_EC 3.4.19.1 Acylaminoacyl-peptidase. 11 PDB entries  
EC 3.-.-.- Hydrolases. [21,051 PDB entries]
EC 3.4.-.- Acting on peptide bonds (peptide hydrolases). [6,852 PDB entries]
EC 3.4.19.- Omega peptidases. [377 PDB entries]
EC 3.4.19.1 Acylaminoacyl-peptidase. [11 PDB entries]    
1ve6

Reaction: Cleavage of an N-acetyl or N-formyl amino acid from the N-terminus of a polypeptide.
 


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Molecule diagrams generated from .mol files obtained from the KEGG ftp site.

Other name(s): Acylamino-acid-releasing enzyme. N-acylpeptide hydrolase.
Comments: 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.
Links:   [IntEnz]   [ExPASy]   [KEGG]  

There are 11 PDB entries in enzyme class E.C.3.4.19.1

  PDB code Protein
1ve6
Crystal structure of an acylpeptide hydrolase/esterase from pernix k1
Source: Aeropyrum pernix. Organism_taxid: 56636. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B (574 residues) CATH domains: 2.130.10.150 3.40.50.1820
1ve7
Crystal structure of an acylpeptide hydrolase/esterase from pernix k1 in complex with p-nitrophenyl phosphate
Source: Aeropyrum pernix. Organism_taxid: 56636. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B (573 residues) CATH domains: 2.130.10.150 3.40.50.1820
2hu5
Binding of inhibitors by acylaminoacyl-peptidase
Source: Aeropyrum pernix. Organism_taxid: 56636. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (573 residues) CATH domains: 2.130.10.150 3.40.50.1820
2hu7
Binding of inhibitors by acylaminoacyl peptidase
Source: Aeropyrum pernix. Organism_taxid: 56636. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (573 residues) CATH domains: 2.130.10.150 3.40.50.1820
2hu8
Binding of inhibitors by acylaminoacyl peptidase
Source: Aeropyrum pernix. Organism_taxid: 56636. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (575 residues) CATH domains: 2.130.10.150 3.40.50.1820
2qr5
Aeropyrum pernix acylaminoacyl peptidase, h367a mutant
Source: Aeropyrum pernix. Archaea. Expressed in: escherichia coli.
Chains: A, B (576 residues) CATH domains: 2.130.10.150 3.40.50.1820
2qzp
Crystal structure of mutation of an acylptide hydrolase/esterase from aeropyrum pernix k1
Source: Aeropyrum pernix. Organism_taxid: 56636. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Chains: A, B (560 residues) CATH domains: 2.130.10.150 3.40.50.1820
3o4g
Structure and catalysis of acylaminoacyl peptidase
Source: Aeropyrum pernix. Organism_taxid: 56636. Gene: ape_1547.1. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B, C, D (577 residues) CATH domains: 2.130.10.150 3.40.50.1820
3o4h
Structure and catalysis of acylaminoacyl peptidase
Source: Aeropyrum pernix. Organism_taxid: 56636. Gene: ape_1547.1. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B, C, D (576 residues) CATH domains: 2.130.10.150 3.40.50.1820
3o4i
Structure and catalysis of acylaminoacyl peptidase
Source: Aeropyrum pernix. Organism_taxid: 56636. Gene: ape_1547.1. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (576 residues) CATH domains: 2.130.10.150 3.40.50.1820
3o4j
Structure and catalysis of acylaminoacyl peptidase
Source: Aeropyrum pernix. Organism_taxid: 56636. Gene: ape_1547.1. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B, C, D (578 residues) CATH domains: 2.130.10.150 3.40.50.1820