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S-adenosylhomocysteine hydrolase (SAHH) is a highly conserved enzyme that catalyzes the reversible hydrolysis of S-adenosylhomocysteine (SAH) into homocysteine and adenosine. It plays a central role in cellular methylation processes and methionine metabolism by regulating the levels of SAH, a potent inhibitor of methyltransferases. AHCY mutations cause SAHH deficiency, leading to elevated methionine/creatine kinase levels and widespread inhibition of cellular methyltransferases. Pharmacologically targeting SAHH has been explored as an indirect means to modulate intracellular transmethylations.
Inhibition of SAHH increases SAH levels, inhibiting methyltransferases.
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