3.4.19.1	evolution	acylaminoacyl peptidase is a member of the prolyl oligopeptidase protein family	
3.4.19.1	evolution	enzyme AAP belongs to alpha/beta-hydrolase enzyme superfamily	
3.4.19.1	evolution	the enzyme belongs to a class of serine-type protease belonging to the prolyl oligopeptidase (POP) family. The members of the POP family are involved in numerous metabolic processes	
3.4.19.1	evolution	the enzyme belongs to a serine peptidase family	
3.4.19.1	evolution	the enzyme belongs to the prolyl oligopeptidase family of serine proteases	
3.4.19.1	malfunction	overexpression of AARE/OPH exhibits no apparent effect on the level of oxidized proteins because wild types have inherently high AARE/OPH activity	
3.4.19.1	malfunction	the AtAARE-suppressed plants using RNAi became susceptible to oxidative stress corresponding to enhanced accumulation of oxidized proteins	
3.4.19.1	malfunction	transgenic overexpression of APH results in crystallin cleavage, impaired lens development, and cataract	
3.4.19.1	metabolism	the existence of the acylamino acid-releasing enzyme in archaea suggests that the mechanisms of protein degradation or initiation of protein synthesis or both in archaea may be similar to those in eukaryotes	
3.4.19.1	additional information	enzyme structure modeling and comparison with the enzyme structure from Aeropyrum pernix, overview. Both enzymes share a high structural homology	
3.4.19.1	additional information	enzyme structure modeling and comparison with the enzyme structure from Sulfurisphaera tokodaii, overview. Both enzymes share a high structural homology	
3.4.19.1	additional information	exploration of the chlorpyrifos escape pathway from acylpeptide hydrolases using steered molecular dynamics simulations, overview	
3.4.19.1	additional information	molecular docking and molecular dynamics simulations using the structure with PDB ID 1VE7, substrate binding structures, overview	
3.4.19.1	additional information	substrate binding structures of wild-type and mutant enzymes, docking study and molecular dynamics simulations, overview. Molecular mechanics/Poisson-Boltzmann surface area (MM/PBSA) calculations	
3.4.19.1	additional information	substrate binding structures of wild-type and mutant R526V enzymes, docking study and molecular dynamics simulations, overview. Molecular mechanics/Poisson-Boltzmann surface area (MM/PBSA) calculations	
3.4.19.1	additional information	the catalytic triad is composed by catalytic residues Ser566, Asp654, and His686	
3.4.19.1	additional information	the closed form of the enzyme is catalytically active, while opening deactivates the catalytic triad. Molecular-dynamics simulations are used to investigate the structure of the complexes formed with longer peptide substrates showing that their binding within the large crevice of the closed form of ApAAP leaves the enzyme structure unperturbed. Their accessing the binding site seems more probable when assisted by opening of the enzyme. Thus, the open form of ApAAP corresponds to a scavenger of possible substrates, the actual cleavage of which only takes place if the enzyme is able to re-close. Structure analysis, detailed overview	
3.4.19.1	additional information	the three-dimensional structure of the psychrophilic acyl aminoacyl peptidase from Sporosarcina psychrophila (SpAAP) highlights adaptive molecular changes resulting in a fine-tuned trade-off between flexibility and stability. A feature of SpAAP cold adaptation is the enlargement of the tunnel connecting the exterior of the protein with the active site. Such a wide channel might compensate for the reduced molecular motions occurring in the cold and allow easy and direct access of substrates to the catalytic site, rendering transient movements between domains unnecessary. Thus, cold-adapted SpAAP has developed a molecular strategy unique within this group of proteins: it is able to enhance the flexibility of each functional unit while still preserving sufficient stability. The Ser-Asp-His catalytic triad in SpAAP (Ser458, Asp540 and His572) matches that of the canonical alpha/beta hydrolase fold	
3.4.19.1	physiological function	APH is involved in the generation of peptides that have the potential to induce protein aggregation	
3.4.19.1	physiological function	AtAARE contributes to eliminate oxidized proteins to sustain the antioxidant system in the cytoplasm	
3.4.19.1	physiological function	acylpeptide hydrolases (APHs) catalyze the removal of N-acylated amino acids from blocked peptides	
3.4.19.1	physiological function	enzyme APEH is a component of the cellular response to DNA damage. APEH is primarily localised in the cytoplasm, but a subfraction of the enzyme is sequestered at sites of nuclear damage following UVA irradiation or following oxidative stress. Localization of APEH at sites of nuclear damage is mediated by direct interaction with XRCC1, a scaffold protein that accelerates the repair of DNA single-strand breaks. APEH interacts with the amino-terminal domain of XRCC1, and APEH facilitates both single-strand break repair and cell survival following exposure to H2O2 in human cells	
3.4.19.1	physiological function	enzyme BmAPHmay be involved in enhancing silkworm tolerance to organophosphorus (OP) insecticides