| Acylaminoacyl-peptidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.4.19.1 | ||||||||
| CAS no. | 73562-30-8 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Acylaminoacyl-peptidase (EC 3.4.19.1, acylamino-acid-releasing enzyme, N-acylpeptide hydrolase, N-formylmethionine (fMet) aminopeptidase, alpha-N-acylpeptide hydrolase) is an enzyme. This enzyme catalyses the following chemical reaction
- Cleavage of an N-acetyl or N-formyl amino acid from the N-terminus of a polypeptide
This enzyme is active at neutral pH.
References
- Tsunasawa S, Narita K, Ogata K (January 1975). "Purification and properties of acylamino acid-releasing enzyme from rat liver". Journal of Biochemistry. 77 (1?): 89–102. PMID 1137989.
- Unger T, Nagelschmidt M, Struck H (June 1979). "N-Acetylaminoacyl-p-nitranilidase from human placenta. Purification and some properties". European Journal of Biochemistry. 97 (1): 205–11. doi:10.1111/j.1432-1033.1979.tb13104.x. PMID 477668.
- Kobayashi K, Smith JA (August 1987). "Acyl-peptide hydrolase from rat liver. Characterization of enzyme reaction". The Journal of Biological Chemistry. 262 (24): 11435–45. PMID 3305492.
External links
- Acylaminoacyl-peptidase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
| Hydrolase: proteases (EC 3.4) | |||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| 3.4.11-19: Exopeptidase |
| ||||||||||||||
| 3.4.21-25: Endopeptidase | |||||||||||||||
| 3.4.99: Unknown | |||||||||||||||
| Enzymes | |
|---|---|
| Activity | |
| Regulation | |
| Classification | |
| Kinetics | |
| Types |
|
