ENZYME entry: EC 3.4.19.1
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 |
BRENDA | 3.4.19.1 |
EC2PDB | 3.4.19.1 |
ExplorEnz | 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 |
Rhea expert-curated reactions | 3.4.19.1 |
UniProtKB/Swiss-Prot |
Q0IXP9, AARE1_ORYSJ; | Q338C0, AARE2_ORYSJ; | Q84LM4, AARE_ARATH; |
P80227, ACPH_BOVIN; | P13798, ACPH_HUMAN; | P19205, ACPH_PIG; |
P25154, ACPH_RABIT; | P13676, ACPH_RAT; | Q9YBQ2, APEH_AERPE; |
Q8R146, APEH_MOUSE; |
|
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