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evolution
enzyme AAP belongs to the M18 family of peptidases
evolution
the enzyme belongs to the M18 family of proteases
evolution
the enzyme belongs to the M18 family of proteases
evolution
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enzyme AAP belongs to the M18 family of peptidases
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evolution
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enzyme AAP belongs to the M18 family of peptidases
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evolution
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enzyme AAP belongs to the M18 family of peptidases
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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
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
malfunction
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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
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malfunction
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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
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malfunction
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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
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malfunction
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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
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malfunction
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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
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malfunction
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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
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physiological function
aspartyl aminopeptidase is a moonlight protein that has aspartyl aminopeptidase and chaperone activities
physiological function
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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
physiological function
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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
physiological function
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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
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
physiological function
the enzyme functions at the terminal stage of hemoglobin degradation of host and completes the hydrolysis process. M18AAP is an exopeptidase that digests the N-terminal aspartic and glutamic acid which cannot be degraded by any other aminopeptidase
physiological function
the only aspartyl aminopeptidase in Plasmodium falciparum, PfM18AAP, is essential for the survival of the organism. PfM18AAP enzyme performs various functions in the parasite and the erythrocytic host such as hemoglobin digestion, erythrocyte invasion, parasite growth and parasite escape from the host cell
physiological function
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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
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physiological function
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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
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physiological function
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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
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additional information
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
additional information
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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
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additional information
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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
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additional information
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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
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