Peptidyl-L-lysine(-L-arginine) hydrolase

Peptidyl-L-lysine(-L-arginine) hydrolase is an enzyme that catalyzes the hydrolysis of peptide bonds involving L-lysine or L-arginine residues. Specifically, it breaks the bond between the carboxyl group of a peptide-bound lysine or arginine and the amino group of an adjacent amino acid. The enzyme is classified as a hydrolase, reflecting its mechanism of action involving the addition of water to cleave the chemical bond. The "( -L-arginine)" portion of the name indicates that while the enzyme primarily acts on lysine residues, it may also exhibit activity, though potentially at a lower rate, on arginine residues within a peptide chain.

The primary function of peptidyl-L-lysine(-L-arginine) hydrolases is in protein and peptide degradation. They contribute to the breakdown of proteins into smaller peptides and eventually into free amino acids. These enzymes may be involved in a variety of cellular processes including protein turnover, processing of pro-proteins into active forms, and the breakdown of damaged or misfolded proteins. Different peptidyl-L-lysine(-L-arginine) hydrolases may exhibit substrate specificity, meaning they preferentially cleave peptide bonds adjacent to lysine or arginine in particular sequence contexts or within specific protein substrates. Further research is often required to fully characterize the specific function and regulation of individual enzymes within this class.