EC |
3.4.22.1 |
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, Gene, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 9047-22-7 |
References: |
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] |
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[EC 3.4.22.1 created 1972] |
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