Bontoxilysin
Definition:
EC Tree > 3 Hydrolases > 3.4 Acting on peptide bonds (peptidases) > 3.4.24 Metalloendopeptidases > 3.4.24.69 bontoxilysin
Interstitial collagenase is a secreted zinc metalloendopeptidase, the type example of peptidase family M10, widely distributed in vertebrates and named for its substrates types I, II and III interstitial collagens, all cleaved in the helical domain (alpha-macroglobulins are cleaved much more rapidly). It cleaves the collagen triple helix about three-quarters of the way from the N-terminus, at Gly775-/-Ile in the alpha1(I) chain, and cleaves synthetic substrates and alpha-macroglobulins at bonds where P1' is a hydrophobic residue. In connective tissue it initiates collagen fibril breakdown. It features an M10-family zinc catalytic domain with a hemopexin-like domain.
Interstitial collagenase is a secreted zinc metalloendopeptidase, the type example of peptidase family M10, widely distributed in vertebrates and named for its substrates types I, II and III interstitial collagens, all cleaved in the helical domain (alpha-macroglobulins are cleaved much more rapidly). It cleaves the collagen triple helix about three-quarters of the way from the N-terminus, at Gly775-/-Ile in the alpha1(I) chain, and cleaves synthetic substrates and alpha-macroglobulins at bonds where P1' is a hydrophobic residue. In connective tissue it initiates collagen fibril breakdown. It features an M10-family zinc catalytic domain with a hemopexin-like domain.
References:
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