EC 220.127.116.11 - Cathepsin B
IntEnz Enzyme Nomenclature
- Hydrolysis 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.
An intracellular (lysosomal) enzyme in peptidase family C1 (papain family).
Links to other databases
Degradation of fructose-1,6-bisphosphate aldolase by cathepsin B. A further example of peptidyldipeptidase activity of this proteinase.Biochem. J. 189: 17-25 (1980). [PMID: 7458901]
Cathepsin B, cathepsin H and cathepsin L.Methods Enzymol. 80C: 535-561 (1981). [PMID: 7043200]
Dissociation of ionizing groups in the binding cleft inversely controls the endo- and exopeptidase activities of cathepsin B.J. Biol. Chem. 262: 14448-14453 (1987). [PMID: 3312190]
Lysosomal cysteine proteinases.ISI Atlas of Science: Biochemistry 1: 256-260 (1988).
Active center differences between cathepsins L and B: the S1 binding region.FEBS Lett. 228: 128-130 (1988). [PMID: 3342870]
[EC 18.104.22.168 created 1972]