Selenocysteine lyase (SCL)

Selenocysteine lyase is a pyridoxal 5'-phosphate-dependent enzyme that specifically catalyzes the decomposition of L-selenocysteine to L-alanine and elemental selenium (selenide), contributing to the recycling of selenium from the degradation of selenoproteins[1][2][3][4][5][6][7]. It exhibits strict substrate specificity for L-selenocysteine and does not act on L-cysteine. Selenocysteine lyase is found primarily in the liver and kidney, usually as a homodimer in mammals, and plays a crucial cellular role in selenium metabolism and homeostasis by providing a source of selenide for new selenoprotein biosynthesis[7][3]. Its molecular structure includes a conserved catalytic cysteine residue essential for substrate specificity, and its activity is vital for maintaining optimal selenium levels in organisms[3][1]. There are no current drugs targeting selenocysteine lyase, nor is it a recognized direct therapeutic target or disease biomarker.

Other names

SCLSCLYL-selenocysteine selenide-lyase (L-alanine-forming)selenocysteine β-lyaseselenocysteine reductase