Stabilization vs. degradation of Staphylococcus aureus metalloproteinase |
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Authors: | J Potempa Z Porwit-Bobr J Travis |
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Affiliation: | Department of Microbiology and Immunology, Jagiellonian University, Kraków, Poland. |
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Abstract: | Purified Staphylococcus aureus metalloproteinase contains trace amounts of a serine proteinase which rapidly degrades the metalloproteinase when EDTA is present. However, no degradation occurs when Ca2+ is added or if the serine proteinase is removed by immunoaffinity chromatography. Selective chelation of Zn2+ by o-phenanthroline, which reversibly inactivates the metalloproteinase, does not result in the degradation of the apometalloproteinase, even with excess of serine proteinase. These data are interpreted as follows: EDTA chelates enzyme-bound Ca2+ and Zn2+, causing irreversible inactivation as well as a conformational change in the metal-free protein. This allows proteolysis by the contaminating serine proteinase and explains why the metalloproteinase purified from serine proteinase-deficient strains of S. aureus was previously thought to be stable to autolysis. |
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