Lysyl oxidase is the key enzyme responsible for the crosslinking of collagen fibrils. It plays a critical role in collagen maturation by catalyzing the oxidative deamination of lysine residues in collagen molecules, which results in the formation of reactive aldehydes. These aldehydes then facilitate the formation of covalent cross-links between collagen molecules, which are crucial for the stability and strength of the collagen fibrils.
Although prolyl hydroxylase and lysyl hydroxylase are also involved in collagen biosynthesis by modifying proline and lysine residues, they are not directly responsible for the crosslinking process. Prolyl oxidase is involved in the hydroxylation of proline but does not contribute to the formation of cross-links in collagen.
The crosslinking of collagen is vital for its structural function, providing tensile strength and resilience to connective tissues such as skin, tendons, and bones.