CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
2 | Mainly Beta |
|
2.130 | 7 Propeller |
|
2.130.10 | Methylamine Dehydrogenase; Chain H |
|
2.130.10.150 | Peptidase/esterase 'gauge' domain |
Domain Context
CATH Clusters
| Superfamily | Peptidase/esterase 'gauge' domain |
| 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 | 2QR5 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Structural and kinetic contributions of the oxyanion binding site to the catalytic activity of acylaminoacyl peptidase
J.Struct.Biol.
|