Biology:Dipeptidyl-peptidase I
From HandWiki
| Dipeptidyl peptidase I | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 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
- ↑ "The catalytic properties of cathepsin C". Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects 89 (3): 511–9. September 1964. doi:10.1016/0926-6569(64)90077-x. PMID 14209333.
- ↑ "Purification and properties of dipeptidyl transferase (Cathepsin C)". Biochemistry 5 (5): 1597–604. May 1966. doi:10.1021/bi00869a021. PMID 5961281.
- ↑ "New observations on the substrate specificity of cathepsin C (dipeptidyl aminopeptidase I). Including the degradation of beta-corticotropin and other peptide hormones". The Journal of Biological Chemistry 244 (10): 2693–709. May 1969. doi:10.1016/S0021-9258(18)83453-6. 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)
 |  |
