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Description

A potent, selective, slow-binding and mechanism-based inhibitor of human gelatinases, MMP-2 (Ki = 13.9 nM) and MMP-9 (Ki = 600 nM). It also exhibits a covalent mechanism based behavior in inhibition of these enzymes. This inhibitor appears to have similarity to TIMP-1 and TIMP-2 in the slow-binding component of inhibition. Shown to directly bind to the zinc in the catalytic site of MMP-2. Does not affect the activities of MMP-1 (Ki = 206 µ,M) MMP-3 (Ki = 15 µ,M), or MMP-7 (Ki = 96 µ,M)., A potent, selective, slow-binding and mechanism-based inhibitor of human gelatinases, MMP-2 (Ki = 13.9 nM), and MMP-9 (Ki = 600 nM). This inhibitor appears to behave similarly to TIMP-1 and TIMP-2 in the slow-binding component of inhibition. Also exhibits a covalent mechanism-based behavior in inhibition of these enzymes. Binds directly to the catalytic zinc ion on MMP-2.