Role of metalloprotease in activation of the precursor of staphylococcal protease.
A metalloprotease was isolated from the culture medium of a mutant of Staphylococcus aureus strain V8. The enzyme had a molecular weight of 38,000 as estimated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and an optimum pH of 7.0 and exhibited a specificity for peptide bonds on the N-terminal side of large hydrophobic residues. The protease was fully inactivated by 0-phenanthroline but could be reactivated by zinc ions. Cobalt may be substituted for zinc, producing an activity which corresponds to 160% of that of the native enzyme. All these data indicate that this protease is a typical bacterial neutral metalloprotease. The role of this metalloprotease in the activation of the precursor of another protease secreted by the same organism, staphylococcal protease, has been identified. Mutants which lack the metalloprotease accumulated the precursor, which can be specifically activated by the addition of the purified metalloprotease or the related enzyme thermolysin. The purification of the precursor is also reported.
D000596:Amino Acids / Q000032:analysis; D003035:Cobalt / Q000494:pharmacology; D004789:Enzyme Activation; D004792:Enzyme Precursors / Q000378:metabolism*; D010447:Peptide Hydrolases / Q000032:analysis / Q000302:isolation & purification / Q000378:metabolism*; D013211:Staphylococcus aureus / Q000201:enzymology*; D015032:Zinc / Q000494:pharmacology
D000596:Amino Acids; D004792:Enzyme Precursors; D003035:Cobalt; D010447:Peptide Hydrolases; D015032:Zinc