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Zinc metalloproteinase aureolysin is a secreted extracellular metalloprotease from *Staphylococcus aureus*, belonging to the thermolysin/M4 family of zinc-dependent proteinases[3]. The mature enzyme consists of a 301-amino acid catalytic domain processed from a larger precursor, and binds one zinc and up to three calcium ions for activity and structural integrity[1][3]. Aureolysin can degrade host plasma proteinase inhibitors, activate prothrombin, modulate immune responses, and process other bacterial proteins, playing an essential role in the virulence and immune evasion capacity of *S. aureus*[1][2][4]. While widely accepted as a bacterial virulence factor and potential therapeutic target, there are currently no approved clinical inhibitors specific to aureolysin[3][4].
Metal chelation (inhibition by removal/blocking of catalytic zinc/cofactor); Protease inhibition (blocking the active site or substrate access)[3]
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