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. 1972 Nov;112(2):940–949. doi: 10.1128/jb.112.2.940-949.1972

Myxobacter AL-1 Protease II: Specific Peptide Bond Cleavage on the Amino Side of Lysine

Marilyn Wingard 1, Gary Matsueda 1, R S Wolfe 1
PMCID: PMC251506  PMID: 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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Selected References

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