Catalytic activity:Glutamyl endopeptidase; bonds cleaved include 370-Thr-Glu-Gly-Glu-|-Ala-Arg-Gly-Ser-377 in the interglobular domain of mammalian aggrecan.,Caution:Has sometimes been referred to as ADAMTS2.,cofactor:Binds 1 zinc ion 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.,Domain:The spacer domain and the TSP type-1 domains are important for a tight interaction with the extracellular matrix.,Function:Cleaves aggrecan, a cartilage proteoglycan, and may be involved in its turnover. May play an important role in the destruction of aggrecan in arthritic diseases. Could also be a critical factor in the exacerbation of neurodegeneration in Alzheimer disease. Cleaves aggrecan at the '392-Glu-|-Ala-393' site.,induction:By interleukin-1.,PTM:The precursor is cleaved by a furin endopeptidase.,similarity:Contains 1 disintegrin domain.,similarity:Contains 1 peptidase M12B domain.,similarity:Contains 1 TSP type-1 domain.,tissue specificity:Expressed in brain, lung and heart. Expressed at very low level in placenta and skeletal muscles.,
展开内容