Biology:Prolyl aminopeptidase
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Short description: Class of enzymes
| Prolyl aminopeptidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.4.11.5 | ||||||||
| CAS number | 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 | ||||||||
| |||||||||
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
This enzyme requires Mn2+ ion to function.
References
- ↑ "Proline iminopeptidase. II. Purification and comparison with iminodipeptidase (prolinase)". The Journal of Biological Chemistry 237 (7): 2207–12. July 1962. doi:10.1016/S0021-9258(19)63420-4. PMID 14497218.
- ↑ "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. April 1973. doi:10.1515/bchm2.1973.354.1.380. PMID 4803482.
- ↑ "Prolyl aminopeptidase from rat brain and kidney. Action on peptides and identification as leucyl aminopeptidase". European Journal of Biochemistry 190 (3): 509–15. July 1990. doi:10.1111/j.1432-1033.1990.tb15603.x. PMID 2373079.
External links
- Prolyl+aminopeptidase at the US National Library of Medicine Medical Subject Headings (MeSH)
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