Cathepsin X

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Cathepsin X
Identifiers
EC no.3.4.18.1
CAS no.37217-21-3
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
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NCBIproteins

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. ^ Nägler DK, Zhang R, Tam W, Sulea T, Purisima EO, Ménard R (September 1999). "Human cathepsin X: A cysteine protease with unique carboxypeptidase activity". Biochemistry. 38 (39): 12648–54. doi:10.1021/bi991371z. PMID 10504234.
  2. ^ Nägler DK, Ménard R (August 1998). "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. doi:10.1016/S0014-5793(98)00964-8. PMID 9738465.
  3. ^ Santamaría I, Velasco G, Pendás AM, Fueyo A, López-Otín C (July 1998). "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. doi:10.1074/jbc.273.27.16816. PMID 9642240.
  4. ^ McDonald JK, Ellis S (October 1975). "On the substrate specificity of cathepsins B1 and B2 including a new fluorogenic substrate for cathepsin B1". Life Sciences. 17 (8): 1269–76. doi:10.1016/0024-3205(75)90137-x. PMID 577.
  5. ^ Otto K, Riesenkönig H (February 1975). "Improved purification of cathepsin B1 and cathepsin B2". Biochimica et Biophysica Acta (BBA) - Protein Structure. 379 (2): 462–75. doi:10.1016/0005-2795(75)90153-1. PMID 1122298.
  6. ^ Ninjoor V, Taylor SL, Tappel AL (November 1974). "Purification and characterization of rat liver lysosomal cathepsin B2". Biochimica et Biophysica Acta (BBA) - Enzymology. 370 (1): 308–21. doi:10.1016/0005-2744(74)90055-2. PMID 4429705.

External links