Overview:

Lysyl-endopeptidase (Lys-c) was isolated from the Gram-negative soil bacterium Achromobacter lyticus by Masaki et al. The protein hydrolyzes amide and peptide ester bonds at the carboxylic side of lysine and S-aminoethylcysteine residues making it an important tool for enzymatic protein sequencing and Lys-X compound synthesis. The enzyme functions optimally between 30 – 37^oC and suffers from degradation when subjected to temperatures above 50^oC.Lysyl-endopeptidase retains complete activity after incubation in 4M urea or in 0.1% SDS solution for up to 6 hours at 30^oC. Conversely, the enzyme is inhibited by DFP, PMSF, TLCK. Lysyl-endopeptidase is involved during the production of recombinant insulin and in proteomics research.

Gene Aliases:

API, Protease I, Lysyl endopeptidase