ADK (adenosine kinase) is a cytosolic enzyme that catalyzes ATP-dependent phosphorylation of adenosine and modified adenosine nucleosides at the 5' position 12. A primary function of ADK is detoxification of modified adenosines containing N(6)-methylated adenine (m6A) post-transcriptional modifications derived from RNA degradation 2. ADK phosphorylates methylated adenosine nucleotides including m6A, m6,6A, and i6A into AMP intermediates for further detoxification 2. Recent studies reveal ADK's metabolic significance in disease pathogenesis. In hepatocytes, ADK promotes excessive fat deposition and liver inflammation by suppressing fatty acid oxidation through increased DNA methylation and decreased Ppara expression, linking it to nonalcoholic fatty liver disease progression 3. In vascular smooth muscle cells, ADK inhibition attenuates abdominal aortic aneurysm formation through epigenetic modulation via decreased S-adenosylmethionine-dependent transmethylation, reducing H3K4me3 binding to inflammatory gene promoters 4. Clinically, ADK deficiency causes hypermethioninemia. The discovery that ADK regulates methylation reactions independent of adenosine receptor signaling identifies it as a potential therapeutic target for metabolic and vascular diseases, particularly through selective ADK inhibition.