catalytic activity:Preferential cleavage where P1' , P2' and P3' are hydrophobic residues. ,cofactor:Binds 2 zinc ions per subunit. ,cofactor:Binds 4 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. ,function:Can degrade fibronectin , laminin , gelatins of type I , III , IV , and V; collagens III , IV , X , and IX , and cartilage proteoglycans. Activates procollagenase. ,similarity:Belongs to the peptidase M10A family. ,similarity:Contains 4 hemopexin-like domains. ,
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