Protein-lysine 6-oxidase (LOX) (LOX)

Protein-lysine 6-oxidase, commonly known as lysyl oxidase (LOX), is a secreted copper-dependent enzyme essential for the structural integrity of the extracellular matrix (ECM) [1, 14]. It catalyzes the oxidative deamination of lysine and hydroxylysine residues in collagen and elastin precursors, leading to the formation of covalent cross-links that stabilize these fibrous proteins [4, 15]. This process is critical for connective tissue maturation, wound healing, and vascular development [1, 18]. In pathological contexts, LOX is frequently upregulated, particularly in various cancers where it promotes tumor progression, invasion, and metastasis by increasing ECM stiffness and remodeling the tumor microenvironment [3, 9, 15]. It also plays a central role in the pathogenesis of fibrotic diseases of the lung, liver, and kidney, where excessive cross-linking leads to organ dysfunction [2, 7, 19]. Consequently, LOX has emerged as a significant therapeutic target, with small-molecule inhibitors like beta-aminopropionitrile (BAPN) and more selective agents like CCT365623 being investigated to mitigate fibrosis and cancer spread [4, 5, 8]. However, therapeutic targeting must balance efficacy with safety, as systemic inhibition can lead to connective tissue defects such as osteolathyrism and vascular complications like aortic aneurysms [1, 14].

Other names

Lysyl oxidaseLOXAAT10LAAOLao

Irreversible inhibition of the copper-dependent catalytic site and competitive inhibition of the active site to prevent oxidative deamination of lysine residues.