in contrast to Gram-negative bacterial aspartate-beta-semialdehyde dehydrogenases which are specific for NADP+ the enzyme of Gram-positive showed a dual specificity for NAD+ and NADP+
very low activity with the wild-type enzyme, but 44fold and 66fold higher activity with enzyme mutants Q350N and Q350N/H171A, respectively, compared to the wild-type
in contrast to Gram-negative bacterial aspartate-beta-semialdehyde dehydrogenases which are specific for NADP+ the enzyme of Gram-positive showed a dual specificity for NAD+ and NADP+
the NADP+-binding domain consists of mixed beta-strands flanked on both sides with alpha-helices, with seven beta-strands, five alpha-helices and two 310-helices
the nicotinamide moiety near the active site cysteine also places it in an optimal position for hydride transfer from NADPH to the enzyme-bound intermediate during the catalytic cycle