Ethanolamine-phosphate phospho-lyase (ETNPPL)

Ethanolamine-phosphate phospho-lyase (ETNPPL), also known as AGXT2L1, is a pyridoxal 5′-phosphate–dependent enzyme that catalyzes the irreversible degradation of O-phosphoethanolamine into acetaldehyde, ammonia, and inorganic phosphate[1][3][6][8]. This step is critical for controlling the availability of phosphoethanolamine, a precursor for phosphatidylethanolamine synthesis in the Kennedy pathway, a major route for mammalian membrane formation[1][3][5][6]. ETNPPL is expressed in tissue types such as liver, brain (particularly in mature astrocytes), salivary gland, kidney, and stomach[4][5][7][9][11]. Dysregulation of ETNPPL impacts lipid homeostasis, and is associated with metabolic liver disease, psychiatric disorders, and hepatocellular carcinoma, in which its downregulation correlates with increased cell migration/invasion and poor prognosis[4][5][8]. Although no direct therapeutic agents target ETNPPL to date, its unique role in lipid metabolism and disease biomarker qualities make it a notable molecular target for future biomedical research[3][5][8][11].

Other names

AGXT2L1Alanine--glyoxylate aminotransferase 2-like 1AT2L1Etnppl1300019H02Rik (mouse ortholog)

Not established; as a metabolic enzyme in a biosynthetic pathway, hypothetical inhibitors would alter phospholipid synthesis by blocking phosphoethanolamine catabolism, leading to altered membrane composition