Biology:Cathepsin X

From HandWiki
Cathepsin X
Identifiers
EC number3.4.18.1
CAS number37217-21-3
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum

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 cysteine cathepsin, a lysosomal cysteine peptidase of family C1 (papain family).

See also

References

  1. "Human cathepsin X: A cysteine protease with unique carboxypeptidase activity". Biochemistry 38 (39): 12648–54. September 1999. doi:10.1021/bi991371z. PMID 10504234. 
  2. "Human cathepsin X: a novel cysteine protease of the papain family with a very short proregion and unique insertions". FEBS Letters 434 (1–2): 135–9. August 1998. doi:10.1016/S0014-5793(98)00964-8. PMID 9738465. 
  3. "Cathepsin Z, a novel human cysteine proteinase with a short propeptide domain and a unique chromosomal location". The Journal of Biological Chemistry 273 (27): 16816–23. July 1998. doi:10.1074/jbc.273.27.16816. PMID 9642240. 
  4. "On the substrate specificity of cathepsins B1 and B2 including a new fluorogenic substrate for cathepsin B1". Life Sciences 17 (8): 1269–76. October 1975. doi:10.1016/0024-3205(75)90137-x. PMID 577. 
  5. "Improved purification of cathepsin B1 and cathepsin B2". Biochimica et Biophysica Acta (BBA) - Protein Structure 379 (2): 462–75. February 1975. doi:10.1016/0005-2795(75)90153-1. PMID 1122298. 
  6. "Purification and characterization of rat liver lysosomal cathepsin B2". Biochimica et Biophysica Acta (BBA) - Enzymology 370 (1): 308–21. November 1974. doi:10.1016/0005-2744(74)90055-2. PMID 4429705. 

External links