Prolyl aminopeptidase (EC 3.4.11.5, proline aminopeptidase, Pro-X aminopeptidase, cytosol aminopeptidase V, proline iminopeptidase) is an enzyme.[1][2][3] This enzyme catalyses the following chemical reaction
| Prolyl aminopeptidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.4.11.5 | ||||||||
| CAS no. | 9025-40-5 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
This enzyme requires Mn2+ ion to function.
References
edit- ^ Sarid S, Berger A, Katchalski E (July 1962). "Proline iminopeptidase. II. Purification and comparison with iminodipeptidase (prolinase)". The Journal of Biological Chemistry. 237 (7): 2207–12. doi:10.1016/S0021-9258(19)63420-4. PMID 14497218.
- ^ Nordwig A, Mayer H (April 1973). "The cleavage of prolyl peptides by kidney peptidases. Detection of a new peptidase capable of removing N-terminal proline". Hoppe-Seyler's Zeitschrift für Physiologische Chemie. 354 (4): 380–3. doi:10.1515/bchm2.1973.354.1.380. PMID 4803482.
- ^ Turzynski A, Mentlein R (July 1990). "Prolyl aminopeptidase from rat brain and kidney. Action on peptides and identification as leucyl aminopeptidase". European Journal of Biochemistry. 190 (3): 509–15. doi:10.1111/j.1432-1033.1990.tb15603.x. PMID 2373079.
External links
edit- Prolyl+aminopeptidase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
