“…Lys278 (273), lysine residue forming a Schiff base (internal aldimine) with the bound PLP in the unliganded enzyme, involved in , -elimination (see Scheme 2 and Section 5.04.2.2.1); Asn209 (202), Tyr240 (233), and Asp237 (230), amino acid residues forming hydrogen bonds with O39 of the pyridine ring and N1 of PLP; Ala127 (120), Thr128 (121), Ser275 (270), Ser277 (272), and Arg286 (281), amino acid residues required for the correct orientation of PLP in the active site, and all of them interact with the oxygens of PLP phosphate moiety (see Scheme 2); Tyr152 (145), mediates the formation of ACC from SAM via a catalytic mechanism involving a quinoid intermediate (according to Li et al 29 ) and stabilizes the pyridine ring of PLP; Glu55 (47), putative ionic interaction between SAM and this residue; Ala54 (46) and Arg412 (407), the -carboxylate group of SAM forms hydrogen bonds with the nitrogen of alanine and the guanidino moiety of arginine; Arg157 (150), O29 and O39 atoms of the sugar of SAM form hydrogen bonds with the guanidine group of arginine; Pro26 (Ser18), Tyr27 (19), Phe28 (20), and Pro153 (144), residues contributing to the hydrophobic pocket for the adenine ring of SAM; Tyr92 (85), probably acts as a platform for the adenine ring of SAM and binds it through a stacking interaction.…”