The Enzyme Database

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Accepted name: cathepsin B
Reaction: 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
Other name(s): cathepsin B1 (obsolete); cathepsin II
Comments: An intracellular (lysosomal) enzyme in peptidase family C1 (papain family)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 9047-22-7
1.  Bond, J.S. and Barrett, A.J. Degradation of fructose-1,6-bisphosphate aldolase by cathepsin B. A further example of peptidyldipeptidase activity of this proteinase. Biochem. J. 189 (1980) 17–25. [PMID: 7458901]
2.  Barrett, A.J. and Kirschke, H. Cathepsin B, cathepsin H and cathepsin L. Methods Enzymol. 80 (1981) 535–561. [PMID: 7043200]
3.  Polgár, L. and Csoma, C. Dissociation of ionizing groups in the binding cleft inversely controls the endo- and exopeptidase activities of cathepsin B. J. Biol. Chem. 262 (1987) 14448–14453. [PMID: 3312190]
4.  Barrett, A.J., Buttle, D.J. and Mason, R.W. Lysosomal cysteine proteinases. ISI Atlas of Science. Biochemistry 1 (1988) 256–260.
5.  Kirschke, H., Wikstrom, P. and Shaw, E. Active center differences between cathepsins L and B: the S1 binding region. FEBS Lett. 228 (1988) 128–130. [DOI] [PMID: 3342870]
[EC created 1972]

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