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Literature summary for 3.4.11.5 extracted from

  • da Silva, F.L.; Dixon, M.W.; Stack, C.M.; Teuscher, F.; Taran, E.; Jones, M.K.; Lovas, E.; Tilley, L.; Brown, C.L.; Trenholme, K.R.; Dalton, J.P.; Gardiner, D.L.; Skinner-Adams, T.S.
    A Plasmodium falciparum S33 proline aminopeptidase is associated with changes in erythrocyte deformability (2016), Exp. Parasitol., 169, 13-21 .
    View publication on PubMed
Search for more literature for 3.4.11.5

Cloned(Commentary)

Cloned (Comment) Organism
quantitative real-time PCR enzyme expression analysis, recombinant expression of the enzyme in Escherichia coli Plasmodium falciparum

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular enzyme PfPAP contains a predicted protein export element. PfPAP is exported into the host red blood cell, where it locates in the cytoplasm Plasmodium falciparum
-
-

Organism

Organism UniProt Comment Textmining
Plasmodium falciparum Q8IM75
-
-

Source Tissue

Source Tissue Comment Organism Textmining
additional information enzyme PfPAP is transcribed throughout the intraerythrocytic asexual lifecycle and exported into the host red blood cells Plasmodium falciparum
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information PfPAPis a prolyl aminopeptidase with a preference for N-terminal proline substrates Plasmodium falciparum ?
-
 ?
Pro-7-amido-4-methylcoumarin + H2O
-
 Plasmodium falciparum Pro + 7-amino-4-methylcoumarin
-
 ?

Synonyms

Synonyms Comment Organism
Pf S33 proline aminopeptidase
-
 Plasmodium falciparum
PfPAP
-
 Plasmodium falciparum
Plasmodium falciparum S33 proline aminopeptidase
-
 Plasmodium falciparum
Prolyl aminopeptidase
-
 Plasmodium falciparum

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Plasmodium falciparum

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Plasmodium falciparum

General Information

General Information Comment Organism
malfunction enzyme deletion lead to an increase in the deformability of parasite-infected red cells and in reduced adherence to the endothelial cell receptor CD36 under flow conditions Plasmodium falciparum
physiological function the Plasmodium falciparum S33 proline aminopeptidase is an exopeptidase associated with changes in erythrocyte deformability Plasmodium falciparum