5-phosphohydroxy-L-lysine phospho-lyase (PHYKPL)

5-phosphohydroxy-L-lysine phospho-lyase (PHYKPL) is a mitochondrial enzyme encoded by the nuclear PHYKPL gene in humans. It catalyzes the breakdown of 5-phosphonooxy-L-lysine to form ammonia, inorganic phosphate, and 2-aminoadipate semialdehyde in a pyridoxal phosphate-dependent reaction[2][3][4]. This enzyme plays a role in lysine degradation. Mutations in PHYKPL may be associated with the rare metabolic disorder phosphohydroxylysinuria[2][4]. The enzyme is localized to the mitochondrion and belongs to the lyase family, specifically characterized by its dependence on the cofactor pyridoxal phosphate[3]. There is no evidence that it is currently a direct therapeutic target for any drug, but it is of biochemical and genetic disease interest.

Other names

AGXT2L2Alanine--glyoxylate aminotransferase 2-like 2PHLU5-phosphonooxy-L-lysine phospho-lyasePP9286MGC15875

Catalysis of 5-phosphohydroxy-L-lysine cleavage; for drugs/cofactors: pyridoxal phosphate acts as an essential cofactor