| Accepted Name |
|---|
| Acylaminoacyl-peptidase.
|
| Alternative Name(s) |
|---|
| Acylamino-acid-releasing enzyme. |
| N-acylpeptide hydrolase. |
| Reaction catalysed |
|---|
| Cleavage of an N-acetyl or N-formyl amino acid from the N-terminus of a polypeptide |
| Comment(s) |
|---|
- Best if P1 = Ser, Ala, Met; poor if P1 = Gly, Tyr, Asp, Asn or Pro.
- Group of similar enzymes liberating N-acetyl or N-formyl amino acid
from proteins and peptides.
- Active at neutral pH.
- Several variants of this enzyme exist; the human erythrocyte enzyme
is relatively specific for removal of N-acetylalanine from peptides.
- Display dipeptidyl-peptidase activity on glycyl-peptides, perhaps as
a result of misrecognition of the glycyl residue as an uncharged
N-acyl group.
- Inhibited by diisopropyl fluorophosphate.
- Belongs to peptidase family S9C.
- Formerly EC 3.4.14.3.
|
| Cross-references |
|---|
| PROSITE | PDOC00587 |
| BRENDA | 3.4.19.1 |
| EC2PDB | 3.4.19.1 |
| PRIAM enzyme-specific profiles | 3.4.19.1 |
| KEGG Ligand Database for Enzyme Nomenclature | 3.4.19.1 |
| IUBMB Enzyme Nomenclature | 3.4.19.1 |
| IntEnz | 3.4.19.1 |
| MEDLINE | Find literature relating to 3.4.19.1 |
| MetaCyc | 3.4.19.1 |
| UniProtKB/Swiss-Prot |
|
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