S‐Adenosyl‐L‐homocysteine hydrolase from Dictyostelium discoideum is inactivated by cAMP and reactivated by NAD+

FEBS Letters

Hohman, Robert J.¹  Veron, Michel¹ 

[1] Unité de Biochimie Cellulaire, Département de Biochimie et Génétique Moléculaire, Institut Pasteur, 28 rue du Dr Roux, 75724 Paris Cedex 15, France

关键词: S-Adenosyl-L-homocysteine hydrolase;    Cyclic AMP;    Methylation;    NAD +;    Differentiation;    Enzyme inactivation;    SAH;    S-adenosyl-L-homocysteine;    SAH hydrolase;    S-adenosyl-L-homocysteine hydrolase (EC 3.3.1.1);    Mops;    3-(N-morpholino)propanesulfonic acid;   

DOI  :  10.1016/0014-5793(84)80182-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown