Product details
Background:
catalytic activity:Cleavage of gelatin types I and V and collagen types IV and V., cofactor:Binds 2 zinc ions per subunit., cofactor:Binds 3 calcium ions per subunit., disease:Defects in MMP9 may be a cause of susceptibility to lumbar disk herniation (LDH) [MIM:603932]. LDH is the predominant cause of low-back pain and unilateral leg pain., domain:The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme., enzyme regulation:Inhibited by histatin-3 1/24 (histatin-5)., function:May play an essential role in local proteolysis of the extracellular matrix and in leukocyte migration. Could play a role in bone osteoclastic resorption. Cleaves KiSS1 at a Gly-|-Leu bond. Cleaves type IV and type V collagen into large C-terminal three quarter fragments and shorter N-terminal one quarter fragments. Degrades fibronectin but not laminin or Pz-peptide., induction:Activated by 4-aminophenylmercuric acetate and phorbol ester., miscellaneous:In the arthritis patient this enzyme might contribute to the pathogenesis of joint destruction and might constitute a useful marker of disease status., PTM:N- and O-glycosylated., PTM:Processing of the precursor yields different active forms of 64, 67 and 82 kDa. Sequentially processing by MMP3 yields the 82 kDa matrix metalloproteinase-9., similarity:Belongs to the peptidase M10A family., similarity:Contains 3 fibronectin type-II domains., similarity:Contains 4 hemopexin-like domains., subunit:Exists as monomer, disulfide-linked homodimer, and as a heterodimer with a 25 kDa protein. Macrophages and transformed cell lines produce only the monomeric form., tissue specificity:Produced by normal alveolar macrophages and granulocytes.,
