S-adenosyl-L-homocysteine hydrolase from Dictyostelium discoideum is inactivated by cAMP and reactivated by NAD+.

@article{Hohman1984SadenosylLhomocysteineHF,
  title={S-adenosyl-L-homocysteine hydrolase from Dictyostelium discoideum is inactivated by cAMP and reactivated by NAD+.},
  author={R J Hohman and M. Veron},
  journal={FEBS letters},
  year={1984},
  volume={165 2},
  pages={
          265-8
        }
}
Purified S-adenosyl-L-homocysteine hydrolase from Dictyostelium discoideum is inactivated when incubated at 25 degrees C with cAMP. Half maximal velocity of the inactivation process occurs at 10 microM cAMP. Catalytic activity is fully restored by further incubation with NAD+, but not with NADP+ or NADH. The enzyme must be preincubated with cAMP or NAD+ to induce inactivation or reactivation, respectively, since neither of these ligands has an effect on the active or inactive enzyme when added… CONTINUE READING
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