MMP8

Neutrophil collagenase ;
Matrix metalloproteinase-8 ;
MMP-8 ;
PMNL collagenase ;
PMNL-CL ;

catalytic activity:Cleavage of interstitial collagens in the triple helical domain. Unlike EC 3.4.24.7, this enzyme cleaves type III collagen more slowly than type I.,cofactor:Binds 2 zinc ions per subunit.,cofactor:Binds 3 calcium ions per subunit.,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:Cannot be activated without removal of the activation peptide.,function:Can degrade fibrillar type I, II, and III collagens.,similarity:Belongs to the peptidase M10A family.,similarity:Contains 4 hemopexin-like domains.,subcellular location:Stored in intracellular granules.,tissue specificity:Neutrophils.,

skeletal system development, ossification, proteolysis, collagen catabolic process, collagen metabolic process,multicellular organismal metabolic process, multicellular organismal catabolic process, multicellular organismal macromolecule metabolic process, bone development,

Cytoplasmic granule. Secreted, extracellular space, extracellular matrix . Stored in intracellular granules.

Neutrophils.