Cathepsin B
Definition:
EC Tree > 3 Hydrolases > 3.4 Acting on peptide bonds (peptidases) > 3.4.22 Cysteine endopeptidases > 3.4.22.1 cathepsin B
Cathepsin B is an intracellular lysosomal cysteine endopeptidase in peptidase family C1 (papain family), found in viruses and cellular organisms. It hydrolyzes proteins with broad specificity for peptide bonds, preferentially cleaving -Arg-Arg-/- bonds in small-molecule substrates, which distinguishes it from cathepsin L. In addition to endopeptidase activity it shows peptidyl-dipeptidase activity, liberating C-terminal dipeptides. In cells it mediates lysosomal protein turnover and, when released, promotes inflammation and cancer invasion. It features a papain-like catalytic cysteine-histidine dyad plus an occluding loop that confers exopeptidase activity.
Cathepsin B is an intracellular lysosomal cysteine endopeptidase in peptidase family C1 (papain family), found in viruses and cellular organisms. It hydrolyzes proteins with broad specificity for peptide bonds, preferentially cleaving -Arg-Arg-/- bonds in small-molecule substrates, which distinguishes it from cathepsin L. In addition to endopeptidase activity it shows peptidyl-dipeptidase activity, liberating C-terminal dipeptides. In cells it mediates lysosomal protein turnover and, when released, promotes inflammation and cancer invasion. It features a papain-like catalytic cysteine-histidine dyad plus an occluding loop that confers exopeptidase activity.
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