EC Number   |
General Information |
Reference |
|---|
   3.4.11.21 | evolution |
enzyme AAP belongs to the M18 family of peptidases |
-, 755445 |
| 3.4.11.21 | evolution |
the enzyme belongs to the M18 family of proteases |
752973, 753110 |
| 3.4.11.21 | malfunction |
a Cryptococcus neoformans ape4 knockout mutant does not grow at 37°C, and also has defects in the expression of important virulence factors such as phospholipase production and capsule formation. The ape4 mutants are sensitive to high temperature growth. ape4 Mutation affects multiple virulence factors in Cryptococcus neoformans |
-, 755145 |
| 3.4.11.21 | malfunction |
TgAAP knockout inhibits the attachment/invasion, replication, and substrate-specific activity in Toxoplasma gondii. TgAAP knockout affects the growth of Toxoplasma gondii but does not completely abolish parasite replication and growth |
-, 755445 |
| 3.4.11.21 | more |
enzyme structure homology modelling, molecular dynamics simulation, secondary structure, acidic residues and hydrophobicity of interior residues demonstrate that aspartyl aminopeptidase has a greater stability than non-salttolerant protease in high salinity. Higher contents of ordered secondary structures, more salt bridges between hydrated surface acidic residues and specific basic residues, and stronger hydrophobicity of interior residues are the salt-tolerance mechanisms of aspartyl aminopeptidase |
-, 753626 |
| 3.4.11.21 | physiological function |
a small portion localizes in the vacuole, but its vacuolar transport is accelerated by nutrient starvation, and it stably resides in the vacuole lumen, it is proposed that cytosolic enzyme is redistributed to the vacuole when yeast cells need more active vacuolar degradation |
717822 |
| 3.4.11.21 | physiological function |
aspartyl aminopeptidase immunoprecipitates with beta-actin and tubulin, suggesting a role in cytoskeletal maintenance. Enzyme is not present in the urine of healthy rats, however, it is readily detected in the urine in rat models of mild and heavy proteinuria. Urinary levels correlate with the severity of proteinuria |
731109 |
| 3.4.11.21 | physiological function |
aspartyl aminopeptidase interacts with ClC-5, a chloride/proton exchanger that plays an obligate role in albumin uptake by the renal proximal tubule. ClC-5 forms an endocytic complex with the albumin receptor megalin/cubilin. Aspartyl aminopeptidase and ClC-5 associate in cells. The two proteins bind directly to each other. Overexpression of wild-type aspartyl aminopeptidase increases cell-surface levels of ClC-5 and albumin uptake. Overexpression results in significant decrease in the amount of G actin, suggesting a role for aspartyl aminopeptidase in stabilizing the cytoskeleton |
731109 |
| 3.4.11.21 | physiological function |
aspartyl aminopeptidase is a moonlight protein that has aspartyl aminopeptidase and chaperone activities |
707859 |
| 3.4.11.21 | physiological function |
Cryptococcus neoformans Ape4 activity is required by facultative intracellular pathogen to survive within macrophages, as well as for virulence in an animal model of cryptococcal infection. The enzyme is involved in autophagy. Cryptococcus neoformans autophagy-related genes are modulated during nitrogen starvation and thermal stress, overview The APE4 gene is involved in multi-stress resistance, aspartyl aminopeptidase encoded by APE4 is important during response to osmotic/salt stress |
-, 755145 |
