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Human full-length CBS polypeptide has three functional domains: (i) an N-terminal domain (residues 1–70) containing residues C52 and H65 that coordinate the ferric heme-b cofactor, (ii) a central catalytic domain (CD, residues 70–381) with the evolutionary conserved K119 residue binding the PLP cofactor via a Schiff bond and (iii) a C-terminal regulatory domain (RD, residues 414–551), that upon binding SAM activates CBS by 3–9-fold (Fig

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21 BridgmanS