| Cathepsin X | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.4.18.1 | ||||||||
| CAS no. | 37217-21-3 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB 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).
- ^ 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.
- ^ 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.
- ^ 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.
- ^ 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.
- ^ 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.
- ^ 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.
- Cathepsin+X at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
| Cathepsin X | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.4.18.1 | ||||||||
| CAS no. | 37217-21-3 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB 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).
- ^ 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.
- ^ 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.
- ^ 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.
- ^ 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.
- ^ 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.
- ^ 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.
- Cathepsin+X at the U.S. National Library of Medicine Medical Subject Headings (MeSH)