EC Number   |
General Information  |
Reference |
|---|
   3.4.19.1 | more |
enzyme structure modeling and comparison with the enzyme structure from Sulfurisphaera tokodaii, overview. Both enzymes share a high structural homology |
-, 752694 |
| 3.4.19.1 | more |
exploration of the chlorpyrifos escape pathway from acylpeptide hydrolases using steered molecular dynamics simulations, overview |
754196 |
| 3.4.19.1 | more |
molecular docking and molecular dynamics simulations using the structure with PDB ID 1VE7, substrate binding structures, overview |
755379 |
| 3.4.19.1 | more |
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 |
-, 754201 |
| 3.4.19.1 | more |
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 |
754201 |
| 3.4.19.1 | more |
the catalytic triad is composed by catalytic residues Ser566, Asp654, and His686 |
753727 |
| 3.4.19.1 | more |
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 |
-, 752387 |
| 3.4.19.1 | more |
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 |
753553 |
| 3.4.19.1 | physiological function |
acylpeptide hydrolases (APHs) catalyze the removal of N-acylated amino acids from blocked peptides |
753902 |
| 3.4.19.1 | physiological function |
APH is involved in the generation of peptides that have the potential to induce protein aggregation |
732175 |
