Dipeptidyl-peptidase I
| Dipeptidyl peptidase I | |||||||||
|---|---|---|---|---|---|---|---|---|---|
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Cathepsin C, heterododekamer, Human | |||||||||
| Identifiers | |||||||||
| EC number | 3.4.14.1 | ||||||||
| CAS number | 9032-68-2 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Dipeptidyl peptidase I (EC 3.4.14.1, cathepsin C, dipeptidyl aminopeptidase I, dipeptidyl transferase, dipeptide arylamidase I, DAP I) is an enzyme.[1][2][3][4] This enzyme catalyses the following chemical reaction
- Release of an N-terminal dipeptide, Xaa-Yaa!Zaa-, except when Xaa is Arg or Lys, or Yaa or Zaa is Pro
This Cl-dependent, lysosomal cysteine-type peptidase is maximally active at acidic pH.
References
- ↑ Planta, R.J.; Gorter, J.; Gruber, M. (1964). "The catalytic properties of cathepsin C". Biochim. Biophys. Acta. 89: 511–519. doi:10.1016/0926-6569(64)90077-x. PMID 14209333.
- ↑ Metrione, R.M.; Neves, A.G.; Fruton, J.S. (1966). "Purification and properties of dipeptidyl transferase (cathepsin C)". Biochemistry. 5: 1597–1604. doi:10.1021/bi00869a021. PMID 5961281.
- ↑ McDonald, J.K.; Zeitman, B.B.; Reilly, T.J.; Ellis, S. (1969). "New observations on the substrate specificity of cathepsin C (dipeptidyl aminopeptidase I) including the degradation of β-corticotropin and other peptide hormones". J. Biol. Chem. 244: 2693–2709. PMID 4306035.
- ↑ McDonald, J.K.; Schwabe, C. (1977). "Intracellular exopeptidases". In Barrett, A.J. Proteinases in Mammalian Cells and Tissues. Amsterdam: North-Holland Publishing Co. pp. 311–391.
External links
- Dipeptidyl peptidase I at the US National Library of Medicine Medical Subject Headings (MeSH)
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