AGXT encodes alanine-glyoxylate aminotransferase (AGT), a peroxisomal enzyme catalyzing transamination of glyoxylate to glycine, thereby detoxifying glyoxylate and preventing oxalate accumulation 123. AGXT also catalyzes transamination between L-serine and pyruvate, contributing to gluconeogenesis 4. Mechanistically, AGT functions as a liver-specific enzyme that regulates the balance between glyoxylate detoxification and oxalate production; when AGXT is suppressed, glyoxylate accumulates and is converted to oxalate by lactate dehydrogenase 5. Loss-of-function mutations in AGXT cause primary hyperoxaluria type 1 (PH1), an autosomal recessive metabolic disorder characterized by excessive endogenous oxalate production leading to calcium oxalate crystal deposition in kidneys, renal dysfunction, and systemic oxalosis 67. PH1 accounts for approximately 68.4% of primary hyperoxaluria cases 7. Recent evidence indicates AGXT suppression also contributes to metabolic dysfunction-associated steatohepatitis (MASH) pathogenesis, where elevated oxalate inhibits fatty acid β-oxidation 5. Clinically, AGXT gene therapy approaches—including CRISPR-Cas9-mediated correction, mRNA replacement therapy, and substrate reduction strategies—show promise for PH1 treatment 8910. Combined liver-kidney transplantation remains the only permanent curative treatment currently available.