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Stromelysin-1 also known as matrix metalloproteinase-3 (MMP-3) is an enzyme that in humans is encoded by the MMP3 gene. The MMP3 gene is part of a cluster of MMP genes which localize to chromosome 11q22.3. [5] MMP-3 has an estimated molecular weight of 54 kDa. [6]
X-ray crystallographic structures of several MMP catalytic domains have shown that this domain is an oblate sphere measuring 35 x 30 x 30 Å (3.5 × 3 x 3 nm). The active site is a 20 Å (2 nm) groove that runs across the catalytic domain.
Hydroxypyrone-based MMP inhibitors are structurally corresponding to the pyrimidinetriones. A recent inhibitor is the compound 3-hydroxypyran-4-one nominated 868368-30-3. It is MMP-3 selective and its 0,0-bidentate chelation of zinc is the structural part proposed to be responsible for the MMP recognition. [7]
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MMP can be defined as a pair of molecules that differ in only a minor single point change (See Fig 1). Matched molecular pairs (MMPs) are widely used in medicinal chemistry to study changes in compound properties which includes biological activity, toxicity, environmental hazards and much more, which are associated with well-defined structural modifications.
The structure and reaction path was determined in 2002 with NMR studies. Much of what we know about pDADMAC in water treatment and personal care is from Jerry Boothe of Calgon Corporation . Synthesis