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Matrilysin, a matrix metalloproteinase (MMP) that lacks the hemopexin domain, retains its catalytic function. This suggests that the hemopexin domain is not required for maintenance of MMP latency, for activation with organomercurials or for binding of inhibitors to the active site. Hemopexin-domain-deleted stromelysin-1 (SL-1) was used to investigate the role of the propeptide in the latency and activation of the enzyme. Mini-SL-1 propeptide deletion gave rise to enzymes with greatly accelerated spontaneous autolytic processing of the propeptide.

The 4-aminophenylmercuric acetate (APMA) is an organomercurial element that activates stromelysin-1 of matrix metalloproteases. The activation of APMA on stromelysin-1 includes other protein interactions besides the detected reaction in the highly conserved amino acid sequence with the cysteine residue. The activity of APMA was inhibited by the diruption of the salt bridge in SL-1 that connects R74 and D79.