EC Number   |
General Information |
Reference  |
|---|
   3.4.19.1 | malfunction |
transgenic overexpression of APH results in crystallin cleavage, impaired lens development, and cataract |
732175 |
| 3.4.19.1 | physiological function |
APH is involved in the generation of peptides that have the potential to induce protein aggregation |
732175 |
| 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 |
732661 |
| 3.4.19.1 | malfunction |
the AtAARE-suppressed plants using RNAi became susceptible to oxidative stress corresponding to enhanced accumulation of oxidized proteins |
732661 |
| 3.4.19.1 | physiological function |
AtAARE contributes to eliminate oxidized proteins to sustain the antioxidant system in the cytoplasm |
732661 |
| 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 |
745261 |
| 3.4.19.1 | evolution |
acylaminoacyl peptidase is a member of the prolyl oligopeptidase protein family |
-, 752387 |
| 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 | evolution |
the enzyme belongs to a serine peptidase family |
-, 752584 |
| 3.4.19.1 | more |
enzyme structure modeling and comparison with the enzyme structure from Aeropyrum pernix, overview. Both enzymes share a high structural homology |
-, 752694 |
