Alpha-lytic endopeptidase or Alpha-lytic protease (EC 3.4.21.12, "myxobacter alpha-lytic proteinase", "alpha-lytic proteinase", "alpha-lytic protease", "Mycobacterium sorangium alpha-lytic proteinase", "Myxobacter 495 alpha-lytic proteinase") is an enzyme isolated from the myxobacterium "Lysobacter enzymogenes". This enzyme is a serine protease that catalyses the breakage of peptide bonds using a hydrolysis chemical reaction. Alpha-lytic protease was named based on the observed cleavage specificity for the α position of the tetrapeptide component in gram-positive bacterial cell walls (alanine). Alpha-lytic protease is also capable of digesting elastin and other proteins.
This protease was recently applied to proteome digestion for production of peptides for mass spectrometry-based proteomics, where it was found to cleave preferentially after several small amino acids, including alanine, serine, threonine, valine, and to a lesser extent, methionine. This specificity is very different than the most commonly-used protease for proteomics, trypsin, which cleaves only after arginine and lysine.
Alpha-lytic protease was also recently reported to find utility as part of a method to map endogenous SUMO modification sites in the proteome.
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