peptidyl-lysine 3-dioxygenase activity

Definition

Target type: molecularfunction

Catalysis of the reaction: protein L-lysine + 2-oxoglutarate + O2 = protein 3-hydroxy-L-lysine + succinate + CO2. [GOC:al, PMID:29915238, RHEA:57152]

Peptidyl-lysine 3-dioxygenase (PKD) is an enzyme that catalyzes the hydroxylation of peptidyl-lysine residues to peptidyl-3-hydroxylysine. This reaction involves the incorporation of one atom of molecular oxygen into the substrate, and the other atom of oxygen is reduced to water. PKD requires ferrous iron as a cofactor and utilizes a non-heme iron center for catalysis. The reaction mechanism proceeds through a series of steps: 1) binding of the substrate peptidyl-lysine and dioxygen to the enzyme, 2) activation of molecular oxygen by the ferrous iron center, 3) formation of a reactive oxygen species, 4) hydroxylation of the substrate, and 5) release of the product peptidyl-3-hydroxylysine. This hydroxylation reaction plays a critical role in the biosynthesis of collagen, elastin, and other extracellular matrix proteins. Hydroxylysine residues serve as sites for cross-linking between polypeptide chains, contributing to the structural integrity and stability of these proteins. PKD is also involved in the regulation of cellular processes such as cell growth, differentiation, and angiogenesis. Its activity can be regulated by various factors including oxygen availability, pH, and the presence of specific inhibitors. The precise molecular mechanisms underlying these regulatory events are still under investigation.'
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Proteins (2)

Compounds (1)