CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.40 | 3-Layer(aba) Sandwich |
|
3.40.50 | Rossmann fold |
|
3.40.50.1820 | alpha/beta hydrolase |
Domain Context
CATH Clusters
| Superfamily | alpha/beta hydrolase |
| Functional Family |
Enzyme Information
| 3.4.19.1 |
Acylaminoacyl-peptidase.
based on mapping to UniProt Q9YBQ2
Cleavage of an N-acetyl or N-formyl amino acid from the N-terminus of a polypeptide.
-!- 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.
|
UniProtKB Entries (1)
| Q9YBQ2 |
APEH_AERPE
Aeropyrum pernix K1
Acylamino-acid-releasing enzyme
|
PDB Structure
| PDB | 2HU5 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
The Acylaminoacyl Peptidase from Aeropyrum pernix K1 Thought to Be an Exopeptidase Displays Endopeptidase Activity
J.Mol.Biol.
|