functionalized TA and confirmation of non-reactivity due to the large distance between its nitrogen atom and the nitrogen atom in the aldimine bond; panel 6: formation of the ketamine intermediate on account of the reaction between o-xylylenediamine and PLP; panel 7: formation of PMP in the active site; panel 8: docking of benzaldehyde within the active site of the TA alongside PMP; panel 9: docking of acetophenone within the active site of the TA alongside PMP; panel 10: docking of 2,6-dimethyl-p-benzoquinone within the active site of the TA alongside PMP.