Biology:Cathepsin L
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Revision as of 16:48, 19 May 2022 by imported>Rjetedi (add)
| Cathepsin L | |||||||||
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| Identifiers | |||||||||
| EC number | 3.4.22.15 | ||||||||
| CAS number | 60616-82-2 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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Cathepsin L (EC 3.4.22.15, Aldrichina grahami cysteine proteinase) is an important lysosomal endopeptidase enzyme which is involved in the initiation of protein degradation.[1][2][3][4] It is a member of the Peptidase C1 family, which play an important role in diverse processes including normal lysosome mediated protein turnover, antigen and proprotein processing, and apoptosis.[5] Cathepsin L has been reported in many organisms including fish,[6] birds, mammals, and sponges.[7]
See also
- Cathepsin L1, previously called cathepsin L
- Cathepsin L2 or cathepsin V
References
- ↑ Barrett, A.J.; Kirschke, H. (1981). "Cathepsin B, cathepsin H and cathepsin L". Methods Enzymol. 80: 535–561. doi:10.1016/s0076-6879(81)80043-2. PMID 7043200.
- ↑ Barrett, A.J.; Buttle, D.J.; Mason, R.W. (1988). "Lysosomal cysteine proteinases". ISI Atlas of Science. Biochemistry 1: 256–260.
- ↑ Joseph, L.J.; Chang, L.C.; Stamenkovich, D.; Sukhatme, V.P. (1988). "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: 1621–1629. doi:10.1172/JCI113497. PMID 2835398.
- ↑ Kirschke, H.; Wikstrom, P.; Shaw, E. (1988). "Active center differences between cathepsins L and B: the S1 binding region". FEBS Lett. 228 (1): 128–130. doi:10.1016/0014-5793(88)80600-8. PMID 3342870.
- ↑ Dickinson DP. Cysteine Peptidases of Mammals: Their Biological Roles and Potential Effects in the Oral Cavity and Other Tissues in Health and Disease, CROBM 2002 13: 238.
- ↑ "A murrel cysteine protease, cathepsin L: bioinformatics characterization, gene expression and proteolytic activity". Biologia 39: 395–406. 2014. doi:10.2478/s11756-013-0326-8.
- ↑ Sevenich L, Pennacchio LA, Peters C, Reinheckel T.Human cathepsin L rescues the neurodegeneration and lethality in cathepsin B/L double-deficient mice. Biol Chem. 2006 Jul;387(7):885-91.
External links
- Cathepsin+L at the US National Library of Medicine Medical Subject Headings (MeSH)
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