Saccharopine Dehydrogenase NAD-binding and catalytic domains
Saccharopine Dehydrogenase (SDH) catalyzes the final step in the reversible NAD-dependent oxidative deamination of saccharopine to alpha-ketoglutarate and lysine, in the alpha-aminoadipate pathway of L-lysine biosynthesis. SHD is structurally related to formate dehydrogenase and similar enzymes, having a 2-domain structure in which a Rossmann-fold NAD(P)-binding domain is inserted within the linear sequence of a catalytic domain of related structure.
Comment:Saccharomyces Cervisiae Saccharopine Dehydrogenase retains the 3D arrangement of the GxGxxG(17-18x)D NAD binding site motif, but has altered spacing between the conserved residues: GxxGxxG(17-20x)D