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EC Number Reaction Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 3.4.22.1Hydrolysis of proteins with broad specificity for peptide bonds. Preferentially cleaves -Arg-Arg-/- bonds in small molecule substrates (thus differing from cathepsin L). In addition to being an endopeptidase, shows peptidyl-dipeptidase activity, liberating C-terminal dipeptides - -
Display the word mapDisplay the reaction diagram Show all sequences 3.4.22.1Hydrolysis of proteins with broad specificity for peptide bonds. Preferentially cleaves -Arg-Arg-/- bonds in small molecule substrates (thus differing from cathepsin L). In addition to being an endopeptidase, shows peptidyl-dipeptidase activity, liberating C-terminal dipeptides cathepsin B possesses a long and narrow substrate-binding active site cleft with catalytic residue Cys, the surfaces of the S1 and S1' subsites are negatively charged due to presence of Glu122 and Glu194, the occluding loop of residue 105-125 is a structural feature containing the two positively charged His residues, His110 and His111, overview 708258
Display the word mapDisplay the reaction diagram Show all sequences 3.4.22.1Hydrolysis of proteins with broad specificity for peptide bonds. Preferentially cleaves -Arg-Arg-/- bonds in small molecule substrates (thus differing from cathepsin L). In addition to being an endopeptidase, shows peptidyl-dipeptidase activity, liberating C-terminal dipeptides kinetics 650051
Display the word mapDisplay the reaction diagram Show all sequences 3.4.22.1Hydrolysis of proteins with broad specificity for peptide bonds. Preferentially cleaves -Arg-Arg-/- bonds in small molecule substrates (thus differing from cathepsin L). In addition to being an endopeptidase, shows peptidyl-dipeptidase activity, liberating C-terminal dipeptides non-active site residue Gln109 and active site Cys115 play an important role in the catalytic mechanism 699729
Display the word mapDisplay the reaction diagram Show all sequences 3.4.22.1Hydrolysis of proteins with broad specificity for peptide bonds. Preferentially cleaves -Arg-Arg-/- bonds in small molecule substrates (thus differing from cathepsin L). In addition to being an endopeptidase, shows peptidyl-dipeptidase activity, liberating C-terminal dipeptides the catalytic residue is Cys29 708228
Results 1 - 5 of 5
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