Prenylcysteine oxidase 1 (PCYOX1)

Prenylcysteine oxidase 1 (PCYOX1) is a monomeric, FAD-dependent enzyme that catalyzes the oxidative cleavage of thioether bonds in prenylated cysteine residues, producing free cysteine, an isoprenoid aldehyde (e.g., farnesal or geranylgeranial), and hydrogen peroxide[1][3][4][5]. It plays a key role in the final catabolic step of prenylated protein turnover, metabolizing S-farnesyl-L-cysteine and S-geranylgeranyl-L-cysteine produced from proteolysis of prenylated proteins[1][3][5]. Structurally, PCYOX1 contains a classical dinucleotide-binding (Rossmann) domain and a substrate-binding domain with hydrophobic regions for membrane association and direct interaction with cell membranes[1][3]. PCYOX1-generated hydrogen peroxide contributes to oxidative stress within lipoproteins, linking the enzyme to the development and progression of atherosclerosis[4]. Inhibitors targeting the active site have been designed, and the enzyme is also capable of metabolizing certain xenobiotics, suggesting roles in drug metabolism[1][3]. PCYOX1 is considered both a novel therapeutic target and a potential biomarker in cardiovascular and inflammatory diseases due to its involvement in oxidative lipid modification and pro-inflammatory processes[4].

Other names

Prenylcysteine lyaseKIAA0908PCL1UNQ597/PRO1183

Cleavage of thioether bond in prenyl-L-cysteines (oxidative degradation); Competitive and non-competitive inhibition of enzyme active site by designed small molecules