| EC |
3.4.22.15 |
| Accepted name: |
cathepsin L |
| Reaction: |
Similar to that of papain. As compared to cathepsin B, cathepsin L exhibits higher activity towards protein substrates, but has little activity on Z-Arg-Arg-NHMec, and no peptidyl-dipeptidase activity |
| Other name(s): |
Aldrichina grahami cysteine proteinase |
| Comments: |
A lysosomal enzyme in peptidase family C1 (papain family) that is readily inhibited by the diazomethane inhibitor Z-Phe-Phe-CHN2 or the epoxide inhibitor E-64 |
| Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 60616-82-2 |
| References: |
| 1. |
Barrett, A.J. and Kirschke, H. Cathepsin B, cathepsin H and cathepsin L. Methods Enzymol. 80 (1981) 535–561. [PMID: 7043200] |
| 2. |
Barrett, A.J., Buttle, D.J. and Mason, R.W. Lysosomal cysteine proteinases. ISI Atlas of Science. Biochemistry 1 (1988) 256–260. |
| 3. |
Joseph, L.J., Chang, L.C., Stamenkovich, D. and Sukhatme, V.P. Complete nucleotide and deduced amino acid sequences of human and murine preprocathepsin L. An abundant transcript induced by transformation of fibroblasts. J. Clin. Invest. 81 (1988) 1621–1629. [DOI] [PMID: 2835398] |
| 4. |
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 3.4.22.15 created 1978 (EC 3.4.99.19 created 1972, incorporated 1981)] |
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