S‐Adenosyl‐L‐homocysteine hydrolase from Dictyostelium discoideum is inactivated by cAMP and reactivated by NAD+
- 9 January 1984
- journal article
- Published by Wiley in FEBS Letters
- Vol. 165 (2) , 265-268
- https://doi.org/10.1016/0014-5793(84)80182-9
Abstract
Purified S‐adenosyl‐L‐homocysteine hydrolase from Dictyostelium discoideum is inactivated when incubated at 25°C with cAMP. Half maximal velocity of the inactivation process occurs at 10 μM 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 directly to the assay. These results suggest a role for cAMP and NAD+ in the regulation of cellular methylation reactions by altering the level of S‐adenosyl‐L‐homocysteine via S‐adenosyl‐L‐homocysteine hydrolase.Keywords
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