Lysyl Endopeptidase® was originally isolated from soil bacterium. Initially the source was indicated as Achromobacter lyticus, based upon physiological and morphological properties.
However, the 16SrDNA sequence has since been confirmed as highly homologous to Lysobacter.
Lysyl Endopeptidase specifically cleaves the peptide bonds at the carboxyterminal side of Lysine and S-aminoethylcysteine residues, with a high degree of specificity. This makes it a valuable tool for protein sequence analysis and for enzymatic synthesis of Lys-X compounds.
An added feature of Lysyl Endopeptidase is its ability to retain complete activity after incubation in 4M urea or in 0.1% SDS solution for up to 6 hours at 30 degrees C.