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, KEGG, MEROPS, Metacyc, 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. [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. [PMID: 3342870]