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  • Title: Myxobacter AL-1 protease II: specific peptide bond cleavage on the amino side of lysine.
    Author: Wingard M, Matsueda G, Wolfe RS.
    Journal: J Bacteriol; 1972 Nov; 112(2):940-9. PubMed ID: 4343825.
    Abstract:
    A second extracellular protease from myxobacter strain AL-1 has been purified to homogeneity and named protease II; the enzyme crystallizes as fine needles. The extracellular, cell wall lytic protease reported previously from the same organism is now designated protease I. Protease II exhibits a pH optimum of 8.5 to 9.0 and is stable from pH 3.0 to 9.0. The enzyme is heat stable at 50 C for 18 hr. Results of sedimentation equilibrium studies yielded a molecular weight of 17,000, and amino acid analysis revealed 157 residues with a minimal molecular weight of 16,660. Cleavage of peptide bonds in the oxidized B-chain of insulin, cytochrome c (horse heart). lysozyme, and vasopressin is restricted to the amino side of lysine. Dilysine and trilysine were not hydrolyzed. Products from digestions of polylysine were lysine and dilysine.
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