Alanine-glyoxylate aminotransferase (AGXT)

Alanine-glyoxylate aminotransferase (AGXT) is a pyridoxal phosphate-dependent enzyme localized to peroxisomes in human liver cells, encoded by the AGXT gene. The enzyme catalyzes the transfer of an amino group from L-alanine to glyoxylate, forming pyruvate and glycine—this reaction is critical for the detoxification of glyoxylate. When AGXT is deficient or mislocalized due to pathogenic mutations, glyoxylate accumulates and is converted into oxalate, leading to primary hyperoxaluria type 1 (PH1), a rare autosomal recessive disorder characterized by recurrent kidney stones and, in severe cases, systemic oxalosis and renal failure. The severity of the condition depends on the nature of the mutation, which may result in complete loss of activity, misfolding, or aberrant targeting to mitochondria. Pyridoxine supplementation may improve enzyme activity in some mutation carriers. Monitoring of urinary and plasma oxalate, detection of AGXT mutations, and early therapeutic intervention are central to disease management

Other names

AGXT1AGTAGT1SPATSPTTLH6PH1Ser-PyrATSerine-pyruvate aminotransferaseprimary hyperoxaluria type 1 enzymeL-alanine:glyoxylate aminotransferase 1glycolicaciduria enzymehepatic peroxisomal alanine:glyoxylate aminotransferasealanine-glyoxylate and serine-pyruvate aminotransferase

Pyridoxine acts as a cofactor supporting enzyme activity and may partially restore function and correct mislocalization in certain AGXT mutations\nPharmacological chaperones or agents preventing mitochondrial mistargeting of the enzyme are under investigation