CATH Classification
Level | CATH Code | Description |
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2 | Mainly Beta |
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2.130 | 7 Propeller |
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2.130.10 | Methylamine Dehydrogenase; Chain H |
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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.
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UniProtKB Entries (1)
Q9YBQ2 |
APEH_AERPE
Aeropyrum pernix K1
Acylamino-acid-releasing enzyme
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PDB Structure
PDB | 4RE6 |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | |
Primary Citation |
Catalytically distinct states captured in a crystal lattice: the substrate-bound and scavenger states of acylaminoacyl peptidase and their implications for functionality.
Acta Crystallogr.,Sect.D
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