Cathepsin X
Cathepsin X (EC 3.4.18.1, cathepsin B2, cysteine-type carboxypeptidase, cathepsin IV, cathepsin Z, acid carboxypeptidase, lysosomal carboxypeptidase B) is an enzyme.[1][2][3][4][5][6] This enzyme catalyses the following chemical reaction
- Release of C-terminal amino acid residues with broad specificity, but lacks action on C-terminal proline. Shows weak endopeptidase activity
Cathepsin X is a lysosomal cysteine peptidase of family C1 (papain family).
References
- ↑ Nägler, D.K., Zhang, R., Tam, W., Sulea, T., Purisima, E.O. and Ménard, R. (1999). "Human cathepsin X: A cysteine protease with unique carboxypeptidase activity". Biochemistry 38 (39): 12648–12654. doi:10.1021/bi991371z. PMID 10504234.
- ↑ Nägler, D.K. and Ménard, R. (1998). "Human cathepsin X: A novel cysteine protease of the papain family with a very short proregion and unique insertions". FEBS Lett. 434: 135–139. doi:10.1016/S0014-5793(98)00964-8. PMID 9738465.
- ↑ Santamaría, I. Velasco, G., Pendás, A.M., Fueyo, A. and López-Otín, C. (1998). "Cathepsin Z, a novel human cysteine proteinase with a short propeptide domain and a unique chromosomal location". J. Biol. Chem. 273: 16816–16823. doi:10.1074/jbc.273.27.16816. PMID 9642240.
- ↑ McDonald, J.K. and Ellis, S. (1975). "On the substrate specificity of cathepsins B1 and B2 including a new fluorogenic substrate for cathepsin B1". Life Sci. 17 (8): 1269–1276. doi:10.1016/0024-3205(75)90137-x. PMID 577.
- ↑ Otto, K. and Riesenkönig, H. (1975). "Improved purification of cathepsin B1 and cathepsin B2". Biochim. Biophys. Acta 379 (2): 462–475. doi:10.1016/0005-2795(75)90153-1. PMID 1122298.
- ↑ Ninjoor, V., Taylor, S.L. and Tappel, A.L. (1974). "Purification and characterization of rat liver lysosomal cathepsin B2". Biochim. Biophys. Acta 370 (1): 308–321. doi:10.1016/0005-2744(74)90055-2. PMID 4429705.
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