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S ‐Adenosyl‐L‐homocysteine hydrolase from Dictyostelium discoideum is inactivated by cAMP and reactivated by NAD +
Author(s) -
Hohman Robert J.,
Veron Michel
Publication year - 1984
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(84)80182-9
Subject(s) - nad+ kinase , dictyostelium discoideum , hydrolase , enzyme , biochemistry , incubation , chemistry , biology , microbiology and biotechnology , gene
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.