3.4.11.20: aminopeptidase Ey
This is an abbreviated version!
For detailed information about aminopeptidase Ey, go to the full flat file.
Word Map on EC 3.4.11.20
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3.4.11.20
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plasmodium
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falciparum
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antimalarial
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aminopeptidases
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bestatin
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hemoglobin
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dipeptide
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malarial
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subsite
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metalloaminopeptidases
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yolk
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hydroxamic
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gallus
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leucyl
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exopeptidases
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domesticus
- 3.4.11.20
- plasmodium
- falciparum
-
antimalarial
- aminopeptidases
- bestatin
- hemoglobin
- dipeptide
-
malarial
-
subsite
-
metalloaminopeptidases
- yolk
-
hydroxamic
- gallus
-
leucyl
-
exopeptidases
- domesticus
Reaction
differs from other aminopeptidases in broad specificity for amino acids in the P1 position and the ability to hydrolyse peptides of four or five residues that contain Pro in the P1' position =
Synonyms
aminopeptidase M17, aminopeptidase N, ANPEP, APN1, Leucyl aminopeptidase, M1 aminopeptidase, M1 metalloaminopeptidase, M1-family aminopeptidase, M17 aminopeptidase, M17 leucyl aminopeptidase, malaria M1 metalloaminopeptidase, metallo-aminopeptidase M1, Pf-LAP, PfA-M1, PfA-M1 aminopeptidase, PfA-M17, Xac2987
ECTree
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General Information
General Information on EC 3.4.11.20 - aminopeptidase Ey
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malfunction
physiological function
synthesized as the precursor p120 form, targeted to the parasitophorous vacuole via the parasite endoplasmic reticulum/Golgi, where it is converted into the transient p96 form; p96 form is eventually redirected into the parasite to be converted into the processed p68 form that is only marginally delivered to the parasite foodvacuole
inhibition caused swelling of the parasite digestive vacuole and prevented proteolysis of hemoglobin derived oligopeptides, likely starving the parasite resulting in death
malfunction
inhibition is lethal to parasites early in the life cycle, prior to the onset of hemoglobin degradation